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Opsin - Wikipedia

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class="vector-toc-text"> <span class="vector-toc-numb">2</span> <span>Functionally conserved residues and motifs</span> </div> </a> <button aria-controls="toc-Functionally_conserved_residues_and_motifs-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Functionally conserved residues and motifs subsection</span> </button> <ul id="toc-Functionally_conserved_residues_and_motifs-sublist" class="vector-toc-list"> <li id="toc-The_retinal_binding_lysine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#The_retinal_binding_lysine"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>The retinal binding lysine</span> </div> </a> <ul id="toc-The_retinal_binding_lysine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-The_NPxxY_motif" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#The_NPxxY_motif"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>The NPxxY motif</span> </div> </a> <ul id="toc-The_NPxxY_motif-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Other_residues_and_motifs" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Other_residues_and_motifs"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Other residues and motifs</span> </div> </a> <ul id="toc-Other_residues_and_motifs-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Spectral_tuning_sites" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Spectral_tuning_sites"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Spectral tuning sites</span> </div> </a> <ul id="toc-Spectral_tuning_sites-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Opsins_in_the_human_eye,_brain,_and_skin" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Opsins_in_the_human_eye,_brain,_and_skin"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Opsins in the human eye, brain, and skin</span> </div> </a> <ul id="toc-Opsins_in_the_human_eye,_brain,_and_skin-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cuttlefish" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Cuttlefish"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Cuttlefish</span> </div> </a> <ul id="toc-Cuttlefish-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Frogs_(order_Anura)" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Frogs_(order_Anura)"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Frogs (order Anura)</span> </div> </a> <ul id="toc-Frogs_(order_Anura)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Phylogeny" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Phylogeny"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Phylogeny</span> </div> </a> <ul id="toc-Phylogeny-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Ciliary_opsins" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Ciliary_opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Ciliary opsins</span> </div> </a> <button aria-controls="toc-Ciliary_opsins-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Ciliary opsins subsection</span> </button> <ul id="toc-Ciliary_opsins-sublist" class="vector-toc-list"> <li id="toc-Vertebrate_visual_opsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Vertebrate_visual_opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.1</span> <span>Vertebrate visual opsins</span> </div> </a> <ul id="toc-Vertebrate_visual_opsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Extraretinal_(or_extra-ocular)_Rhodopsin-Like_Opsins_(Exo-Rh)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Extraretinal_(or_extra-ocular)_Rhodopsin-Like_Opsins_(Exo-Rh)"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.2</span> <span>Extraretinal (or extra-ocular) Rhodopsin-Like Opsins (Exo-Rh)</span> </div> </a> <ul id="toc-Extraretinal_(or_extra-ocular)_Rhodopsin-Like_Opsins_(Exo-Rh)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Pinopsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Pinopsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.3</span> <span>Pinopsins</span> </div> </a> <ul id="toc-Pinopsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Vertebrate_Ancient_(VA)_opsin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Vertebrate_Ancient_(VA)_opsin"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.4</span> <span>Vertebrate Ancient (VA) opsin</span> </div> </a> <ul id="toc-Vertebrate_Ancient_(VA)_opsin-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Parapinopsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Parapinopsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.5</span> <span>Parapinopsins</span> </div> </a> <ul id="toc-Parapinopsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Parietopsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Parietopsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.6</span> <span>Parietopsins</span> </div> </a> <ul id="toc-Parietopsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Encephalopsin_or_Panopsin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Encephalopsin_or_Panopsin"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.7</span> <span>Encephalopsin or Panopsin</span> </div> </a> <ul id="toc-Encephalopsin_or_Panopsin-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Teleost_Multiple_Tissue_(TMT)_Opsin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Teleost_Multiple_Tissue_(TMT)_Opsin"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.8</span> <span>Teleost Multiple Tissue (TMT) Opsin</span> </div> </a> <ul id="toc-Teleost_Multiple_Tissue_(TMT)_Opsin-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Opsins_in_cnidarians" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Opsins_in_cnidarians"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>Opsins in cnidarians</span> </div> </a> <ul id="toc-Opsins_in_cnidarians-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Rhabdomeric_opsins" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Rhabdomeric_opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>Rhabdomeric opsins</span> </div> </a> <button aria-controls="toc-Rhabdomeric_opsins-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Rhabdomeric opsins subsection</span> </button> <ul id="toc-Rhabdomeric_opsins-sublist" class="vector-toc-list"> <li id="toc-Melanopsin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Melanopsin"> <div class="vector-toc-text"> <span class="vector-toc-numb">10.1</span> <span>Melanopsin</span> </div> </a> <ul id="toc-Melanopsin-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Tetraopsins" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Tetraopsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">11</span> <span>Tetraopsins</span> </div> </a> <button aria-controls="toc-Tetraopsins-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Tetraopsins subsection</span> </button> <ul id="toc-Tetraopsins-sublist" class="vector-toc-list"> <li id="toc-Neuropsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Neuropsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">11.1</span> <span>Neuropsins</span> </div> </a> <ul id="toc-Neuropsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Go-opsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Go-opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">11.2</span> <span>Go-opsins</span> </div> </a> <ul id="toc-Go-opsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-RGR-opsins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#RGR-opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">11.3</span> <span>RGR-opsins</span> </div> </a> <ul id="toc-RGR-opsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Peropsin" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Peropsin"> <div class="vector-toc-text"> <span class="vector-toc-numb">11.4</span> <span>Peropsin</span> </div> </a> <ul id="toc-Peropsin-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Other_proteins_called_opsins" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Other_proteins_called_opsins"> <div class="vector-toc-text"> <span class="vector-toc-numb">12</span> <span>Other proteins called opsins</span> </div> </a> <ul id="toc-Other_proteins_called_opsins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">13</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">14</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">15</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> 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contents</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Opsin</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 22 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-22" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">22 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%A3%D9%88%D8%A8%D8%B3%D9%8A%D9%86" title="أوبسين – Arabic" lang="ar" hreflang="ar" data-title="أوبسين" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Opsina" title="Opsina – Catalan" lang="ca" hreflang="ca" data-title="Opsina" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Opsin" title="Opsin – German" lang="de" hreflang="de" data-title="Opsin" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Opsina" title="Opsina – Spanish" lang="es" hreflang="es" data-title="Opsina" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%A7%D9%BE%D8%B3%DB%8C%D9%86" title="اپسین – Persian" lang="fa" hreflang="fa" data-title="اپسین" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Opsine" title="Opsine – French" lang="fr" hreflang="fr" data-title="Opsine" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Opsina" title="Opsina – Galician" lang="gl" hreflang="gl" data-title="Opsina" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EC%98%B5%EC%8B%A0" title="옵신 – Korean" lang="ko" hreflang="ko" data-title="옵신" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Opsin" title="Opsin – Indonesian" lang="id" hreflang="id" data-title="Opsin" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Opsina" title="Opsina – Italian" lang="it" hreflang="it" data-title="Opsina" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%90%D7%95%D7%A4%D7%A1%D7%99%D7%9F" title="אופסין – Hebrew" lang="he" hreflang="he" data-title="אופסין" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Opsine" title="Opsine – Dutch" lang="nl" hreflang="nl" data-title="Opsine" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%AA%E3%83%97%E3%82%B7%E3%83%B3" title="オプシン – Japanese" lang="ja" hreflang="ja" data-title="オプシン" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Opsyny" title="Opsyny – Polish" lang="pl" hreflang="pl" data-title="Opsyny" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Opsina" title="Opsina – Portuguese" lang="pt" hreflang="pt" data-title="Opsina" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%9E%D0%BF%D1%81%D0%B8%D0%BD" title="Опсин – Russian" lang="ru" hreflang="ru" data-title="Опсин" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-simple mw-list-item"><a href="https://simple.wikipedia.org/wiki/Opsin" title="Opsin – Simple English" lang="en-simple" hreflang="en-simple" data-title="Opsin" data-language-autonym="Simple English" data-language-local-name="Simple English" class="interlanguage-link-target"><span>Simple English</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Opsin" title="Opsin – Serbian" lang="sr" hreflang="sr" data-title="Opsin" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Opsin" title="Opsin – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Opsin" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Opsiinit" title="Opsiinit – Finnish" lang="fi" hreflang="fi" data-title="Opsiinit" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Opsin" title="Opsin – Turkish" lang="tr" hreflang="tr" data-title="Opsin" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E8%A7%86%E8%9B%8B%E7%99%BD" title="视蛋白 – Chinese" lang="zh" hreflang="zh" data-title="视蛋白" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q24785022#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></span></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div 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class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Class of light-sensitive proteins</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">This article is about animal opsins. For microbial opsins, see <a href="/wiki/Microbial_rhodopsin" title="Microbial rhodopsin">microbial rhodopsin</a>.</div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Rhodopsin_3D.jpeg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/84/Rhodopsin_3D.jpeg/150px-Rhodopsin_3D.jpeg" decoding="async" width="150" height="233" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/84/Rhodopsin_3D.jpeg/225px-Rhodopsin_3D.jpeg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/84/Rhodopsin_3D.jpeg/300px-Rhodopsin_3D.jpeg 2x" data-file-width="445" data-file-height="690" /></a><figcaption>Three-dimensional structure of cattle rhodopsin. The seven transmembrane domains are shown in varying colors. The <a href="/wiki/Chromophore" title="Chromophore">chromophore</a> is shown in red.</figcaption></figure> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:1415_Retinal_Isomers.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/f8/1415_Retinal_Isomers.jpg/400px-1415_Retinal_Isomers.jpg" decoding="async" width="400" height="378" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/f8/1415_Retinal_Isomers.jpg/600px-1415_Retinal_Isomers.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/f8/1415_Retinal_Isomers.jpg/800px-1415_Retinal_Isomers.jpg 2x" data-file-width="2237" data-file-height="2112" /></a><figcaption>The retinal molecule inside an opsin protein absorbs a photon of light. Absorption of the photon causes retinal to change from its 11-cis-retinal isomer into its all-trans-retinal isomer. This change in shape of retinal pushes against the outer opsin protein to begin a signal cascade, which may eventually result in chemical signaling being sent to the brain as visual perception. The retinal is re-loaded by the body so that signaling can happen again.</figcaption></figure> <p><b>Animal opsins</b> are <a href="/wiki/G-protein-coupled_receptor" class="mw-redirect" title="G-protein-coupled receptor">G-protein-coupled receptors</a> and a group of proteins made light-sensitive via a <a href="/wiki/Chromophore" title="Chromophore">chromophore</a>, typically <a href="/wiki/Retinal" title="Retinal">retinal</a>. When bound to retinal, opsins become <a href="/wiki/Retinylidene_protein" title="Retinylidene protein">retinylidene proteins</a>, but are usually still called opsins regardless. Most prominently, they are found in <a href="/wiki/Photoreceptor_cell" title="Photoreceptor cell">photoreceptor cells</a> of the <a href="/wiki/Retina" title="Retina">retina</a>. Five classical groups of opsins are involved in <a href="/wiki/Visual_perception" title="Visual perception">vision</a>, mediating the conversion of a <a href="/wiki/Photon" title="Photon">photon</a> of light into an electrochemical signal, the first step in the <a href="/wiki/Visual_phototransduction" title="Visual phototransduction">visual transduction cascade</a>. Another opsin found in the mammalian retina, <a href="/wiki/Melanopsin" title="Melanopsin">melanopsin</a>, is involved in <a href="/wiki/Circadian_rhythm" title="Circadian rhythm">circadian rhythms</a> and <a href="/wiki/Pupillary_light_reflex" title="Pupillary light reflex">pupillary reflex</a> but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense <a href="/wiki/Temperature" title="Temperature">temperature</a>, <a href="/wiki/Sound" title="Sound">sound</a>, or <a href="/wiki/Chemical" class="mw-redirect" title="Chemical">chemicals</a>. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Structure_and_function">Structure and function</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=1" title="Edit section: Structure and function"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Animal opsins detect light and are the molecules that allow us to see. Opsins are <a href="/wiki/G-protein-coupled_receptor" class="mw-redirect" title="G-protein-coupled receptor">G-protein-coupled receptors</a> (GPCRs),<sup id="cite_ref-Casey1988_1-0" class="reference"><a href="#cite_note-Casey1988-1"><span class="cite-bracket">&#91;</span>1<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Attwood1994_2-0" class="reference"><a href="#cite_note-Attwood1994-2"><span class="cite-bracket">&#91;</span>2<span class="cite-bracket">&#93;</span></a></sup> which are <a href="/wiki/Chemoreceptor" title="Chemoreceptor">chemoreceptors</a> and have seven transmembrane <a href="/wiki/Alpha_helix" title="Alpha helix">domains</a> forming a <a href="/wiki/Binding_pocket" class="mw-redirect" title="Binding pocket">binding pocket</a> for a ligand.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">&#91;</span>3<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">&#91;</span>4<span class="cite-bracket">&#93;</span></a></sup> The <a href="/wiki/Ligand" title="Ligand">ligand</a> for opsins is the <a href="/wiki/Vitamin_A" title="Vitamin A">vitamin A</a>-based <a href="/wiki/Chromophore" title="Chromophore">chromophore</a> 11-<i>cis</i>-retinal,<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">&#91;</span>6<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">&#91;</span>7<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">&#91;</span>8<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">&#91;</span>9<span class="cite-bracket">&#93;</span></a></sup> which is covalently bound to a <a href="/wiki/Lysine" title="Lysine">lysine</a> residue<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">&#91;</span>10<span class="cite-bracket">&#93;</span></a></sup> in the seventh transmembrane domain<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">&#91;</span>11<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Palczewski2000_12-0" class="reference"><a href="#cite_note-Palczewski2000-12"><span class="cite-bracket">&#91;</span>12<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Murakami2008_13-0" class="reference"><a href="#cite_note-Murakami2008-13"><span class="cite-bracket">&#91;</span>13<span class="cite-bracket">&#93;</span></a></sup> through a <a href="/wiki/Schiff-base" class="mw-redirect" title="Schiff-base">Schiff-base</a>.<sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">&#91;</span>14<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">&#91;</span>15<span class="cite-bracket">&#93;</span></a></sup> However, 11-<i>cis</i>-retinal only blocks the binding pocket and does not activate the opsin. The opsin is only activated when 11-<i>cis</i>-retinal absorbs a <a href="/wiki/Photon" title="Photon">photon</a> of light and <a href="/wiki/Isomerization" title="Isomerization">isomerizes</a> to all-<i>trans</i>-retinal,<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">&#91;</span>16<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">&#91;</span>17<span class="cite-bracket">&#93;</span></a></sup> the receptor activating form,<sup id="cite_ref-Choe2011_18-0" class="reference"><a href="#cite_note-Choe2011-18"><span class="cite-bracket">&#91;</span>18<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Wald1968_19-0" class="reference"><a href="#cite_note-Wald1968-19"><span class="cite-bracket">&#91;</span>19<span class="cite-bracket">&#93;</span></a></sup> causing conformal changes in the opsin,<sup id="cite_ref-Choe2011_18-1" class="reference"><a href="#cite_note-Choe2011-18"><span class="cite-bracket">&#91;</span>18<span class="cite-bracket">&#93;</span></a></sup> which activate a <a href="/wiki/Phototransduction_cascade" class="mw-redirect" title="Phototransduction cascade">phototransduction cascade</a>.<sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">&#91;</span>20<span class="cite-bracket">&#93;</span></a></sup> Thus, a chemoreceptor is converted to a <a href="/wiki/Photoreceptor_protein" title="Photoreceptor protein">light or photo(n)receptor</a>.<sup id="cite_ref-Guehmann2022_21-0" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p><p>In the vertebrate photoreceptor cells, all-<i>trans</i>-retinal is released and replaced by a newly synthesized 11-<i>cis</i>-retinal provided from the retinal epithelial cells. Beside 11-<i><a href="/wiki/Cis-trans_isomerism" class="mw-redirect" title="Cis-trans isomerism">cis</a></i>-retinal (A1), 11-<i>cis</i>-3,4-didehydroretinal (A2) is also found in <a href="/wiki/Vertebrate" title="Vertebrate">vertebrates</a> as ligand such as in freshwater fishes.<sup id="cite_ref-Wald1968_19-1" class="reference"><a href="#cite_note-Wald1968-19"><span class="cite-bracket">&#91;</span>19<span class="cite-bracket">&#93;</span></a></sup> A2-bound opsins have a shifted <i>λ</i><sub>max</sub> and absorption spectrum compared to A1-bound opsins.<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">&#91;</span>22<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Functionally_conserved_residues_and_motifs">Functionally conserved residues and motifs</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=2" title="Edit section: Functionally conserved residues and motifs"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The seven transmembrane α-helical domains in opsins are connected by three extra-cellular and three <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasmic</a> loops. Along the α-helices and the loops, many <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> residues are highly conserved between all opsin groups, indicating that they serve important functions and thus are called <i>functionally conserved residues</i>. Actually, insertions and deletions in the α-helices are very rare and should preferentially occur in the loops. Therefore, different G-protein-coupled receptors have different length and homologous residues may be in different positions. To make such positions comparable between different receptors, Ballesteros and <a href="/w/index.php?title=Harel_Weinstein&amp;action=edit&amp;redlink=1" class="new" title="Harel Weinstein (page does not exist)">Weinstein</a> introduced a common numbering scheme for G-protein-coupled receptors.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">&#91;</span>23<span class="cite-bracket">&#93;</span></a></sup> The number before the period is the number of the transmembrane domain. The number after the period is set arbitrarily to 50 for the most conserved residue in that transmembrane domain among GPCRs known in 1995. For instance in the seventh transmembrane domain, the <a href="/wiki/Proline" title="Proline">proline</a> in the highly conserved NPxxY<sup>7.53</sup> <a href="/wiki/Sequence_motif" title="Sequence motif">motif</a> is Pro<sup>7.50</sup>, the <a href="/wiki/Asparagine" title="Asparagine">asparagine</a> before is then Asp<sup>7.49</sup>, and the <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a> three residues after is then Tyr<sup>7.53</sup>.<sup id="cite_ref-Guehmann2022_21-1" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> Another numbering scheme is based on <a href="/wiki/Cattle" title="Cattle">cattle</a> rhodopsin. Cattle <a href="/wiki/Rhodopsin" title="Rhodopsin">rhodopsin</a> has 348 <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> and is the first opsin whose <a href="/wiki/Protein_primary_structure" title="Protein primary structure">amino acid sequence</a><sup id="cite_ref-Ovchinnikov1982_24-0" class="reference"><a href="#cite_note-Ovchinnikov1982-24"><span class="cite-bracket">&#91;</span>24<span class="cite-bracket">&#93;</span></a></sup> and whose <a href="/wiki/Protein_tertiary_structure" title="Protein tertiary structure">3D-structure</a> were determined.<sup id="cite_ref-Palczewski2000_12-1" class="reference"><a href="#cite_note-Palczewski2000-12"><span class="cite-bracket">&#91;</span>12<span class="cite-bracket">&#93;</span></a></sup> The cattle rhodopsin numbering scheme is widespread in the opsin literature.<sup id="cite_ref-Guehmann2022_21-2" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> Therefore, it is useful to use both schemes. </p> <div class="mw-heading mw-heading3"><h3 id="The_retinal_binding_lysine">The retinal binding lysine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=3" title="Edit section: The retinal binding lysine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Opsins without the retinal binding lysine are not light sensitive.<sup id="cite_ref-Katana2019_25-0" class="reference"><a href="#cite_note-Katana2019-25"><span class="cite-bracket">&#91;</span>25<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Leung2020_26-0" class="reference"><a href="#cite_note-Leung2020-26"><span class="cite-bracket">&#91;</span>26<span class="cite-bracket">&#93;</span></a></sup> In <a href="/wiki/Cattle" title="Cattle">cattle</a> <a href="/wiki/Rhodopsin" title="Rhodopsin">rhodopsin</a>, this lysine is the 296th amino acid<sup id="cite_ref-Palczewski2000_12-2" class="reference"><a href="#cite_note-Palczewski2000-12"><span class="cite-bracket">&#91;</span>12<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ovchinnikov1982_24-1" class="reference"><a href="#cite_note-Ovchinnikov1982-24"><span class="cite-bracket">&#91;</span>24<span class="cite-bracket">&#93;</span></a></sup> and thus according to both numbering schemes Lys296<sup>7.43</sup>. It is well conserved among opsins, so well conserved that sequences without it were not even considered opsins and thus excluded from large scale <a href="/wiki/Computational_phylogenetics" title="Computational phylogenetics">phylogenetic reconstructions</a>.<sup id="cite_ref-PorterBlasic2011_27-0" class="reference"><a href="#cite_note-PorterBlasic2011-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-0" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup> Even so, most opsins have Lys296<sup>7.43</sup>, some have lost it during evolution: In the nemopsins from <a href="/wiki/Nematode" title="Nematode">nematodes</a>, Lys296<sup>7.43</sup> is replaced by <a href="/wiki/Arginine" title="Arginine">Arginine</a>.<sup id="cite_ref-Troemmel_29-0" class="reference"><a href="#cite_note-Troemmel-29"><span class="cite-bracket">&#91;</span>29<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Guehmann2022_21-3" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> In the astropsins from <a href="/wiki/Sea_urchin" title="Sea urchin">sea urchins</a><sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">&#91;</span>30<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Guehmann2022_21-4" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> and in the gluopsins, Lys296<sup>7.43</sup> is replaced by <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a>.<sup id="cite_ref-Guehmann2022_21-5" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> A nemopsin is expressed in chemosensory cells in <i><a href="/wiki/Caenorhabditis_elegans" title="Caenorhabditis elegans">Caenorhabditis elegans</a></i>. Therefore, the nemopsins are thought to be <a href="/wiki/Chemoreceptor" title="Chemoreceptor">chemoreceptors</a>.<sup id="cite_ref-Troemmel_29-1" class="reference"><a href="#cite_note-Troemmel-29"><span class="cite-bracket">&#91;</span>29<span class="cite-bracket">&#93;</span></a></sup> The gluopsins are found in <a href="/wiki/Insect" title="Insect">insects</a> such as <a href="/wiki/Beetle" title="Beetle">beetles</a>, <a href="/wiki/Scorpionfly" class="mw-redirect" title="Scorpionfly">scorpionflies</a>, <a href="/wiki/Dragonfly" title="Dragonfly">dragonflies</a>, and <a href="/wiki/Butterfly" title="Butterfly">butterflies</a> and <a href="/wiki/Moth" title="Moth">moths</a> including <a href="/wiki/Model_organism" title="Model organism">model organisms</a> such as the <a href="/wiki/Bombyx_mori" title="Bombyx mori">silk moth</a> and the <a href="/wiki/Tobacco_hawk_moth" class="mw-redirect" title="Tobacco hawk moth">tobacco hawk moth</a>. However, the gluopsins have no known function.<sup id="cite_ref-Guehmann2022_21-6" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p><p>Such function does not need to be light detection, as some opsins are also involved in <a href="/wiki/Thermosensation" class="mw-redirect" title="Thermosensation">thermosensation</a>,<sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">&#91;</span>31<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Mechanoreception" class="mw-redirect" title="Mechanoreception">mechanoreception</a> such as <a href="/wiki/Hearing" title="Hearing">hearing</a><sup id="cite_ref-32" class="reference"><a href="#cite_note-32"><span class="cite-bracket">&#91;</span>32<span class="cite-bracket">&#93;</span></a></sup> detecting <a href="/wiki/Phospholipid" title="Phospholipid">phospholipids</a>, <a href="/wiki/Chemoreceptor" title="Chemoreceptor">chemosensation</a>, and other functions.<sup id="cite_ref-Feuda2022_33-0" class="reference"><a href="#cite_note-Feuda2022-33"><span class="cite-bracket">&#91;</span>33<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Leung2017_34-0" class="reference"><a href="#cite_note-Leung2017-34"><span class="cite-bracket">&#91;</span>34<span class="cite-bracket">&#93;</span></a></sup> In particular, the <a href="/wiki/Drosophila_melanogaster" title="Drosophila melanogaster">Drosophila</a> rhabdomeric opsins (rhabopsins, r-opsins) Rh1, Rh4, and Rh7 function not only as photoreceptors, but also as chemoreceptors for <a href="/wiki/Aristolochic_acid" title="Aristolochic acid">aristolochic acid</a>. These opsins still have Lys296<sup>7.43</sup> like other opsins. However, if this lysine is replaced by an arginine in Rh1, then Rh1 loses light sensitivity but still responds to aristolochic acid. Thus, Lys296<sup>7.43</sup> is not needed for Rh1 to function as chemoreceptor.<sup id="cite_ref-Leung2020_26-1" class="reference"><a href="#cite_note-Leung2020-26"><span class="cite-bracket">&#91;</span>26<span class="cite-bracket">&#93;</span></a></sup> Also the Drosophila rhabopsins Rh1 and Rh6 are involved in mechanoreception, again for mechanoreception Lys296<sup>7.43</sup> is not needed, but needed for proper function in the photoreceptor cells.<sup id="cite_ref-Katana2019_25-1" class="reference"><a href="#cite_note-Katana2019-25"><span class="cite-bracket">&#91;</span>25<span class="cite-bracket">&#93;</span></a></sup> </p><p>Beside these functions, an opsin without Lys296<sup>7.43</sup>, such as a gluopsin, could still be light sensitive, since in cattle rhodopsin, the retinal binding lysine can be shifted from position 296 to other positions, even into other transmembrane domains, without changing light sensitivity.<sup id="cite_ref-DevineOprian2013_35-0" class="reference"><a href="#cite_note-DevineOprian2013-35"><span class="cite-bracket">&#91;</span>35<span class="cite-bracket">&#93;</span></a></sup> </p> <style data-mw-deduplicate="TemplateStyles:r1275594942">@media all and (max-width:720px){.mw-parser-output .mod-gallery{width:100%!important}}.mw-parser-output .mod-gallery{display:table}.mw-parser-output .mod-gallery-default{background:transparent;margin-top:4px}.mw-parser-output .mod-gallery-center{margin-left:auto;margin-right:auto}.mw-parser-output .mod-gallery-left{float:left}.mw-parser-output .mod-gallery-right{float:right}.mw-parser-output .mod-gallery-none{float:none}.mw-parser-output .mod-gallery-center .gallery{justify-content:center}.mw-parser-output .mod-gallery-left .gallery{justify-content:left}.mw-parser-output .mod-gallery-right .gallery{justify-content:right}.mw-parser-output .mod-gallery-collapsible{width:100%}.mw-parser-output .mod-gallery .title,.mw-parser-output .mod-gallery .main,.mw-parser-output .mod-gallery .footer{display:table-row}.mw-parser-output .mod-gallery .title>div{display:table-cell;padding:0 4px 4px;text-align:center;font-weight:bold}.mw-parser-output .mod-gallery .main>div{display:table-cell}.mw-parser-output .mod-gallery .gallery.gallery.gallery{line-height:1.35em;display:flex;flex-wrap:wrap;column-gap:4px}.mw-parser-output .mod-gallery .footer>div{display:table-cell;padding:4px;text-align:right;font-size:85%;line-height:1em}.mw-parser-output .mod-gallery .title>div *,.mw-parser-output .mod-gallery .footer>div *{overflow:visible}.mw-parser-output .mod-gallery .gallerybox img{background:none!important}.mw-parser-output .mod-gallery .bordered-images .thumb img{outline:solid var(--background-color-neutral,#eaecf0)1px}.mw-parser-output .mod-gallery .whitebg .thumb{background:var(--background-color-base,#fff)!important}@media screen{html.skin-theme-clientpref-night .mw-parser-output .mod-gallery .bordered-images .thumb img[alt*="\200b \200b \200b "],html.skin-theme-clientpref-night .mw-parser-output .skin-invert-image .mod-gallery .whitebg .thumb.thumb.thumb img{outline:solid #d7d7d7 1px}html.skin-theme-clientpref-night .mw-parser-output .skin-invert-image .mod-gallery .whitebg .thumb.thumb.thumb img{background:none!important}html.skin-theme-clientpref-night .mw-parser-output .mod-gallery .whitebg .thumb img:not([alt*="\200b \200b \200b "]):not([alt*="\200b \200b \200c "]){background:white!important}html.skin-theme-clientpref-night .mw-parser-output .mod-gallery img[alt*="\200b \200b \200b "]{filter:invert(1)hue-rotate(180deg)}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .mod-gallery .bordered-images .thumb img[alt*="\200b \200b \200b "],html.skin-theme-clientpref-os .mw-parser-output .skin-invert-image .mod-gallery .whitebg .thumb.thumb.thumb img{outline:solid #d7d7d7 1px}html.skin-theme-clientpref-os .mw-parser-output .skin-invert-image .mod-gallery .whitebg .thumb.thumb.thumb img{background:none!important}html.skin-theme-clientpref-os .mw-parser-output .mod-gallery .whitebg .thumb img:not([alt*="\200b \200b \200b "]):not([alt*="\200b \200b \200c "]){background:white!important}html.skin-theme-clientpref-os .mw-parser-output .mod-gallery img[alt*="\200b \200b \200b "]{filter:invert(1)hue-rotate(180deg)}}</style><div class="mod-gallery mod-gallery-default mod-gallery-left"><div class="title"><div>Opsins have the retinal binding lysine, except the nemopsins and gluopsins<sup id="cite_ref-Guehmann2022_21-7" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup></div></div><div class="main"><div><ul class="gallery mw-gallery-packed nochecker bordered-images whitebg"> <li class="gallerybox" style="width: 469.33333333333px"> <div class="thumb" style="width: 467.33333333333px;"><span typeof="mw:File"><a href="/wiki/File:Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg" class="mw-file-description" title="Most known opsins have the retinal binding lysine except some among the tetraopins, The outgroup contains other G protein-coupled receptors."><img alt="Most known opsins have the retinal binding lysine except some among the tetraopins, The outgroup contains other G protein-coupled receptors." src="//upload.wikimedia.org/wikipedia/commons/thumb/8/81/Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg/701px-Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg.png" decoding="async" width="468" height="300" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/81/Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg/1051px-Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/81/Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg/1401px-Opsin_Phylogeny_with_the_main_Groups_the_Tetraopsins_Highlighted.svg.png 2x" data-file-width="1650" data-file-height="1060" /></a></span></div> <div class="gallerytext">Most known opsins have the retinal binding lysine except some among the tetraopins, The outgroup contains other <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptors</a>.</div> </li> <li class="gallerybox" style="width: 610.66666666667px"> <div class="thumb" style="width: 608.66666666667px;"><span typeof="mw:File"><a href="/wiki/File:Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg" class="mw-file-description" title="Most tetraopsins have also the retinal binding lysine except some of the chromopsins, which are highlighted by the frame and expanded in the next image. The outgroup contains other G protein-coupled receptors including the other opsins."><img alt="Most tetraopsins have also the retinal binding lysine except some of the chromopsins, which are highlighted by the frame and expanded in the next image. The outgroup contains other G protein-coupled receptors including the other opsins." src="//upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg/913px-Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg.png" decoding="async" width="609" height="300" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg/1369px-Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg/1825px-Tetraopsin_Phylogeny_with_the_Chromopsins_Highlighted.svg.png 2x" data-file-width="1500" data-file-height="740" /></a></span></div> <div class="gallerytext">Most tetraopsins have also the retinal binding lysine except some of the chromopsins, which are highlighted by the frame and expanded in the next image. The outgroup contains other G protein-coupled receptors including the other opsins.</div> </li> <li class="gallerybox" style="width: 491.33333333333px"> <div class="thumb" style="width: 489.33333333333px;"><span typeof="mw:File"><a href="/wiki/File:Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg" class="mw-file-description" title="Most chromopsins have also the retinal binding lysine except the nemopsins, where it is replaced by argenine (R), and the gluopsins, where it is replaced by glutamic acid (E). The astropsins, the nemopsins and the gluopsins are highlighted by the frames. The outgroup contains other G protein-coupled receptors including the other opsins."><img alt="Most chromopsins have also the retinal binding lysine except the nemopsins, where it is replaced by argenine (R), and the gluopsins, where it is replaced by glutamic acid (E). The astropsins, the nemopsins and the gluopsins are highlighted by the frames. The outgroup contains other G protein-coupled receptors including the other opsins." src="//upload.wikimedia.org/wikipedia/commons/thumb/7/75/Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg/734px-Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg.png" decoding="async" width="490" height="300" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/75/Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg/1101px-Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/75/Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg/1468px-Chromopsins_with_the_Gluopsins_Nemopsins_and_Astropsins_Highlighted.svg.png 2x" data-file-width="2300" data-file-height="1410" /></a></span></div> <div class="gallerytext">Most chromopsins have also the retinal binding lysine except the nemopsins, where it is replaced by <a href="/wiki/Argenine" class="mw-redirect" title="Argenine">argenine</a> (R), and the gluopsins, where it is replaced by <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a> (E). The astropsins, the nemopsins and the gluopsins are highlighted by the frames. The outgroup contains other G protein-coupled receptors including the other opsins.</div> </li> </ul></div></div></div> <div style="clear:both;" class=""></div> <p>In the <a href="/wiki/Phylogeny" class="mw-redirect" title="Phylogeny">phylogeny</a> above, each <a href="/wiki/Clade" title="Clade">clade</a> contains sequences from opsins and other G protein-coupled receptors. The number of sequences and two pie charts are shown next to the clade. The first pie chart shows the percentage of a certain <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> at the position in the sequences corresponding Lys296<sup>7.43</sup> in cattle rhodopsin. The amino acids are color-coded. The colors are red for <a href="/wiki/Lysine" title="Lysine">lysine</a> (K), purple for <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a> (E), orange for <a href="/wiki/Argenine" class="mw-redirect" title="Argenine">argenine</a> (R), dark and mid-gray for other amino acids, and light gray for sequences that have no data at that position. The second pie chart gives the taxon composition for each clade, green stands for <a href="/wiki/Craniate" title="Craniate">craniates</a>, dark green for <a href="/wiki/Cephalochordate" class="mw-redirect" title="Cephalochordate">cephalochordates</a>, mid green for <a href="/wiki/Echinoderm" title="Echinoderm">echinoderms</a>, brown for <a href="/wiki/Nematode" title="Nematode">nematodes</a>, pale pink for <a href="/wiki/Annelid" title="Annelid">annelids</a>, dark blue for <a href="/wiki/Arthropod" title="Arthropod">arthropods</a>, light blue for <a href="/wiki/Mollusk" class="mw-redirect" title="Mollusk">mollusks</a>, and purple for <a href="/wiki/Cnidarian" class="mw-redirect" title="Cnidarian">cnidarians</a>. The branches to the clades have pie charts, which give support values for the branches. The values are from right to left SH-aLRT/aBayes/UFBoot. The branches are considered supported when SH-aLRT ≥ 80%, aBayes ≥ 0.95, and UFBoot ≥ 95%. If a support value is above its threshold the pie chart is black otherwise gray.<sup id="cite_ref-Guehmann2022_21-8" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="The_NPxxY_motif">The NPxxY motif</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=4" title="Edit section: The NPxxY motif"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/w/index.php?title=NPxxY_motif&amp;action=edit&amp;redlink=1" class="new" title="NPxxY motif (page does not exist)">NPxxY<sup>7.53</sup> motif</a> is well-conserved among opsins and G-protein-coupled receptors. This motif is important for G-protein binding and receptor activation.<sup id="cite_ref-Guehmann2022_21-9" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> For instance, if it is mutated to DPxxY<sup>7.53</sup> (<a href="/wiki/Asparagine" title="Asparagine">Asn</a><sup>7.49</sup> → <a href="/wiki/Aspartic_acid" title="Aspartic acid">Asp</a><sup>7.49</sup>) in the <a href="/wiki/Human" title="Human">human</a> <a href="/wiki/M3_muscarinic_receptor" class="mw-redirect" title="M3 muscarinic receptor">m3 muscarinic receptor</a>, activation is not affected, but it is abolished if it is mutated to APxxY<sup>7.53</sup> (<a href="/wiki/Asparagine" title="Asparagine">Asn</a><sup>7.49</sup> → <a href="/wiki/Alanine" title="Alanine">Ala</a><sup>7.49</sup>).<sup id="cite_ref-Borroto-Escuela2011_36-0" class="reference"><a href="#cite_note-Borroto-Escuela2011-36"><span class="cite-bracket">&#91;</span>36<span class="cite-bracket">&#93;</span></a></sup> Such a mutation to APxxY<sup>7.53</sup> (Asn<sup>7.49</sup> → Ala<sup>7.49</sup>) reduces the G-protein activation of cattle rhodopsin to 45% compared to wild type. Also in cattle rhodopsin, if the motif is mutated to NPxxA<sup>7.53</sup> (<a href="/wiki/Tyrosine" title="Tyrosine">Tyr</a><sup>7.53</sup> → <a href="/wiki/Alanine" title="Alanine">Ala</a><sup>7.53</sup>), cattle rhodopsin does not activate the G-protein.<sup id="cite_ref-Fritze2003_37-0" class="reference"><a href="#cite_note-Fritze2003-37"><span class="cite-bracket">&#91;</span>37<span class="cite-bracket">&#93;</span></a></sup> Such a mutation also reduces the activation of the <a href="/wiki/Vasopressin_V2_receptor" class="mw-redirect" title="Vasopressin V2 receptor">vasopressin V2 receptor</a>. In fact in G-protein-coupled receptors, only <a href="/wiki/Loss_of_function" class="mw-redirect" title="Loss of function">loss of function</a> disease mutations are known for Tyr<sup>7.53</sup>⁠.<sup id="cite_ref-Zhou2019_38-0" class="reference"><a href="#cite_note-Zhou2019-38"><span class="cite-bracket">&#91;</span>38<span class="cite-bracket">&#93;</span></a></sup> </p><p>Also mutations of <a href="/wiki/Proline" title="Proline">Pro</a><sup>7.50</sup> influence G-protein activation, if the motif is mutated to NAxxY<sup>7.53</sup> (<a href="/wiki/Proline" title="Proline">Pro</a><sup>7.50</sup> → <a href="/wiki/Alanine" title="Alanine">Ala</a><sup>7.50</sup>) in the <a href="/wiki/Rat" title="Rat">rat</a> <a href="/wiki/M3_muscarinic_receptor" class="mw-redirect" title="M3 muscarinic receptor">m3 muscarinic receptor</a>, the receptor can still be activated but less efficiently,<sup id="cite_ref-Wess1993_39-0" class="reference"><a href="#cite_note-Wess1993-39"><span class="cite-bracket">&#91;</span>39<span class="cite-bracket">&#93;</span></a></sup> this mutation even abolishes activation in the <a href="/wiki/Cholecystokinin_B_receptor" title="Cholecystokinin B receptor">cholecystokinin B receptor</a> completely.<sup id="cite_ref-Gales2000_40-0" class="reference"><a href="#cite_note-Gales2000-40"><span class="cite-bracket">&#91;</span>40<span class="cite-bracket">&#93;</span></a></sup>⁠ In fact, the <a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">RGR-opsins</a> have NAxxY<sup>7.53</sup> and <a href="/w/index.php?title=Retinochrome&amp;action=edit&amp;redlink=1" class="new" title="Retinochrome (page does not exist)">retinochromes</a> have VPxxY7.53 for annelids or YPxxY7.53 for mollusks, natively. Both RGR-opsins and retinochromes, belong to the chromopsins.<sup id="cite_ref-Guehmann2022_21-10" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> RGR-opsins<sup id="cite_ref-Hao1999_41-0" class="reference"><a href="#cite_note-Hao1999-41"><span class="cite-bracket">&#91;</span>41<span class="cite-bracket">&#93;</span></a></sup> and retinochromes<sup id="cite_ref-42" class="reference"><a href="#cite_note-42"><span class="cite-bracket">&#91;</span>42<span class="cite-bracket">&#93;</span></a></sup> also bind unlike most opsins all-<i>trans</i>-retinal in the dark and convert it to 11-<i>cis</i>-retinal when illuminated. Therefore, RGR-opsins and retinochromes are thought to neither signal nor activate a phototransduction cascade but to work as <a href="/wiki/Photoisomerase" class="mw-redirect" title="Photoisomerase">photoisomerases</a> to produce 11-<i>cis</i>-retinal for other opsins.<sup id="cite_ref-Tsukamoto2010_43-0" class="reference"><a href="#cite_note-Tsukamoto2010-43"><span class="cite-bracket">&#91;</span>43<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Terakita2005_44-0" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> This view is considered established in the opsin literature,<sup id="cite_ref-Leung2017_34-1" class="reference"><a href="#cite_note-Leung2017-34"><span class="cite-bracket">&#91;</span>34<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">&#91;</span>45<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Tsukamoto2010_43-1" class="reference"><a href="#cite_note-Tsukamoto2010-43"><span class="cite-bracket">&#91;</span>43<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-46" class="reference"><a href="#cite_note-46"><span class="cite-bracket">&#91;</span>46<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Kato2016_47-0" class="reference"><a href="#cite_note-Kato2016-47"><span class="cite-bracket">&#91;</span>47<span class="cite-bracket">&#93;</span></a></sup> even so it has not been shown, conclusively.<sup id="cite_ref-Guehmann2022_21-11" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> In fact, the human MT2 <a href="/wiki/Melatonin_receptor" title="Melatonin receptor">melatonin receptor</a> signals via a <a href="/wiki/G-protein" class="mw-redirect" title="G-protein">G-protein</a> and has an NAxxY<sup>7.53</sup> motif natively. If this motif is mutated to NPxxY<sup>7.53</sup> (Ala<sup>7.50</sup> → Pro<sup>7.50</sup>), the receptor cannot be activated, but can be rescued partially if the motif is mutated to NVxxY<sup>7.53</sup> (Ala<sup>7.50</sup> → <a href="/wiki/Valine" title="Valine">Val</a><sup>7.50</sup>).<sup id="cite_ref-Mazna2008_48-0" class="reference"><a href="#cite_note-Mazna2008-48"><span class="cite-bracket">&#91;</span>48<span class="cite-bracket">&#93;</span></a></sup> Furthermore, when the motif is mutated to NAxxY<sup>7.53</sup> (Pro<sup>7.50</sup> → Ala<sup>7.50</sup>) in cattle rhodopsin, the mutant has 141% of wild type activity.<sup id="cite_ref-Fritze2003_37-1" class="reference"><a href="#cite_note-Fritze2003-37"><span class="cite-bracket">&#91;</span>37<span class="cite-bracket">&#93;</span></a></sup> This evidence shows that a GPCR does not need a standard NPxxY<sup>7.53</sup> motif for signaling.<sup id="cite_ref-Guehmann2022_21-12" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p> <figure class="mw-halign-left" typeof="mw:File/Frame"><a href="/wiki/File:Chromopsin_Consensus_Sequence_Logos.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e4/Chromopsin_Consensus_Sequence_Logos.svg/1073px-Chromopsin_Consensus_Sequence_Logos.svg.png" decoding="async" width="1073" height="230" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e4/Chromopsin_Consensus_Sequence_Logos.svg/1610px-Chromopsin_Consensus_Sequence_Logos.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e4/Chromopsin_Consensus_Sequence_Logos.svg/2146px-Chromopsin_Consensus_Sequence_Logos.svg.png 2x" data-file-width="1073" data-file-height="230" /></a><figcaption>Consensus sequences of the different chromopsins: The first column contains a number for each chromopsin group for easy reference. The second column shows the names for each group. The third contains the number of sequences in each group. And the fourth column contains the <a href="/wiki/Sequence_logo" title="Sequence logo">sequence logo</a>, the height of the letters indicates the percentage of that <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> given at that position. The x-axis gives the position of the amino acid corresponding to cattle rhodopsin. Positions 292<sup>7.39</sup> and 314<sup>7.64</sup> are highlighted in gray. <a href="/wiki/Lysine" title="Lysine">Lysine</a> (K) 296<sup>7.43</sup> is highlighted with a gray background, which is replaced in the nemopsins by <a href="/wiki/Arginine" title="Arginine">arginine</a> (R) and in the gluopsins by <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a> (E). The NPxxY<sup>7.53</sup> motif is highlighted with a gray background. It is conserved in most opsins and G-protein-coupled receptors, however it is derived in the retinochromes, RGR-opsins, and Gluopsins.<sup id="cite_ref-Guehmann2022_21-13" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup></figcaption></figure> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading3"><h3 id="Other_residues_and_motifs">Other residues and motifs</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=5" title="Edit section: Other residues and motifs"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Cys138 and Cys110 form a highly conserved <a href="/wiki/Disulfide_bridge" class="mw-redirect" title="Disulfide bridge">disulfide bridge</a>. Glu113 serves as the counterion, stabilizing the protonation of the Schiff linkage between Lys296 and the ligand retinal. The Glu134-Arg135-Tyr136 is another highly conserved motif, involved in the propagation of the transduction signal once a photon has been absorbed. </p> <div class="mw-heading mw-heading2"><h2 id="Spectral_tuning_sites">Spectral tuning sites</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=6" title="Edit section: Spectral tuning sites"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Certain <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> residues, termed <i>spectral tuning sites</i>, have a strong effect on <i>λ</i><sub>max</sub> values. Using <a href="/wiki/Site-directed_mutagenesis" title="Site-directed mutagenesis">site-directed mutagenesis</a>, it is possible to selectively mutate these residues and investigate the resulting changes in light absorption properties of the opsin. It is important to differentiate <i>spectral tuning sites</i>, residues that affect the wavelength at which the opsin absorbs light, from <i>functionally conserved sites</i>, residues important for the proper functioning of the opsin. They are not mutually exclusive, but, for practical reasons, it is easier to investigate spectral tuning sites that do not affect opsin functionality. For a comprehensive review of spectral tuning sites see Yokoyama<sup id="cite_ref-49" class="reference"><a href="#cite_note-49"><span class="cite-bracket">&#91;</span>49<span class="cite-bracket">&#93;</span></a></sup> and Deeb.<sup id="cite_ref-50" class="reference"><a href="#cite_note-50"><span class="cite-bracket">&#91;</span>50<span class="cite-bracket">&#93;</span></a></sup> The impact of spectral tuning sites on <i>λ</i><sub>max</sub> differs between different opsin groups and between opsin groups of different species. </p> <div class="mw-heading mw-heading2"><h2 id="Opsins_in_the_human_eye,_brain,_and_skin"><span id="Opsins_in_the_human_eye.2C_brain.2C_and_skin"></span>Opsins in the human eye, brain, and skin</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=7" title="Edit section: Opsins in the human eye, brain, and skin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <table class="wikitable"> <tbody><tr> <th><abbr title="Abbreviation">Abbr.</abbr> </th> <th>Name </th> <th>λ<sub>max</sub> </th> <th>Color </th> <th>Eye </th> <th>Brain </th> <th>Skin </th> <th>Chromosomal location<sup id="cite_ref-Terakita2005_44-1" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </th></tr> <tr> <td><a href="/wiki/OPN1LW" title="OPN1LW">OPN1LW</a> </td> <td>L-cone (red-cone) opsin </td> <td>557&#160;nm </td> <td>Yellow </td> <td>Cone </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>Xq28<sup id="cite_ref-Terakita2005_44-2" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/OPN1MW" title="OPN1MW">OPN1MW</a> </td> <td>M-cone (green-cone) opsin </td> <td>527&#160;nm </td> <td>Green </td> <td>Cone </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>Xq28<sup id="cite_ref-Terakita2005_44-3" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/OPN1SW" title="OPN1SW">OPN1SW</a> </td> <td>S-cone (blue-cone) opsin </td> <td>420&#160;nm </td> <td>Violet </td> <td>Cone </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>Melanocytes, keratinocytes<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-0" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup> </td> <td>7q32.1<sup id="cite_ref-Terakita2005_44-4" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Rhodopsin" title="Rhodopsin">OPN2</a> (RHO) </td> <td>Rhodopsin </td> <td>505&#160;nm </td> <td>Blue–green </td> <td>Rod </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>Melanocytes, keratinocytes<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-1" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup> </td> <td>3q22.1<sup id="cite_ref-Terakita2005_44-5" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/OPN3" title="OPN3">OPN3</a> </td> <td>Encephalopsin, panopsin </td> <td>S-M </td> <td>Blue–green </td> <td>Rod, cone, OPL, IPL, GCL<sup id="cite_ref-WhiteChiano2008_52-0" class="reference"><a href="#cite_note-WhiteChiano2008-52"><span class="cite-bracket">&#91;</span>52<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Cerebral cortex, cerebellum, striatum, thalamus, hypothalamus<sup id="cite_ref-Blackshaw1999_53-0" class="reference"><a href="#cite_note-Blackshaw1999-53"><span class="cite-bracket">&#91;</span>53<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-54" class="reference"><a href="#cite_note-54"><span class="cite-bracket">&#91;</span>54<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Melanocytes, keratinocytes<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-2" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup> </td> <td>1q43<sup id="cite_ref-Terakita2005_44-6" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/OPN4" class="mw-redirect" title="OPN4">OPN4</a> </td> <td>Melanopsin </td> <td>480&#160;nm<sup id="cite_ref-BailesLucas2013_55-0" class="reference"><a href="#cite_note-BailesLucas2013-55"><span class="cite-bracket">&#91;</span>55<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Sky blue </td> <td>ipRGC<sup id="cite_ref-BailesLucas2013_55-1" class="reference"><a href="#cite_note-BailesLucas2013-55"><span class="cite-bracket">&#91;</span>55<span class="cite-bracket">&#93;</span></a></sup> </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>10q23.2<sup id="cite_ref-Terakita2005_44-7" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/OPN5" title="OPN5">OPN5</a> </td> <td>Neuropsin </td> <td>380&#160;nm<sup id="cite_ref-Kojima2011_56-0" class="reference"><a href="#cite_note-Kojima2011-56"><span class="cite-bracket">&#91;</span>56<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Ultraviolet<sup id="cite_ref-Kojima2011_56-1" class="reference"><a href="#cite_note-Kojima2011-56"><span class="cite-bracket">&#91;</span>56<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Neural retina, RPE<sup id="cite_ref-TarttelinBellingham2003_57-0" class="reference"><a href="#cite_note-TarttelinBellingham2003-57"><span class="cite-bracket">&#91;</span>57<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Anterior <a href="/wiki/Hypothalamus" title="Hypothalamus">hypothalamus</a><sup id="cite_ref-YamashitaOno2014_58-0" class="reference"><a href="#cite_note-YamashitaOno2014-58"><span class="cite-bracket">&#91;</span>58<span class="cite-bracket">&#93;</span></a></sup> </td> <td>Melanocytes, keratinocytes<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-3" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup> </td> <td>6p12.3<sup id="cite_ref-Terakita2005_44-8" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/RRH" title="RRH">RRH</a> </td> <td>Peropsin </td> <td> </td> <td> </td> <td>RPE cells - microvilli </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>4q25<sup id="cite_ref-Terakita2005_44-9" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">RGR</a> </td> <td>Retinal G protein coupled receptor </td> <td> </td> <td> </td> <td>RPE cells </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">— </td> <td>10q23.1<sup id="cite_ref-Terakita2005_44-10" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> </td></tr></tbody></table> <p>RPE, <a href="/wiki/Retinal_pigment_epithelium" title="Retinal pigment epithelium">retinal pigment epithelium</a>; ipRGC, <a href="/wiki/Intrinsically_photosensitive_retinal_ganglion_cells" class="mw-redirect" title="Intrinsically photosensitive retinal ganglion cells">intrinsically photosensitive retinal ganglion cells</a>; OPL, <a href="/wiki/Outer_plexiform_layer" title="Outer plexiform layer">outer plexiform layer</a>; IPL, <a href="/wiki/Inner_plexiform_layer" title="Inner plexiform layer">inner plexiform layer</a>; GCL, <a href="/wiki/Ganglion_cell_layer" title="Ganglion cell layer">ganglion cell layer</a> </p> <div class="mw-heading mw-heading2"><h2 id="Cuttlefish">Cuttlefish</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=8" title="Edit section: Cuttlefish"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Cuttlefish" title="Cuttlefish">Cuttlefish</a> and <a href="/wiki/Octopus" title="Octopus">octopuses</a> contain opsin in their skin as part of the chromophores. The opsin is part of the sensing network detecting the colour and shape of the cuttlefish's surroundings.<sup id="cite_ref-Mäthger2010_59-0" class="reference"><a href="#cite_note-Mäthger2010-59"><span class="cite-bracket">&#91;</span>59<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Yong2015_60-0" class="reference"><a href="#cite_note-Yong2015-60"><span class="cite-bracket">&#91;</span>60<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Yu2014_61-0" class="reference"><a href="#cite_note-Yu2014-61"><span class="cite-bracket">&#91;</span>61<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Frogs_(order_Anura)"><span id="Frogs_.28order_Anura.29"></span>Frogs (order Anura)</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=9" title="Edit section: Frogs (order Anura)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Frog" title="Frog">Frogs</a> have evolved unique visual systems to adapt to their diverse habitats, from brightly lit forests to dimly lit ponds. Frogs are distinct among <a href="/wiki/Vertebrate" title="Vertebrate">vertebrates</a> because they lack the RH2 <a class="mw-selflink selflink">opsin</a>, typically used for detecting middle wavelengths of light in other species. This loss likely reflects their evolutionary focus on low-light vision, with RH1, a rod-specific opsin, taking the lead in supporting <a href="/wiki/Nocturnality" title="Nocturnality">nocturnal</a> and <a href="/wiki/Crepuscular_animal" title="Crepuscular animal">crepuscular</a> (dawn and dusk) activity.<sup id="cite_ref-:0_62-0" class="reference"><a href="#cite_note-:0-62"><span class="cite-bracket">&#91;</span>62<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-63" class="reference"><a href="#cite_note-63"><span class="cite-bracket">&#91;</span>63<span class="cite-bracket">&#93;</span></a></sup> </p><p>Despite the loss of RH2, frogs retain three cone opsins—SWS1, SWS2, and LWS—that allow for color vision during daylight. The SWS2 opsin, for instance, is tuned to detect blue and green light, which is especially useful in aquatic environments or shaded areas. This tuning is enhanced by specific <a href="/wiki/Mutation" title="Mutation">mutations</a> which increases sensitivity to low-light conditions and stabilizes the protein for better performance in dim environments.<sup id="cite_ref-:0_62-1" class="reference"><a href="#cite_note-:0-62"><span class="cite-bracket">&#91;</span>62<span class="cite-bracket">&#93;</span></a></sup> However, some frog species, such as <a href="/wiki/Poison_dart_frog" title="Poison dart frog">poison dart frogs</a> in the family Dendrobatidae, have lost the SWS2 opsin entirely. This change aligns with their reliance on longer wavelengths, like red and yellow, for tasks such as mate selection and predator deterrence, often linked to their vibrant <a href="/wiki/Aposematism" title="Aposematism">aposematic</a> (warning) coloration.<sup id="cite_ref-64" class="reference"><a href="#cite_note-64"><span class="cite-bracket">&#91;</span>64<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Phylogeny">Phylogeny</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=10" title="Edit section: Phylogeny"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Animal opsins (also known as type 2 opsins) are members of the seven-transmembrane-domain proteins of the <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptor</a> (GPCR) superfamily.<sup id="cite_ref-Casey1988_1-1" class="reference"><a href="#cite_note-Casey1988-1"><span class="cite-bracket">&#91;</span>1<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Attwood1994_2-1" class="reference"><a href="#cite_note-Attwood1994-2"><span class="cite-bracket">&#91;</span>2<span class="cite-bracket">&#93;</span></a></sup> </p><p>Animal opsins fall phylogenetically into five groups: The ciliary opsins (cilopsins, c-opsins), the <a href="/wiki/Rhabdomeric" class="mw-redirect" title="Rhabdomeric">rhabdomeric</a> opsins (r-opsins, rhabopsins), the xenopsins, the nessopsins, and the tetraopsins. Four of these subclades occur in <a href="/wiki/Bilateria" title="Bilateria">Bilateria</a> (all but the nessopsins).<sup id="cite_ref-Guehmann2022_21-14" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-1" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup> However, the bilaterian clades constitute a <a href="/wiki/Paraphyly" title="Paraphyly">paraphyletic</a> taxon without the opsins from the <a href="/wiki/Cnidarian" class="mw-redirect" title="Cnidarian">cnidarians</a>.<sup id="cite_ref-Guehmann2022_21-15" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-2" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-PorterBlasic2011_27-1" class="reference"><a href="#cite_note-PorterBlasic2011-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-LiegertováPergner2015_65-0" class="reference"><a href="#cite_note-LiegertováPergner2015-65"><span class="cite-bracket">&#91;</span>65<span class="cite-bracket">&#93;</span></a></sup> The nessopsins are also known as anthozoan opsins II<sup id="cite_ref-66" class="reference"><a href="#cite_note-66"><span class="cite-bracket">&#91;</span>66<span class="cite-bracket">&#93;</span></a></sup> or simply as the cnidarian opsins.<sup id="cite_ref-Rawlinson2019_67-0" class="reference"><a href="#cite_note-Rawlinson2019-67"><span class="cite-bracket">&#91;</span>67<span class="cite-bracket">&#93;</span></a></sup> The tetraopsins are also known as RGR/Go<sup id="cite_ref-FeudaHamilton2012_68-0" class="reference"><a href="#cite_note-FeudaHamilton2012-68"><span class="cite-bracket">&#91;</span>68<span class="cite-bracket">&#93;</span></a></sup> or Group 4 opsins<sup id="cite_ref-PorterBlasic2011_27-2" class="reference"><a href="#cite_note-PorterBlasic2011-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup> and contain three subgroups: the <a href="/wiki/OPN5" title="OPN5">neuropsins</a>, the Go-opsins, and the chromopsins.<sup id="cite_ref-Guehmann2022_21-16" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-3" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Rawlinson2019_67-1" class="reference"><a href="#cite_note-Rawlinson2019-67"><span class="cite-bracket">&#91;</span>67<span class="cite-bracket">&#93;</span></a></sup> The chromopsins have seven subgroups: the <a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">RGR-opsins</a>, the <a href="/w/index.php?title=Retinochrome&amp;action=edit&amp;redlink=1" class="new" title="Retinochrome (page does not exist)">retinochromes</a>, the <a href="/wiki/Peropsin" class="mw-redirect" title="Peropsin">peropsins</a>, the varropsins, the astropsins, the nemopsins, and the gluopsins.<sup id="cite_ref-Guehmann2022_21-17" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p><p>Animal visual opsins are traditionally classified as either ciliary or rhabdomeric. Ciliary opsins, found in <a href="/wiki/Vertebrates" class="mw-redirect" title="Vertebrates">vertebrates</a> and <a href="/wiki/Cnidarians" class="mw-redirect" title="Cnidarians">cnidarians</a>, attach to ciliary structures such as <a href="/wiki/Rod_cell" title="Rod cell">rods</a> and <a href="/wiki/Cone_cell" title="Cone cell">cones</a>. <a href="/wiki/Rhabdomeric" class="mw-redirect" title="Rhabdomeric">Rhabdomeric</a> opsins are attached to light-gathering organelles called rhabdomeres. This classification cuts across phylogenetic categories (clades) so that both the terms "ciliary" and "rhabdomeric" can be ambiguous. Here, "C-opsins (ciliary)" refers to a clade found exclusively in <a href="/wiki/Bilateria" title="Bilateria">Bilateria</a> and excludes cnidarian ciliary opsins such as those found in the <a href="/wiki/Box_jellyfish" title="Box jellyfish">box jellyfish</a>. Similarly, "R-opsin (rhabdomeric)" includes melanopsin even though it does not occur on rhabdomeres in vertebrates.<sup id="cite_ref-PorterBlasic2011_27-3" class="reference"><a href="#cite_note-PorterBlasic2011-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Ciliary_opsins">Ciliary opsins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=11" title="Edit section: Ciliary opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Ciliary opsins (cilopsins, c-opsins) are expressed in ciliary photoreceptor cells, and include the vertebrate visual opsins and encephalopsins.<sup id="cite_ref-Shichida2009_69-0" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> They convert light signals to nerve impulses via cyclic nucleotide gated ion channels, which work by increasing the charge differential across the cell membrane (i.e. <a href="/wiki/Hyperpolarization_(biology)" title="Hyperpolarization (biology)">hyperpolarization</a>.<sup id="cite_ref-Plachetzki2009_70-0" class="reference"><a href="#cite_note-Plachetzki2009-70"><span class="cite-bracket">&#91;</span>70<span class="cite-bracket">&#93;</span></a></sup>) </p> <div class="mw-heading mw-heading3"><h3 id="Vertebrate_visual_opsins">Vertebrate visual opsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=12" title="Edit section: Vertebrate visual opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951" /><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Vertebrate_visual_opsin" title="Vertebrate visual opsin">Vertebrate visual opsin</a></div> <p>Vertebrate visual opsins are a subclass of ciliary opsins that express in the vertebrate retina and mediate vision. They are further subdivided into: </p> <ul><li><a href="/wiki/Photopsin" class="mw-redirect" title="Photopsin">Photopsins</a> - those responsible for <a href="/wiki/Photopic_vision" title="Photopic vision">photopic vision</a> (daylight), which are expressed in cone cells; hence also <a href="/wiki/Cone_opsin" class="mw-redirect" title="Cone opsin">cone opsins</a>. Photopsins are further subdivided according to their <a href="/wiki/Spectral_sensitivity" title="Spectral sensitivity">spectral sensitivity</a>, namely the wavelength at which the highest light absorption is observed (<i>λ</i><sub>max</sub>). Vertebrates generally have four (SWS1, SWS2, RH2, LWS) classes of photopsins.<sup id="cite_ref-HuntCarvalho2009_71-0" class="reference"><a href="#cite_note-HuntCarvalho2009-71"><span class="cite-bracket">&#91;</span>71<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-TreziseCollin2005_72-0" class="reference"><a href="#cite_note-TreziseCollin2005-72"><span class="cite-bracket">&#91;</span>72<span class="cite-bracket">&#93;</span></a></sup> Mammals lost Rh2 and SWS2 classes during the <a href="/wiki/Nocturnal_bottleneck" title="Nocturnal bottleneck">nocturnal bottleneck</a>, so are generally <a href="/wiki/Dichromacy" title="Dichromacy">dichromatic</a>. <a href="/wiki/Evolution_of_color_vision_in_primates" title="Evolution of color vision in primates">Primate ancestors later developed</a> two distinct LWS opsins (LWS and MWS), leaving humans with 3 photopsins in 2 classes: SWS1 (<a href="/wiki/OPN1SW" title="OPN1SW">OPN1SW</a>) and two forms of LWS (<a href="/wiki/OPN1LW" title="OPN1LW">OPN1LW</a>, <a href="/wiki/OPN1MW" title="OPN1MW">OPN1MW</a>).</li> <li><a href="/wiki/Scotopsin" class="mw-redirect" title="Scotopsin">Scotopsins</a> - those responsible for <a href="/wiki/Scotopic_vision" title="Scotopic vision">scotopic vision</a> (dim light), which are expressed in rod cells; hence also <a href="/wiki/Rod_opsin" class="mw-redirect" title="Rod opsin">rod opsins</a>.<sup id="cite_ref-Shichida2009_69-1" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> The most common form of scotopsin is <a href="/wiki/Rhodopsin" title="Rhodopsin">rhodopsin</a>, thus usually denoted Rh1.<sup id="cite_ref-pmid28289214_73-0" class="reference"><a href="#cite_note-pmid28289214-73"><span class="cite-bracket">&#91;</span>73<span class="cite-bracket">&#93;</span></a></sup></li></ul> <div class="mw-heading mw-heading3"><h3 id="Extraretinal_(or_extra-ocular)_Rhodopsin-Like_Opsins_(Exo-Rh)"><span id="Extraretinal_.28or_extra-ocular.29_Rhodopsin-Like_Opsins_.28Exo-Rh.29"></span>Extraretinal (or extra-ocular) Rhodopsin-Like Opsins (Exo-Rh)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=13" title="Edit section: Extraretinal (or extra-ocular) Rhodopsin-Like Opsins (Exo-Rh)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>These pineal opsins, found in the <a href="/wiki/Actinopterygii" title="Actinopterygii">Actinopterygii</a> (ray-finned fish) apparently arose as a result of gene duplication from Rh1 (rhodopsin). These opsins appear to serve functions similar to those of pinopsin found in birds and reptiles.<sup id="cite_ref-pmid10581404_74-0" class="reference"><a href="#cite_note-pmid10581404-74"><span class="cite-bracket">&#91;</span>74<span class="cite-bracket">&#93;</span></a></sup> <sup id="cite_ref-TarttelinFransen2011_75-0" class="reference"><a href="#cite_note-TarttelinFransen2011-75"><span class="cite-bracket">&#91;</span>75<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Pinopsins">Pinopsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=14" title="Edit section: Pinopsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The first Pineal Opsin (Pinopsin) was found in the chicken <a href="/wiki/Pineal_gland" title="Pineal gland">pineal gland</a>. It is a blue sensitive opsin (<i>λ</i><sub>max</sub> = 470&#160;nm).<sup id="cite_ref-pmid7969427_76-0" class="reference"><a href="#cite_note-pmid7969427-76"><span class="cite-bracket">&#91;</span>76<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Nakane-Yoshimura-2019_77-0" class="reference"><a href="#cite_note-Nakane-Yoshimura-2019-77"><span class="cite-bracket">&#91;</span>77<span class="cite-bracket">&#93;</span></a></sup> </p><p>Pineal opsins have a wide range of expression in the brain, most notably in the <a href="/wiki/Pineal_gland" title="Pineal gland">pineal region</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Vertebrate_Ancient_(VA)_opsin"><span id="Vertebrate_Ancient_.28VA.29_opsin"></span>Vertebrate Ancient (VA) opsin</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=15" title="Edit section: Vertebrate Ancient (VA) opsin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Vertebrate Ancient (VA) opsin has three isoforms VA short (VAS), VA medium (VAM), and VA long (VAL). It is expressed in the inner retina, within the horizontal and <a href="/wiki/Amacrine_cells" class="mw-redirect" title="Amacrine cells">amacrine cells</a>, as well as the pineal organ and <a href="/wiki/Habenular" class="mw-redirect" title="Habenular">habenular</a> region of the brain.<sup id="cite_ref-pmid10821749_78-0" class="reference"><a href="#cite_note-pmid10821749-78"><span class="cite-bracket">&#91;</span>78<span class="cite-bracket">&#93;</span></a></sup> It is sensitive to approximately 500&#160;nm [14], found in most vertebrate classes, but not in mammals.<sup id="cite_ref-PoletiniRamos2015_79-0" class="reference"><a href="#cite_note-PoletiniRamos2015-79"><span class="cite-bracket">&#91;</span>79<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Parapinopsins">Parapinopsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=16" title="Edit section: Parapinopsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The first parapinopsin (PP) was found in the <a href="/wiki/Parapineal_organ" class="mw-redirect" title="Parapineal organ">parapineal organ</a> of the <a href="/wiki/Catfish" title="Catfish">catfish</a>.<sup id="cite_ref-pmid9334384_80-0" class="reference"><a href="#cite_note-pmid9334384-80"><span class="cite-bracket">&#91;</span>80<span class="cite-bracket">&#93;</span></a></sup> The parapinopsin of <a href="/wiki/Lamprey" title="Lamprey">lamprey</a> is a UV-sensitive opsin (<i>λ</i><sub>max</sub> = 370&#160;nm).<sup id="cite_ref-Koyanagi2004_81-0" class="reference"><a href="#cite_note-Koyanagi2004-81"><span class="cite-bracket">&#91;</span>81<span class="cite-bracket">&#93;</span></a></sup> The teleosts have two groups of parapinopsins, one is sensitive to UV (<i>λ</i><sub>max</sub> = 360-370&#160;nm), the other is sensitive to blue (<i>λ</i><sub>max</sub> = 460-480&#160;nm) light.<sup id="cite_ref-82" class="reference"><a href="#cite_note-82"><span class="cite-bracket">&#91;</span>82<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Parietopsins">Parietopsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=17" title="Edit section: Parietopsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The first parietopsin was found in the photoreceptor cells of the lizard parietal eye. The lizard parietopsin is green-sensitive (<i>λ</i><sub>max</sub> = 522&#160;nm), and despite it is a c-opsin, like the vertebrate visual opsins, it does not induce hyperpolarization via a Gt-protein, but induces depolarization via a Go-protein.<sup id="cite_ref-83" class="reference"><a href="#cite_note-83"><span class="cite-bracket">&#91;</span>83<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-KoyanagiTerakita2014_84-0" class="reference"><a href="#cite_note-KoyanagiTerakita2014-84"><span class="cite-bracket">&#91;</span>84<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Encephalopsin_or_Panopsin">Encephalopsin or Panopsin</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=18" title="Edit section: Encephalopsin or Panopsin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/OPN3" title="OPN3">panopsins</a> are found in many tissues (skin,<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-4" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup> brain,<sup id="cite_ref-Blackshaw1999_53-1" class="reference"><a href="#cite_note-Blackshaw1999-53"><span class="cite-bracket">&#91;</span>53<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Halford2001_85-0" class="reference"><a href="#cite_note-Halford2001-85"><span class="cite-bracket">&#91;</span>85<span class="cite-bracket">&#93;</span></a></sup> testes,<sup id="cite_ref-Blackshaw1999_53-2" class="reference"><a href="#cite_note-Blackshaw1999-53"><span class="cite-bracket">&#91;</span>53<span class="cite-bracket">&#93;</span></a></sup> heart, liver,<sup id="cite_ref-Halford2001_85-1" class="reference"><a href="#cite_note-Halford2001-85"><span class="cite-bracket">&#91;</span>85<span class="cite-bracket">&#93;</span></a></sup> kidney, skeletal muscle, lung, pancreas and retina<sup id="cite_ref-Halford2001_85-2" class="reference"><a href="#cite_note-Halford2001-85"><span class="cite-bracket">&#91;</span>85<span class="cite-bracket">&#93;</span></a></sup>). They were originally found in the human and <a href="/wiki/Mouse_brain" title="Mouse brain">mouse brain</a> and thus called encephalopsin.<sup id="cite_ref-Blackshaw1999_53-3" class="reference"><a href="#cite_note-Blackshaw1999-53"><span class="cite-bracket">&#91;</span>53<span class="cite-bracket">&#93;</span></a></sup> </p><p>The first invertebrate panopsin was found in the ciliary photoreceptor cells of the annelid <i><a href="/wiki/Platynereis_dumerilii" title="Platynereis dumerilii">Platynereis dumerilii</a></i> and is called c(iliary)-opsin.<sup id="cite_ref-Arendt2004_86-0" class="reference"><a href="#cite_note-Arendt2004-86"><span class="cite-bracket">&#91;</span>86<span class="cite-bracket">&#93;</span></a></sup> This c-opsin is <a href="/wiki/UV" class="mw-redirect" title="UV">UV</a>-sensitive (<i>λ</i><sub>max</sub> = 383&#160;nm) and can be tuned by 125&#160;nm at a single <a href="/wiki/Amino-acid" class="mw-redirect" title="Amino-acid">amino-acid</a> (range <i>λ</i><sub>max</sub> = 377 - 502&#160;nm).<sup id="cite_ref-Tsukamoto2017_87-0" class="reference"><a href="#cite_note-Tsukamoto2017-87"><span class="cite-bracket">&#91;</span>87<span class="cite-bracket">&#93;</span></a></sup> Thus, not unsurprisingly, a second but cyan sensitive c-opsin (<i>λ</i><sub>max</sub> = 490&#160;nm) exists in <i>Platynereis dumerilii</i>.<sup id="cite_ref-Ayers2018_88-0" class="reference"><a href="#cite_note-Ayers2018-88"><span class="cite-bracket">&#91;</span>88<span class="cite-bracket">&#93;</span></a></sup> The first c-opsin mediates in the larva UV induced <a href="/wiki/Gravitaxis" title="Gravitaxis">gravitaxis</a>. The gravitaxis forms with <a href="/wiki/Phototaxis" title="Phototaxis">phototaxis</a> a ratio-chromatic <a href="/wiki/Depth_gauge" title="Depth gauge">depth-gauge</a>.<sup id="cite_ref-Veraszto2018_89-0" class="reference"><a href="#cite_note-Veraszto2018-89"><span class="cite-bracket">&#91;</span>89<span class="cite-bracket">&#93;</span></a></sup> In different depths, the light in water is composed of different <a href="/wiki/Wavelength" title="Wavelength">wavelengths</a>: First the red (&gt; 600&#160;nm) and the UV and violet (&lt; 420&#160;nm) wavelengths disappear. The higher the depth the narrower the spectrum so that only <a href="/wiki/Cyan" title="Cyan">cyan</a> light (480&#160;nm) is left.<sup id="cite_ref-Guehmann2015_90-0" class="reference"><a href="#cite_note-Guehmann2015-90"><span class="cite-bracket">&#91;</span>90<span class="cite-bracket">&#93;</span></a></sup> Thus, the larvae can determine their depth by color. The color unlike brightness stays almost constant independent of time of day or the weather, for instance if it is cloudy.<sup id="cite_ref-Nilsson2009_91-0" class="reference"><a href="#cite_note-Nilsson2009-91"><span class="cite-bracket">&#91;</span>91<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Nilsson2013_92-0" class="reference"><a href="#cite_note-Nilsson2013-92"><span class="cite-bracket">&#91;</span>92<span class="cite-bracket">&#93;</span></a></sup> </p><p>Panopsins are also expressed in the brains of some insects.<sup id="cite_ref-Shichida2009_69-2" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> The panopsins of mosquito and pufferfish absorb maximally at 500&#160;nm and 460&#160;nm, respectively. Both activate in vitro Gi and Go proteins.<sup id="cite_ref-93" class="reference"><a href="#cite_note-93"><span class="cite-bracket">&#91;</span>93<span class="cite-bracket">&#93;</span></a></sup> </p><p>The panopsins are sister to the TMT-opsins.<sup id="cite_ref-Ramirez2016_28-4" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Sakai2015_94-0" class="reference"><a href="#cite_note-Sakai2015-94"><span class="cite-bracket">&#91;</span>94<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Kato2016_47-1" class="reference"><a href="#cite_note-Kato2016-47"><span class="cite-bracket">&#91;</span>47<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Fischer2013_95-0" class="reference"><a href="#cite_note-Fischer2013-95"><span class="cite-bracket">&#91;</span>95<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Teleost_Multiple_Tissue_(TMT)_Opsin"><span id="Teleost_Multiple_Tissue_.28TMT.29_Opsin"></span>Teleost Multiple Tissue (TMT) Opsin</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=19" title="Edit section: Teleost Multiple Tissue (TMT) Opsin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The first TMT-opsin was found in many tissues in <a href="/wiki/Teleost" title="Teleost">Teleost</a> fish and therefore they are called Teleost Multiple Tissue (TMT) opsins.<sup id="cite_ref-Moutsaki2003_96-0" class="reference"><a href="#cite_note-Moutsaki2003-96"><span class="cite-bracket">&#91;</span>96<span class="cite-bracket">&#93;</span></a></sup> TMT-opsins form three groups which are most closely related to a fourth group the panopsins, which thus are <a href="/wiki/Paralogous" class="mw-redirect" title="Paralogous">paralogous</a> to the TMT-opsins.<sup id="cite_ref-Ramirez2016_28-5" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Kato2016_47-2" class="reference"><a href="#cite_note-Kato2016-47"><span class="cite-bracket">&#91;</span>47<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Sakai2015_94-1" class="reference"><a href="#cite_note-Sakai2015-94"><span class="cite-bracket">&#91;</span>94<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Fischer2013_95-1" class="reference"><a href="#cite_note-Fischer2013-95"><span class="cite-bracket">&#91;</span>95<span class="cite-bracket">&#93;</span></a></sup> TMT-opsins and panopsins also share the same <a href="/wiki/Intron" title="Intron">introns</a>, which confirms that they belong together.<sup id="cite_ref-Moutsaki2003_96-1" class="reference"><a href="#cite_note-Moutsaki2003-96"><span class="cite-bracket">&#91;</span>96<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Opsins_in_cnidarians">Opsins in cnidarians</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=20" title="Edit section: Opsins in cnidarians"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Cnidaria" title="Cnidaria">Cnidaria</a>, which include jellyfish, corals, and sea <a href="/wiki/Sea_anemone" title="Sea anemone">anemones</a>, are the most <a href="/wiki/Basal_animals" class="mw-redirect" title="Basal animals">basal animals</a> to possess complex eyes. Jellyfish opsins in the <a href="/wiki/Rhopalium" title="Rhopalium">rhopalia</a> couple to Gs-proteins raising the intracellular cAMP level.<sup id="cite_ref-Koyanagi2008_97-0" class="reference"><a href="#cite_note-Koyanagi2008-97"><span class="cite-bracket">&#91;</span>97<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-LiegertováPergner2015_65-1" class="reference"><a href="#cite_note-LiegertováPergner2015-65"><span class="cite-bracket">&#91;</span>65<span class="cite-bracket">&#93;</span></a></sup> Coral opsins can couple to Gq-proteins and Gc-proteins. Gc-proteins are a subtype of G-proteins specific to cnidarians.<sup id="cite_ref-Mason2012_98-0" class="reference"><a href="#cite_note-Mason2012-98"><span class="cite-bracket">&#91;</span>98<span class="cite-bracket">&#93;</span></a></sup> The cnidarian opsins belong to two groups the xenopsins and the nessopsins. The xenopsins contain also bilaterian opsins, while the nessopsins are restricted to the cnidarians.<sup id="cite_ref-Guehmann2022_21-18" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-6" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup> However, earlier studies have found that some cnidarian opsins belong to the cilopsins, rhabopsins, and the tetraopsins of the <a href="/wiki/Bilaterian" class="mw-redirect" title="Bilaterian">bilaterians</a>.<sup id="cite_ref-FeudaHamilton2012_68-1" class="reference"><a href="#cite_note-FeudaHamilton2012-68"><span class="cite-bracket">&#91;</span>68<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Suga2008_99-0" class="reference"><a href="#cite_note-Suga2008-99"><span class="cite-bracket">&#91;</span>99<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Feuda2014_100-0" class="reference"><a href="#cite_note-Feuda2014-100"><span class="cite-bracket">&#91;</span>100<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Rhabdomeric_opsins">Rhabdomeric opsins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=21" title="Edit section: Rhabdomeric opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Rhabdomeric opsins (rhabopsins, r-opsins) are also known as Gq-opsins, because they couple to a Gq-protein. Rhabopsins are used by molluscs and arthropods. Arthropods appear to attain colour vision in a similar fashion to the vertebrates, by using three (or more) distinct groups of opsins, distinct both in terms of phylogeny and spectral sensitivity.<sup id="cite_ref-Shichida2009_69-3" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> The rhabopsin melanopsin is also expressed in vertebrates, where it regulates <a href="/wiki/Circadian_rhythm" title="Circadian rhythm">circadian rhythms</a> and mediates the pupillary reflex.<sup id="cite_ref-Shichida2009_69-4" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> </p><p>Unlike cilopsins, rhabopsins are associated with canonical transient receptor potential ion channels; these lead to the electric potential difference across a cell membrane being eradicated (i.e. <a href="/wiki/Depolarization" title="Depolarization">depolarization</a>).<sup id="cite_ref-Plachetzki2009_70-1" class="reference"><a href="#cite_note-Plachetzki2009-70"><span class="cite-bracket">&#91;</span>70<span class="cite-bracket">&#93;</span></a></sup> </p><p>The identification of the crystal structure of squid rhodopsin<sup id="cite_ref-Murakami2008_13-1" class="reference"><a href="#cite_note-Murakami2008-13"><span class="cite-bracket">&#91;</span>13<span class="cite-bracket">&#93;</span></a></sup> is likely to further our understanding of its function in this group. </p><p>Arthropods use different opsins in their different eye types, but at least in <i><a href="/wiki/Limulus" title="Limulus">Limulus</a></i> the opsins expressed in the lateral and the compound eyes are 99% identical and presumably diverged recently.<sup id="cite_ref-101" class="reference"><a href="#cite_note-101"><span class="cite-bracket">&#91;</span>101<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Melanopsin">Melanopsin</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=22" title="Edit section: Melanopsin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Melanopsin" title="Melanopsin">Melanopsin</a> (OPN4) is involved in <a href="/wiki/Circadian_rhythm" title="Circadian rhythm">circadian rhythms</a>, the <a href="/wiki/Pupillary_reflex" title="Pupillary reflex">pupillary reflex</a>, and color correction in high-brightness situations. Phylogenetically, it is a member of the rhabdomeric opsins (rhabopsins, r-opsins) and functionally and structurally a rhabopsin, but does not occur in rhabdomeres. </p> <div class="mw-heading mw-heading2"><h2 id="Tetraopsins">Tetraopsins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=23" title="Edit section: Tetraopsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The tetraopsins include the <a href="/wiki/OPN5" title="OPN5">neuropsins</a>, the Go-opsins, and the chromopsins.<sup id="cite_ref-Guehmann2022_21-19" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Ramirez2016_28-7" class="reference"><a href="#cite_note-Ramirez2016-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Rawlinson2019_67-2" class="reference"><a href="#cite_note-Rawlinson2019-67"><span class="cite-bracket">&#91;</span>67<span class="cite-bracket">&#93;</span></a></sup> The chromopsins consist of seven subgroups: the <a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">RGR-opsins</a>, the <a href="/w/index.php?title=Retinochrome&amp;action=edit&amp;redlink=1" class="new" title="Retinochrome (page does not exist)">retinochromes</a>, the <a href="/wiki/Peropsin" class="mw-redirect" title="Peropsin">peropsins</a>, the varropsins, the astropsins, the nemopsins, and the gluopsins.<sup id="cite_ref-Guehmann2022_21-20" class="reference"><a href="#cite_note-Guehmann2022-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Neuropsins">Neuropsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=24" title="Edit section: Neuropsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Neuropsins are sensitive to UVA, typically at 380&#160;nm. They are found in the brain, testes, skin, and retina of humans and rodents, as well as in the brain and retina of birds. In birds and rodents they mediate ultraviolet vision.<sup id="cite_ref-HaltaufderhydeOzdeslik2015_51-5" class="reference"><a href="#cite_note-HaltaufderhydeOzdeslik2015-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Kojima2011_56-2" class="reference"><a href="#cite_note-Kojima2011-56"><span class="cite-bracket">&#91;</span>56<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Yamashita2010_102-0" class="reference"><a href="#cite_note-Yamashita2010-102"><span class="cite-bracket">&#91;</span>102<span class="cite-bracket">&#93;</span></a></sup> They couple to Gi-proteins.<sup id="cite_ref-Kojima2011_56-3" class="reference"><a href="#cite_note-Kojima2011-56"><span class="cite-bracket">&#91;</span>56<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Yamashita2010_102-1" class="reference"><a href="#cite_note-Yamashita2010-102"><span class="cite-bracket">&#91;</span>102<span class="cite-bracket">&#93;</span></a></sup> In humans, Neuropsin is encoded by the <a href="/wiki/OPN5" title="OPN5">OPN5</a> gene. In the human retina, its function is unknown. In the mouse, it photo-entrains the retina and cornea at least ex vivo.<sup id="cite_ref-Buhr2015_103-0" class="reference"><a href="#cite_note-Buhr2015-103"><span class="cite-bracket">&#91;</span>103<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Go-opsins">Go-opsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=25" title="Edit section: Go-opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Go-opsins are absent from <a href="/wiki/Higher_vertebrates" class="mw-redirect" title="Higher vertebrates">higher vertebrates</a><sup id="cite_ref-PorterBlasic2011_27-4" class="reference"><a href="#cite_note-PorterBlasic2011-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup> and <a href="/wiki/Ecdysozoan" class="mw-redirect" title="Ecdysozoan">ecdysozoans</a>.<sup id="cite_ref-HeringMayer2014_104-0" class="reference"><a href="#cite_note-HeringMayer2014-104"><span class="cite-bracket">&#91;</span>104<span class="cite-bracket">&#93;</span></a></sup> They are found in the ciliary photoreceptor cells of the <a href="/wiki/Scallop" title="Scallop">scallop</a> eye<sup id="cite_ref-Kojima1997_105-0" class="reference"><a href="#cite_note-Kojima1997-105"><span class="cite-bracket">&#91;</span>105<span class="cite-bracket">&#93;</span></a></sup> and the basal chordate <a href="/wiki/Amphioxus" class="mw-redirect" title="Amphioxus">amphioxus</a>.<sup id="cite_ref-106" class="reference"><a href="#cite_note-106"><span class="cite-bracket">&#91;</span>106<span class="cite-bracket">&#93;</span></a></sup> In <i><a href="/wiki/Platynereis_dumerilii" title="Platynereis dumerilii">Platynereis dumerilii</a></i> however, a Go-opsin is expressed in the rhabdomeric photoreceptor cells of the eyes.<sup id="cite_ref-Guehmann2015_90-1" class="reference"><a href="#cite_note-Guehmann2015-90"><span class="cite-bracket">&#91;</span>90<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="RGR-opsins">RGR-opsins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=26" title="Edit section: RGR-opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>RGR-opsins, also known as <a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">Retinal G protein coupled receptors</a> are expressed in the <a href="/wiki/Retinal_pigment_epithelium" title="Retinal pigment epithelium">retinal pigment epithelium</a> (RPE) and <a href="/wiki/M%C3%BCller_cells" class="mw-redirect" title="Müller cells">Müller cells</a>.<sup id="cite_ref-Jiang1993_107-0" class="reference"><a href="#cite_note-Jiang1993-107"><span class="cite-bracket">&#91;</span>107<span class="cite-bracket">&#93;</span></a></sup> They preferentially bind all-trans-retinal in the dark instead of 11-cis-retinal.<sup id="cite_ref-Hao1999_41-1" class="reference"><a href="#cite_note-Hao1999-41"><span class="cite-bracket">&#91;</span>41<span class="cite-bracket">&#93;</span></a></sup> RGR-opsins were thought to be photoisomerases<sup id="cite_ref-Terakita2005_44-11" class="reference"><a href="#cite_note-Terakita2005-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup> but instead, they regulate retinoid traffic and production.<sup id="cite_ref-Shichida2009_69-5" class="reference"><a href="#cite_note-Shichida2009-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Nagata2010_108-0" class="reference"><a href="#cite_note-Nagata2010-108"><span class="cite-bracket">&#91;</span>108<span class="cite-bracket">&#93;</span></a></sup> In particular, they speed up light-independently the production of 11-cis-retinol (a precursor of 11-cis-retinal) from all-trans-retinyl-esters.<sup id="cite_ref-Wenzel2005_109-0" class="reference"><a href="#cite_note-Wenzel2005-109"><span class="cite-bracket">&#91;</span>109<span class="cite-bracket">&#93;</span></a></sup> However, the all-trans-retinyl-esters are made available light-dependently by RGR-opsins. Whether RGR-opsins regulate this via a G-protein or another signaling mechanism is unknown.<sup id="cite_ref-Radu2008_110-0" class="reference"><a href="#cite_note-Radu2008-110"><span class="cite-bracket">&#91;</span>110<span class="cite-bracket">&#93;</span></a></sup> The cattle RGR-opsin absorbs maximally at different wavelengths depending on the pH-value. At high pH it absorbs maximally blue (469&#160;nm) light and at low pH it absorbs maximally UV (370&#160;nm) light.<sup id="cite_ref-Hao1996_111-0" class="reference"><a href="#cite_note-Hao1996-111"><span class="cite-bracket">&#91;</span>111<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Peropsin">Peropsin</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=27" title="Edit section: Peropsin"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Peropsin" class="mw-redirect" title="Peropsin">Peropsin</a>, a visual pigment-like receptor, is a <a href="/wiki/Protein" title="Protein">protein</a> that in humans is encoded by the <i>RRH</i> <a href="/wiki/Gene" title="Gene">gene</a>.<sup id="cite_ref-pmid9275222_112-0" class="reference"><a href="#cite_note-pmid9275222-112"><span class="cite-bracket">&#91;</span>112<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Other_proteins_called_opsins">Other proteins called opsins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=28" title="Edit section: Other proteins called opsins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951" /><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Microbial_rhodopsin" title="Microbial rhodopsin">Microbial rhodopsin</a></div> <p>Photoreceptors can be classified several ways, including function (vision, phototaxis, photoperiodism, etc.), type of <a href="/wiki/Chromophore" title="Chromophore">chromophore</a> (<a href="/wiki/Retinal" title="Retinal">retinal</a>, <a href="/wiki/Flavine" class="mw-redirect" title="Flavine">flavine</a>, <a href="/wiki/Bilin_(biochemistry)" title="Bilin (biochemistry)">bilin</a>), molecular structure (<a href="/wiki/Biomolecular_structure#Tertiary_structure" title="Biomolecular structure">tertiary</a>, <a href="/wiki/Biomolecular_structure#Quaternary_structure" title="Biomolecular structure">quaternary</a>), signal output (<a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a>, <a href="/wiki/Redox" title="Redox">reduction</a>, <a href="/wiki/Oxidation" class="mw-redirect" title="Oxidation">oxidation</a>), etc.<sup id="cite_ref-Björn2015_113-0" class="reference"><a href="#cite_note-Björn2015-113"><span class="cite-bracket">&#91;</span>113<span class="cite-bracket">&#93;</span></a></sup> </p><p>Beside animal opsins, which are <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptors</a>, there is another group of <a href="/wiki/Photoreceptor_protein" title="Photoreceptor protein">photoreceptor proteins</a> called opsins.<sup id="cite_ref-Plachetzki2009_70-2" class="reference"><a href="#cite_note-Plachetzki2009-70"><span class="cite-bracket">&#91;</span>70<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Fernald2006_114-0" class="reference"><a href="#cite_note-Fernald2006-114"><span class="cite-bracket">&#91;</span>114<span class="cite-bracket">&#93;</span></a></sup> These are the <a href="/wiki/Microbial_rhodopsin" title="Microbial rhodopsin">microbial opsin</a>, they are used by <a href="/wiki/Prokaryote" title="Prokaryote">prokaryotes</a> and by some <a href="/wiki/Algae" title="Algae">algae</a> (as a component of <a href="/wiki/Channelrhodopsins" class="mw-redirect" title="Channelrhodopsins">channelrhodopsins</a>) and <a href="/wiki/Fungi" class="mw-redirect" title="Fungi">fungi</a>,<sup id="cite_ref-Waschuk2005_115-0" class="reference"><a href="#cite_note-Waschuk2005-115"><span class="cite-bracket">&#91;</span>115<span class="cite-bracket">&#93;</span></a></sup> whereas <a href="/wiki/Animal" title="Animal">animals</a> use animal opsins, exclusively. No opsins have been found outside these groups (for instance in plants, or <a href="/wiki/Placozoans" class="mw-redirect" title="Placozoans">placozoans</a>).<sup id="cite_ref-Plachetzki2009_70-3" class="reference"><a href="#cite_note-Plachetzki2009-70"><span class="cite-bracket">&#91;</span>70<span class="cite-bracket">&#93;</span></a></sup> </p><p>Microbial and animal opsins are also called type 1 and type 2 opsins respectively. Both types are called opsins, because at one time it was thought that they were related: Both are seven-transmembrane receptors and bind covalently <a href="/wiki/Retinal" title="Retinal">retinal</a> as chromophore, which turns them into <a href="/wiki/Photoreceptor_protein" title="Photoreceptor protein">photoreceptors</a> sensing light. However, both types are not related on the sequence level.<sup id="cite_ref-116" class="reference"><a href="#cite_note-116"><span class="cite-bracket">&#91;</span>116<span class="cite-bracket">&#93;</span></a></sup> </p><p>In fact, the sequence identity between animal and mirobial opsins is no greater than could be accounted for by random chance. However, in recent years new methods have been developed specific to <i>deep <a href="/wiki/Phylogeny" class="mw-redirect" title="Phylogeny">phylogeny</a></i>. As a result, several studies have found evidence of a possible phylogenetic relationship between the two.<sup id="cite_ref-ShenChen2013_117-0" class="reference"><a href="#cite_note-ShenChen2013-117"><span class="cite-bracket">&#91;</span>117<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-DevineOprian2013_35-1" class="reference"><a href="#cite_note-DevineOprian2013-35"><span class="cite-bracket">&#91;</span>35<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-ZhangWu2014_118-0" class="reference"><a href="#cite_note-ZhangWu2014-118"><span class="cite-bracket">&#91;</span>118<span class="cite-bracket">&#93;</span></a></sup> However, this does not necessarily mean that the last common ancestor of microbial and animal opsins was itself light sensitive: All animal opsins arose (by gene duplication and divergence) late in the history of the large <a href="/wiki/G-protein_coupled_receptor" class="mw-redirect" title="G-protein coupled receptor">G-protein coupled receptor</a> (GPCR) <a href="/wiki/Gene_family" title="Gene family">gene family</a>, which itself arose after the divergence of plants, fungi, choanflagellates and sponges from the earliest animals. The retinal chromophore is found solely in the opsin branch of this large gene family, meaning its occurrence elsewhere represents <a href="/wiki/Convergent_evolution" title="Convergent evolution">convergent evolution</a>, not <a href="/wiki/Homology_(biology)" title="Homology (biology)">homology</a>. Microbial rhodopsins are, by sequence, very different from any of the GPCR families.<sup id="cite_ref-pmid21402729_119-0" class="reference"><a href="#cite_note-pmid21402729-119"><span class="cite-bracket">&#91;</span>119<span class="cite-bracket">&#93;</span></a></sup> According to one hypothesis, both microbial and animal opsins belong to the <i><a href="/wiki/TOG_Superfamily" class="mw-redirect" title="TOG Superfamily">transporter-opsin-G protein-coupled receptor (TOG) superfamily</a></i>, a proposed clade that includes <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptor</a> (GPCR), Ion-translocating <a href="/wiki/Microbial_rhodopsin" title="Microbial rhodopsin">microbial rhodopsin</a> (MR), and seven others.<sup id="cite_ref-YeeShlykov2013_120-0" class="reference"><a href="#cite_note-YeeShlykov2013-120"><span class="cite-bracket">&#91;</span>120<span class="cite-bracket">&#93;</span></a></sup> </p><p>Most microbial opsins are <a href="/wiki/Ion_channel" title="Ion channel">ion channels</a> or <a href="/wiki/Ion_pump" title="Ion pump">pumps</a> instead of proper receptors and do not bind to a <a href="/wiki/G_protein" title="G protein">G protein</a>. Microbial opsins are found in all three domains of life: <a href="/wiki/Archaea" title="Archaea">Archaea</a>, <a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, and <a href="/wiki/Eukaryota" class="mw-redirect" title="Eukaryota">Eukaryota</a>. In Eukaryota, microbial opsins are found mainly in unicellular organisms such as green algae, and in fungi. In most complex multicellular eukaryotes, microbial opsins have been replaced with other light-sensitive molecules such as <a href="/wiki/Cryptochrome" title="Cryptochrome">cryptochrome</a> and <a href="/wiki/Phytochrome" title="Phytochrome">phytochrome</a> in plants, and animal opsins in <a href="/wiki/Animal" title="Animal">animals</a>.<sup id="cite_ref-YoshizawaKumagai2014_121-0" class="reference"><a href="#cite_note-YoshizawaKumagai2014-121"><span class="cite-bracket">&#91;</span>121<span class="cite-bracket">&#93;</span></a></sup> </p><p>Microbial opsins are often known by the rhodopsin form of the molecule, i.e., rhodopsin (in the broad sense) = opsin + chromophore. Among the many kinds of microbial opsins are the <a href="/wiki/Proton_pump" title="Proton pump">proton pumps</a> <a href="/wiki/Bacteriorhodopsin" title="Bacteriorhodopsin">bacteriorhodopsin</a> (BR) and xanthorhodopsin (xR), the <a href="/w/index.php?title=Chloride_pump&amp;action=edit&amp;redlink=1" class="new" title="Chloride pump (page does not exist)">chloride pump</a> <a href="/wiki/Halorhodopsin" title="Halorhodopsin">halorhodopsin</a> (HR), the photosensors sensory rhodopsin I (SRI) and <a href="/wiki/Sensory_rhodopsin_II" title="Sensory rhodopsin II">sensory rhodopsin II</a> (SRII), as well as <a href="/wiki/Proteorhodopsin" title="Proteorhodopsin">proteorhodopsin</a> (PR), <a href="/wiki/Neurospora" title="Neurospora">Neurospora</a> opsin I (NOPI), Chlamydomonas sensory rhodopsins A (CSRA), Chlamydomonas sensory rhodopsins B (CSRB), <a href="/wiki/Channelrhodopsin" title="Channelrhodopsin">channelrhodopsin</a> (ChR), and <a href="/wiki/Archaerhodopsin" title="Archaerhodopsin">archaerhodopsin</a> (Arch).<sup id="cite_ref-GroteEngelhard2014_122-0" class="reference"><a href="#cite_note-GroteEngelhard2014-122"><span class="cite-bracket">&#91;</span>122<span class="cite-bracket">&#93;</span></a></sup> </p><p>Several microbal opsins, such as <a href="/wiki/Proteorhodopsin" title="Proteorhodopsin">proteo-</a> and <a href="/wiki/Bacteriorhodopsin" title="Bacteriorhodopsin">bacteriorhodopsin</a>, are used by various bacterial groups to harvest energy from light to carry out metabolic processes using a non-<a href="/wiki/Chlorophyll" title="Chlorophyll">chlorophyll</a>-based pathway. Beside that, <a href="/wiki/Halorhodopsins" class="mw-redirect" title="Halorhodopsins">halorhodopsins</a> of <a href="/wiki/Halobacteria" class="mw-redirect" title="Halobacteria">Halobacteria</a> and <a href="/wiki/Channelrhodopsins" class="mw-redirect" title="Channelrhodopsins">channelrhodopsins</a> of some algae, e.g. <a href="/wiki/Volvox" title="Volvox">Volvox</a>, serve them as <a href="/wiki/Light-gated_ion_channel" title="Light-gated ion channel">light-gated ion channels</a>, amongst others also for <a href="/wiki/Phototaxis" title="Phototaxis">phototactic</a> purposes. Sensory rhodopsins exist in Halobacteria that induce a phototactic response by interacting with <a href="/wiki/Signal_transduction" title="Signal transduction">transducer</a> membrane-embedded proteins that have no relation to G proteins.<sup id="cite_ref-RomplerStaubert2007_123-0" class="reference"><a href="#cite_note-RomplerStaubert2007-123"><span class="cite-bracket">&#91;</span>123<span class="cite-bracket">&#93;</span></a></sup> </p><p>Microbal opsins (like <a href="/wiki/Channelrhodopsin" title="Channelrhodopsin">channelrhodopsin</a>, <a href="/wiki/Halorhodopsin" title="Halorhodopsin">halorhodopsin</a>, and <a href="/wiki/Archaerhodopsin" title="Archaerhodopsin">archaerhodopsin</a>) are used in <a href="/wiki/Optogenetics" title="Optogenetics">optogenetics</a> to switch on or off neuronal activity. Microbal opsins are preferred if the neuronal activity should be modulated at higher frequency, because they respond faster than animal opsins. This is because microbal opsins are ion channels or proton/<a href="/wiki/Ion_pump" title="Ion pump">ion pumps</a> and thus are activated by light directly, while animal opsins activate G-proteins, which then activate <a href="/wiki/Effector_(biology)" title="Effector (biology)">effector</a> enzymes that produce metabolites to open ion channels.<sup id="cite_ref-124" class="reference"><a href="#cite_note-124"><span class="cite-bracket">&#91;</span>124<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=29" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Retinylidene_protein" title="Retinylidene protein">Retinylidene protein</a></li> <li><a href="/wiki/Visual_cycle" title="Visual cycle">Visual cycle</a></li> <li><a href="/wiki/Visual_phototransduction" title="Visual phototransduction">Visual phototransduction</a></li> <li><a href="/wiki/Microbial_rhodopsin" title="Microbial rhodopsin">Microbial rhodopsin</a></li> <li><a href="/wiki/Channelrhodopsins" class="mw-redirect" title="Channelrhodopsins">Channelrhodopsins</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=30" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="http://homepages.bw.edu/~mbumbuli/cell/fig/opsin/">Illustration</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20200109152958/http://homepages.bw.edu/~mbumbuli/cell/fig/opsin/">Archived</a> 2020-01-09 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a> at <a href="/wiki/Baldwin-Wallace_College" class="mw-redirect" title="Baldwin-Wallace College">Baldwin-Wallace College</a></li> <li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Opsin">Opsin</a> at the U.S. National Library of Medicine <a href="/wiki/Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Opsin&amp;action=edit&amp;section=31" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist 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href="#cite_ref-Casey1988_1-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon 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style="width:1%;background-color: AntiqueWhite"><a class="mw-selflink selflink">Opsin</a><br />(<a href="/wiki/Retinylidene_protein" title="Retinylidene protein">retinylidene protein</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="/wiki/Vertebrate_visual_opsin" title="Vertebrate visual opsin">visual</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Rhodopsin" title="Rhodopsin">Rhodopsin</a></li> <li><a href="/wiki/Cone_opsin" class="mw-redirect" title="Cone opsin">Cone opsins</a> <ul><li><a href="/wiki/OPN1LW" title="OPN1LW">OPN1LW</a></li> <li><a href="/wiki/OPN1MW" title="OPN1MW">OPN1MW</a>/<a href="/wiki/OPN1MW2" title="OPN1MW2">OPN1MW2</a></li> <li><a href="/wiki/OPN1SW" title="OPN1SW">OPN1SW</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a class="mw-selflink-fragment" href="#Novel_type_2_opsin_groups">nonvisual</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Melanopsin" title="Melanopsin">Melanopsin</a></li> <li><a href="/wiki/OPN3" title="OPN3">OPN3</a></li> <li><a href="/wiki/OPN5" title="OPN5">OPN5</a></li> <li><a href="/wiki/RRH" title="RRH">RRH</a></li> <li><a href="/wiki/RGR_(gene)" class="mw-redirect" title="RGR (gene)">RGR</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite"><a href="/wiki/Crystallin" title="Crystallin">Crystallin</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Alpha_crystallin" class="mw-redirect" title="Alpha crystallin">Alpha</a> (<a href="/wiki/CRYAA" title="CRYAA">A</a></li> <li><a href="/wiki/CRYAB" title="CRYAB">B</a>)</li> <li><a href="/wiki/Beta_gamma_crystallin" class="mw-redirect" title="Beta gamma crystallin">Beta</a> (<a href="/wiki/Crystallin,_beta_A1" title="Crystallin, beta A1">A1</a></li> <li><a href="/w/index.php?title=CRYBA2&amp;action=edit&amp;redlink=1" class="new" title="CRYBA2 (page does not exist)">A2</a></li> <li><a href="/wiki/CRYBA4" title="CRYBA4">A4</a></li> <li><a href="/wiki/CRYBB1" title="CRYBB1">B1</a></li> <li><a href="/wiki/CRYBB2" title="CRYBB2">B2</a></li> <li><a href="/wiki/CRYBB3" title="CRYBB3">B3</a>)</li> <li><a href="/wiki/Beta_gamma_crystallin" class="mw-redirect" title="Beta gamma crystallin">Gamma</a> (<a href="/wiki/CRYGA" title="CRYGA">A</a></li> <li><a href="/wiki/CRYGB" title="CRYGB">B</a></li> <li><a href="/wiki/CRYGC" title="CRYGC">C</a></li> <li><a href="/wiki/Crystallin,_gamma_D" title="Crystallin, gamma D">D</a></li> <li><a href="/w/index.php?title=CRYGN&amp;action=edit&amp;redlink=1" class="new" title="CRYGN (page does not exist)">N</a></li> <li><a href="/wiki/CRYGS" title="CRYGS">S</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%;background-color: AntiqueWhite">Other</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Arrestin" title="Arrestin">Arrestin</a></li> <li><a href="/wiki/Guanylate_cyclase_activator" title="Guanylate cyclase activator">Guanylate cyclase activator</a></li> <li><a href="/wiki/Recoverin" title="Recoverin">Recoverin</a></li> <li><a href="/wiki/Rhodopsin_kinase" title="Rhodopsin kinase">Rhodopsin kinase</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235" /></div><div role="navigation" class="navbox" aria-labelledby="Cell_surface_receptor:_G_protein-coupled_receptors58" style="padding:3px"><table class="nowraplinks mw-collapsible mw-collapsed navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231" /><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:G_protein-coupled_receptors" title="Template:G protein-coupled receptors"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:G_protein-coupled_receptors" title="Template talk:G protein-coupled receptors"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:G_protein-coupled_receptors" title="Special:EditPage/Template:G protein-coupled receptors"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Cell_surface_receptor:_G_protein-coupled_receptors58" style="font-size:114%;margin:0 4em"><a href="/wiki/Cell_surface_receptor" title="Cell surface receptor">Cell surface receptor</a>: <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptors</a></div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Class_A:_Rhodopsin-like58" style="font-size:114%;margin:0 4em"><a href="/wiki/Rhodopsin-like_receptors" title="Rhodopsin-like receptors">Class A</a>: <a href="/wiki/Rhodopsin" title="Rhodopsin">Rhodopsin</a>-like</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Neurotransmitter_receptor" title="Neurotransmitter receptor">Neurotransmitter</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Adrenergic_receptor" title="Adrenergic receptor">Adrenergic</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Alpha-1_adrenergic_receptor" title="Alpha-1 adrenergic receptor">α1</a> (<a href="/wiki/Alpha-1A_adrenergic_receptor" title="Alpha-1A adrenergic receptor">A</a></li> <li><a href="/wiki/Alpha-1B_adrenergic_receptor" title="Alpha-1B adrenergic receptor">B</a></li> <li><a href="/wiki/Alpha-1D_adrenergic_receptor" title="Alpha-1D adrenergic receptor">D</a>)</li> <li><a href="/wiki/Alpha-2_adrenergic_receptor" title="Alpha-2 adrenergic receptor">α2</a> (<a href="/wiki/Alpha-2A_adrenergic_receptor" title="Alpha-2A adrenergic receptor">A</a></li> <li><a href="/wiki/Alpha-2B_adrenergic_receptor" title="Alpha-2B adrenergic receptor">B</a></li> <li><a href="/wiki/Alpha-2C_adrenergic_receptor" title="Alpha-2C adrenergic receptor">C</a>)</li> <li><a href="/wiki/Beta-1_adrenergic_receptor" title="Beta-1 adrenergic receptor">β1</a></li> <li><a href="/wiki/Beta-2_adrenergic_receptor" title="Beta-2 adrenergic receptor">β2</a></li> <li><a href="/wiki/Beta-3_adrenergic_receptor" title="Beta-3 adrenergic receptor">β3</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Purinergic_receptor" title="Purinergic receptor">Purinergic</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Adenosine_receptor" title="Adenosine receptor">Adenosine</a> (<a href="/wiki/Adenosine_A1_receptor" title="Adenosine A1 receptor">A1</a></li> <li><a href="/wiki/Adenosine_A2A_receptor" title="Adenosine A2A receptor">A2A</a></li> <li><a href="/wiki/Adenosine_A2B_receptor" title="Adenosine A2B receptor">A2B</a></li> <li><a href="/wiki/Adenosine_A3_receptor" title="Adenosine A3 receptor">A3</a>)</li> <li><a href="/wiki/P2Y_receptor" title="P2Y receptor">P2Y</a> (<a href="/wiki/P2RY1" title="P2RY1">1</a></li> <li><a href="/wiki/P2RY2" title="P2RY2">2</a></li> <li><a href="/wiki/P2RY4" title="P2RY4">4</a></li> <li><a href="/wiki/LPAR6" title="LPAR6">5</a></li> <li><a href="/wiki/P2RY6" title="P2RY6">6</a></li> <li><a href="/wiki/P2RY8" title="P2RY8">8</a></li> <li><a href="/wiki/GPR23" class="mw-redirect" title="GPR23">9</a></li> <li><a href="/wiki/P2RY10" title="P2RY10">10</a></li> <li><a href="/wiki/P2RY11" title="P2RY11">11</a></li> <li><a href="/wiki/P2Y12" title="P2Y12">12</a></li> <li><a href="/wiki/P2RY13" title="P2RY13">13</a></li> <li><a href="/wiki/P2RY14" title="P2RY14">14</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/5-HT_receptor" title="5-HT receptor">Serotonin</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>(all but <a href="/wiki/5-HT3_receptor" title="5-HT3 receptor">5-HT3</a>)</i> <a href="/wiki/5-HT1_receptor" title="5-HT1 receptor">5-HT1</a> (<a href="/wiki/5-HT1A_receptor" title="5-HT1A receptor">A</a></li> <li><a href="/wiki/5-HT1B_receptor" title="5-HT1B receptor">B</a></li> <li><a href="/wiki/5-HT1D_receptor" title="5-HT1D receptor">D</a></li> <li><a href="/wiki/5-HT1E_receptor" title="5-HT1E receptor">E</a></li> <li><a href="/wiki/5-HT1F_receptor" title="5-HT1F receptor">F</a>)</li> <li><a href="/wiki/5-HT2_receptor" title="5-HT2 receptor">5-HT2</a> (<a href="/wiki/5-HT2A_receptor" title="5-HT2A receptor">A</a></li> <li><a href="/wiki/5-HT2B_receptor" title="5-HT2B receptor">B</a></li> <li><a href="/wiki/5-HT2C_receptor" title="5-HT2C receptor">C</a>)</li> <li><i>5-HT</i> (<a href="/wiki/5-HT4_receptor" title="5-HT4 receptor">4</a></li> <li><a href="/wiki/5-HT5A_receptor" title="5-HT5A receptor">5A</a></li> <li><a href="/wiki/5-HT6_receptor" title="5-HT6 receptor">6</a></li> <li><a href="/wiki/5-HT7_receptor" title="5-HT7 receptor">7</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Muscarinic_acetylcholine_receptor" title="Muscarinic acetylcholine receptor">Acetylcholine</a> (<a href="/wiki/Muscarinic_acetylcholine_receptor_M1" title="Muscarinic acetylcholine receptor M1">M1</a></li> <li><a href="/wiki/Muscarinic_acetylcholine_receptor_M2" title="Muscarinic acetylcholine receptor M2">M2</a></li> <li><a href="/wiki/Muscarinic_acetylcholine_receptor_M3" title="Muscarinic acetylcholine receptor M3">M3</a></li> <li><a href="/wiki/Muscarinic_acetylcholine_receptor_M4" title="Muscarinic acetylcholine receptor M4">M4</a></li> <li><a href="/wiki/Muscarinic_acetylcholine_receptor_M5" title="Muscarinic acetylcholine receptor M5">M5</a>)</li> <li><a href="/wiki/Dopamine_receptor" title="Dopamine receptor">Dopamine</a> <ul><li><a href="/wiki/Dopamine_receptor_D1" title="Dopamine receptor D1">D1</a></li> <li><a href="/wiki/Dopamine_receptor_D2" title="Dopamine receptor D2">D2</a></li> <li><a href="/wiki/Dopamine_receptor_D3" title="Dopamine receptor D3">D3</a></li> <li><a href="/wiki/Dopamine_receptor_D4" title="Dopamine receptor D4">D4</a></li> <li><a href="/wiki/Dopamine_receptor_D5" title="Dopamine receptor D5">D5</a></li></ul></li> <li><a href="/wiki/GHB_receptor" title="GHB receptor">GHB receptor</a></li> <li><a href="/wiki/Histamine_receptor" title="Histamine receptor">Histamine</a> <ul><li><a href="/wiki/Histamine_H1_receptor" title="Histamine H1 receptor">H1</a></li> <li><a href="/wiki/Histamine_H2_receptor" title="Histamine H2 receptor">H2</a></li> <li><a href="/wiki/Histamine_H3_receptor" title="Histamine H3 receptor">H3</a></li> <li><a href="/wiki/Histamine_H4_receptor" title="Histamine H4 receptor">H4</a></li></ul></li> <li><a href="/wiki/Melatonin_receptor" title="Melatonin receptor">Melatonin</a> (<a href="/wiki/Melatonin_receptor_1A" title="Melatonin receptor 1A">1A</a></li> <li><a href="/wiki/Melatonin_receptor_1B" title="Melatonin receptor 1B">1B</a></li> <li><a href="/wiki/Melatonin_receptor_1C" title="Melatonin receptor 1C">1C</a>)</li> <li><a href="/wiki/Trace_amine-associated_receptor" title="Trace amine-associated receptor">TAAR</a> (<a href="/wiki/TAAR1" title="TAAR1">1</a></li> <li><a href="/wiki/TAAR2" title="TAAR2">2</a></li> <li><a href="/wiki/TAAR5" title="TAAR5">5</a></li> <li><a href="/wiki/TAAR6" title="TAAR6">6</a></li> <li><a href="/wiki/TAAR8" title="TAAR8">8</a></li> <li><a href="/wiki/TAAR9" title="TAAR9">9</a>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Metabolites and<br />signaling molecules</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Eicosanoid_receptor" title="Eicosanoid receptor">Eicosanoid</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>CysLT</i> (<a href="/wiki/Cysteinyl_leukotriene_receptor_1" title="Cysteinyl leukotriene receptor 1">1</a></li> <li><a href="/wiki/Cysteinyl_leukotriene_receptor_2" title="Cysteinyl leukotriene receptor 2">2</a>)</li> <li><a href="/wiki/Leukotriene_B4" title="Leukotriene B4">LTB4</a> <ul><li><a href="/wiki/Leukotriene_B4_receptor" title="Leukotriene B4 receptor">1</a></li> <li><a href="/wiki/Leukotriene_B4_receptor_2" title="Leukotriene B4 receptor 2">2</a></li></ul></li> <li><a href="/wiki/Formyl_peptide_receptor_2" title="Formyl peptide receptor 2"> FPRL1</a></li> <li><a href="/wiki/Oxoeicosanoid_receptor_1" title="Oxoeicosanoid receptor 1">OXE</a></li> <li><a href="/wiki/Prostaglandin_receptor" title="Prostaglandin receptor">Prostaglandin</a> <ul><li><i>DP</i> (<a href="/wiki/Prostaglandin_D2_receptor" title="Prostaglandin D2 receptor">1</a></li> <li><a href="/wiki/GPR44" class="mw-redirect" title="GPR44">2</a>), <i>EP</i> (<a href="/wiki/EP1_receptor" class="mw-redirect" title="EP1 receptor">1</a></li> <li><a href="/wiki/Prostaglandin_E2_receptor" title="Prostaglandin E2 receptor">2</a></li> <li><a href="/wiki/Prostaglandin_E_receptor_3" class="mw-redirect" title="Prostaglandin E receptor 3">3</a></li> <li><a href="/wiki/EP4_receptor" class="mw-redirect" title="EP4 receptor">4</a>), <a href="/wiki/Prostaglandin_F_receptor" title="Prostaglandin F receptor">FP</a></li></ul></li> <li><a href="/wiki/Prostacyclin_receptor" title="Prostacyclin receptor">Prostacyclin</a></li> <li><a href="/wiki/Thromboxane_receptor" title="Thromboxane receptor">Thromboxane</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/G_protein-coupled_bile_acid_receptor" title="G protein-coupled bile acid receptor">Bile acid</a></li> <li><a href="/wiki/Cannabinoid_receptor" title="Cannabinoid receptor">Cannabinoid</a> (<a href="/wiki/Cannabinoid_receptor_type_1" class="mw-redirect" title="Cannabinoid receptor type 1">CB1</a></li> <li><a href="/wiki/Cannabinoid_receptor_type_2" class="mw-redirect" title="Cannabinoid receptor type 2">CB2</a>, <i>GPR</i> (<a href="/wiki/GPR18" class="mw-redirect" title="GPR18">18</a></li> <li><a href="/wiki/GPR55" title="GPR55">55</a></li> <li><a href="/wiki/GPR119" title="GPR119">119</a>))</li> <li><a href="/wiki/GPR183" title="GPR183">EBI2</a></li> <li><a href="/wiki/GPER" title="GPER">Estrogen</a></li> <li><a href="/wiki/Free_fatty_acid_receptor" title="Free fatty acid receptor">Free fatty acid</a> (<a href="/wiki/Free_fatty_acid_receptor_1" title="Free fatty acid receptor 1">1</a></li> <li><a href="/wiki/Free_fatty_acid_receptor_2" title="Free fatty acid receptor 2">2</a></li> <li><a href="/wiki/Free_fatty_acid_receptor_3" title="Free fatty acid receptor 3">3</a></li> <li><a href="/wiki/GPR42" title="GPR42">4</a>)</li> <li><a href="/wiki/Hydroxycarboxylic_acid_receptor" title="Hydroxycarboxylic acid receptor">Hydroxycarboxylic acids</a> <ul><li><a href="/wiki/Hydroxycarboxylic_acid_receptor_1" title="Hydroxycarboxylic acid receptor 1">1</a></li> <li><a href="/wiki/Hydroxycarboxylic_acid_receptor_2" title="Hydroxycarboxylic acid receptor 2">2</a></li> <li><a href="/wiki/Hydroxycarboxylic_acid_receptor_3" title="Hydroxycarboxylic acid receptor 3">3</a></li></ul></li> <li><a href="/wiki/Lysophosphatidic_acid" title="Lysophosphatidic acid">Lysophosphatidic acid</a> (<a href="/wiki/LPAR1" title="LPAR1">1</a></li> <li><a href="/wiki/LPAR2" title="LPAR2">2</a></li> <li><a href="/wiki/LPAR3" title="LPAR3">3</a></li> <li><a href="/wiki/LPAR4" title="LPAR4">4</a></li> <li><a href="/wiki/LPAR5" title="LPAR5">5</a></li> <li><a href="/wiki/LPAR6" title="LPAR6">6</a>)</li> <li><a href="/wiki/Lysophospholipid_receptor" title="Lysophospholipid receptor">Lysophospholipid</a> (<a href="/wiki/S1PR1" title="S1PR1">1</a></li> <li><a href="/wiki/LPAR1" title="LPAR1">2</a></li> <li><a href="/wiki/S1PR3" title="S1PR3">3</a></li> <li><a href="/wiki/LPAR2" title="LPAR2">4</a></li> <li><a href="/wiki/S1PR2" title="S1PR2">5</a></li> <li><a href="/wiki/S1PR4" title="S1PR4">6</a></li> <li><a href="/wiki/LPAR3" title="LPAR3">7</a></li> <li><a href="/wiki/S1PR5" title="S1PR5">8</a>)</li> <li><a href="/wiki/OXGR1" title="OXGR1">Oxoglutarate</a></li> <li><a href="/wiki/Platelet-activating_factor_receptor" title="Platelet-activating factor receptor">PAF</a></li> <li><a href="/wiki/Sphingosine-1-phosphate" title="Sphingosine-1-phosphate">Sphingosine-1-phosphate</a> (<a href="/wiki/S1PR1" title="S1PR1">1</a></li> <li><a href="/wiki/S1PR2" title="S1PR2">2</a></li> <li><a href="/wiki/S1PR3" title="S1PR3">3</a></li> <li><a href="/wiki/S1PR4" title="S1PR4">4</a></li> <li><a href="/wiki/S1PR5" title="S1PR5">5</a>)</li> <li><a href="/wiki/SUCNR1" title="SUCNR1">Succinate</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Peptide</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/GPCR_neuropeptide_receptor" title="GPCR neuropeptide receptor">Neuropeptide</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Neuropeptide_B/W_receptor" title="Neuropeptide B/W receptor">B/W</a> (<a href="/wiki/Neuropeptides_B/W_receptor_1" title="Neuropeptides B/W receptor 1">1</a></li> <li><a href="/wiki/Neuropeptides_B/W_receptor_2" title="Neuropeptides B/W receptor 2">2</a>)</li> <li><a href="/wiki/Neuropeptide_FF_receptor" title="Neuropeptide FF receptor">FF</a> (<a href="/wiki/Neuropeptide_FF_receptor_1" title="Neuropeptide FF receptor 1">1</a></li> <li><a href="/wiki/Neuropeptide_FF_receptor_2" title="Neuropeptide FF receptor 2">2</a>)</li> <li><a href="/wiki/Neuropeptide_S_receptor" title="Neuropeptide S receptor">S</a></li> <li><a href="/wiki/Neuropeptide_Y_receptor" title="Neuropeptide Y receptor">Y</a> (<a href="/wiki/Neuropeptide_Y_receptor_Y1" title="Neuropeptide Y receptor Y1">1</a></li> <li><a href="/wiki/Neuropeptide_Y_receptor_Y2" title="Neuropeptide Y receptor Y2">2</a></li> <li><a href="/wiki/Pancreatic_polypeptide_receptor_1" title="Pancreatic polypeptide receptor 1">4</a></li> <li><a href="/wiki/Neuropeptide_Y_receptor_Y5" title="Neuropeptide Y receptor Y5">5</a>)</li> <li><i>Neuromedin</i> (<a href="/wiki/Neuromedin_B_receptor" title="Neuromedin B receptor">B</a></li> <li><a href="/wiki/Neuromedin_U_receptor" title="Neuromedin U receptor">U</a> (<a href="/wiki/Neuromedin_U_receptor_1" title="Neuromedin U receptor 1">1</a></li> <li><a href="/wiki/Neuromedin_U_receptor_2" title="Neuromedin U receptor 2">2</a>))</li> <li><a href="/wiki/Neurotensin_receptor" title="Neurotensin receptor">Neurotensin</a> (<a href="/wiki/Neurotensin_receptor_1" title="Neurotensin receptor 1">1</a></li> <li><a href="/wiki/Neurotensin_receptor_2" title="Neurotensin receptor 2">2</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Anaphylatoxin_receptors" title="Anaphylatoxin receptors">Anaphylatoxin</a> (<a href="/wiki/C3a_receptor" title="C3a receptor">C3a</a></li> <li>C5a (<a href="/wiki/C5a_receptor" title="C5a receptor">1</a></li> <li><a href="/wiki/C5AR2" title="C5AR2">2</a>))</li> <li><a href="/wiki/Angiotensin_receptor" class="mw-redirect" title="Angiotensin receptor">Angiotensin</a> (<a href="/wiki/Angiotensin_II_receptor_type_1" title="Angiotensin II receptor type 1">1</a></li> <li><a href="/wiki/Angiotensin_II_receptor_type_2" title="Angiotensin II receptor type 2">2</a>)</li> <li><a href="/wiki/Apelin_receptor" title="Apelin receptor">Apelin</a></li> <li><a href="/wiki/Bombesin_receptor" title="Bombesin receptor">Bombesin</a> <ul><li><a href="/wiki/Bombesin-like_receptor_3" title="Bombesin-like receptor 3">BRS3</a></li> <li><a href="/wiki/Gastrin-releasing_peptide_receptor" title="Gastrin-releasing peptide receptor">GRPR</a></li> <li><a href="/wiki/Neuromedin_B_receptor" title="Neuromedin B receptor">NMBR</a>)</li> <li><a href="/wiki/Bradykinin_receptor" title="Bradykinin receptor">Bradykinin</a> (<a href="/wiki/Bradykinin_receptor_B1" title="Bradykinin receptor B1">B1</a></li> <li><a href="/wiki/Bradykinin_receptor_B2" title="Bradykinin receptor B2">B2</a>)</li></ul></li> <li><a href="/wiki/Chemokine_receptor" title="Chemokine receptor">Chemokine</a></li> <li><a href="/wiki/Cholecystokinin_receptor" title="Cholecystokinin receptor">Cholecystokinin</a> (<a href="/wiki/Cholecystokinin_A_receptor" title="Cholecystokinin A receptor">A</a></li> <li><a href="/wiki/Cholecystokinin_B_receptor" title="Cholecystokinin B receptor">B</a>)</li> <li><a href="/wiki/Endothelin_receptor" title="Endothelin receptor">Endothelin</a> <ul><li><a href="/wiki/Endothelin_A_receptor" title="Endothelin A receptor">A</a></li> <li><a href="/wiki/Endothelin_B_receptor" class="mw-redirect" title="Endothelin B receptor">B</a></li></ul></li> <li><a href="/wiki/Formyl_peptide_receptor" title="Formyl peptide receptor">Formyl peptide</a> (<a href="/wiki/Formyl_peptide_receptor_1" title="Formyl peptide receptor 1">1</a></li> <li><a href="/wiki/Formyl_peptide_receptor_2" title="Formyl peptide receptor 2">2</a></li> <li><a href="/wiki/Formyl_peptide_receptor_3" title="Formyl peptide receptor 3">3</a>)</li> <li><a href="/wiki/Follicle-stimulating_hormone_receptor" title="Follicle-stimulating hormone receptor">FSH</a></li> <li><a href="/wiki/Galanin_receptor" title="Galanin receptor">Galanin</a> (<a href="/wiki/Galanin_receptor_1" title="Galanin receptor 1">1</a></li> <li><a href="/wiki/Galanin_receptor_2" title="Galanin receptor 2">2</a></li> <li><a href="/wiki/Galanin_receptor_3" title="Galanin receptor 3">3</a>)</li> <li><a href="/wiki/Gonadotropin-releasing_hormone_receptor" title="Gonadotropin-releasing hormone receptor">Gonadotropin-releasing hormone</a> (<a href="/wiki/GNRHR" title="GNRHR">1</a></li> <li><a href="/wiki/GNRHR2" title="GNRHR2">2</a>)</li> <li><a href="/wiki/Growth_hormone_secretagogue_receptor" title="Growth hormone secretagogue receptor">Ghrelin</a></li> <li><a href="/wiki/KiSS1-derived_peptide_receptor" title="KiSS1-derived peptide receptor"> Kisspeptin</a></li> <li><a href="/wiki/Luteinizing_hormone/choriogonadotropin_receptor" title="Luteinizing hormone/choriogonadotropin receptor">Luteinizing hormone/choriogonadotropin</a></li> <li><a href="/wiki/MAS1_oncogene" title="MAS1 oncogene">MAS</a> (<a href="/wiki/MAS1" title="MAS1">1</a></li> <li><a href="/wiki/MAS1L" title="MAS1L">1L</a></li> <li><a href="/wiki/MRGPRD" title="MRGPRD">D</a></li> <li><a href="/wiki/MRGPRE" title="MRGPRE">E</a></li> <li><a href="/wiki/MRGPRF" title="MRGPRF">F</a></li> <li><a href="/wiki/MRGPRG" title="MRGPRG">G</a></li> <li><a href="/wiki/MRGPRX1" title="MRGPRX1">X1</a></li> <li><a href="/wiki/MRGPRX2" title="MRGPRX2">X2</a></li> <li><a href="/wiki/MRGPRX3" title="MRGPRX3">X3</a></li> <li><a href="/wiki/MRGPRX4" title="MRGPRX4">X4</a>)</li> <li><a href="/wiki/Melanocortin_receptor" title="Melanocortin receptor">Melanocortin</a> (<a href="/wiki/Melanocortin_1_receptor" title="Melanocortin 1 receptor">1</a></li> <li><a href="/wiki/ACTH_receptor" title="ACTH receptor">2</a></li> <li><a href="/wiki/Melanocortin_3_receptor" title="Melanocortin 3 receptor">3</a></li> <li><a href="/wiki/Melanocortin_4_receptor" title="Melanocortin 4 receptor">4</a></li> <li><a href="/wiki/Melanocortin_5_receptor" title="Melanocortin 5 receptor">5</a>)</li> <li><a href="/wiki/Melanin-concentrating_hormone_receptor" title="Melanin-concentrating hormone receptor">MCHR</a> (<a href="/wiki/Melanin-concentrating_hormone_receptor_1" title="Melanin-concentrating hormone receptor 1">1</a></li> <li><a href="/wiki/Melanin-concentrating_hormone_receptor_2" title="Melanin-concentrating hormone receptor 2">2</a>)</li> <li><a href="/wiki/Motilin_receptor" title="Motilin receptor">Motilin</a></li> <li><a href="/wiki/Opioid_receptor" title="Opioid receptor">Opioid</a> (<a href="/wiki/%CE%94-opioid_receptor" title="Δ-opioid receptor">Delta</a></li> <li><a href="/wiki/%CE%9A-opioid_receptor" title="Κ-opioid receptor">Kappa</a></li> <li><a href="/wiki/%CE%9C-opioid_receptor" title="Μ-opioid receptor">Mu</a></li> <li><a href="/wiki/Nociceptin_receptor" title="Nociceptin receptor">Nociceptin</a> &amp; <a href="/wiki/OGFr" title="OGFr">Zeta</a>, but not <a href="/wiki/Sigma_receptor" title="Sigma receptor">Sigma</a>)</li> <li><a href="/wiki/Orexin_receptor" title="Orexin receptor">Orexin</a> (<a href="/wiki/Hypocretin_(orexin)_receptor_1" title="Hypocretin (orexin) receptor 1">1</a></li> <li><a href="/wiki/Hypocretin_(orexin)_receptor_2" title="Hypocretin (orexin) receptor 2">2</a>)</li> <li><a href="/wiki/Oxytocin_receptor" title="Oxytocin receptor">Oxytocin</a></li> <li><a href="/wiki/Prokineticin_receptor" title="Prokineticin receptor">Prokineticin</a> (<a href="/wiki/Prokineticin_receptor_1" title="Prokineticin receptor 1">1</a></li> <li><a href="/wiki/Prokineticin_receptor_2" title="Prokineticin receptor 2">2</a>)</li> <li><a href="/wiki/Prolactin-releasing_peptide_receptor" title="Prolactin-releasing peptide receptor">Prolactin-releasing peptide</a></li> <li><a href="/wiki/Relaxin_receptor" title="Relaxin receptor">Relaxin</a> (<a href="/wiki/Relaxin/insulin-like_family_peptide_receptor_1" title="Relaxin/insulin-like family peptide receptor 1">1</a></li> <li><a href="/wiki/Relaxin/insulin-like_family_peptide_receptor_2" title="Relaxin/insulin-like family peptide receptor 2">2</a></li> <li><a href="/wiki/Relaxin/insulin-like_family_peptide_receptor_3" title="Relaxin/insulin-like family peptide receptor 3">3</a></li> <li><a href="/wiki/Relaxin/insulin-like_family_peptide_receptor_4" title="Relaxin/insulin-like family peptide receptor 4">4</a>)</li> <li><a href="/wiki/Somatostatin_receptor" title="Somatostatin receptor">Somatostatin</a> (<a href="/wiki/Somatostatin_receptor_1" title="Somatostatin receptor 1">1</a></li> <li><a href="/wiki/Somatostatin_receptor_2" title="Somatostatin receptor 2">2</a></li> <li><a href="/wiki/Somatostatin_receptor_3" title="Somatostatin receptor 3">3</a></li> <li><a href="/wiki/Somatostatin_receptor_4" title="Somatostatin receptor 4">4</a></li> <li><a href="/wiki/Somatostatin_receptor_5" title="Somatostatin receptor 5">5</a>)</li> <li><a href="/wiki/Tachykinin_receptor" title="Tachykinin receptor">Tachykinin</a> (<a href="/wiki/Tachykinin_receptor_1" title="Tachykinin receptor 1">1</a></li> <li><a href="/wiki/Tachykinin_receptor_2" title="Tachykinin receptor 2">2</a></li> <li><a href="/wiki/Tachykinin_receptor_3" title="Tachykinin receptor 3">3</a>)</li> <li><a href="/wiki/Thyrotropin_receptor" title="Thyrotropin receptor">Thyrotropin</a></li> <li><a href="/wiki/Thyrotropin-releasing_hormone_receptor" title="Thyrotropin-releasing hormone receptor">Thyrotropin-releasing hormone</a></li> <li><a href="/wiki/Urotensin-II_receptor" title="Urotensin-II receptor">Urotensin-II</a></li> <li><a href="/wiki/Vasopressin_receptor" title="Vasopressin receptor">Vasopressin</a> (<a href="/wiki/Arginine_vasopressin_receptor_1A" class="mw-redirect" title="Arginine vasopressin receptor 1A">1A</a></li> <li><a href="/wiki/Arginine_vasopressin_receptor_1B" class="mw-redirect" title="Arginine vasopressin receptor 1B">1B</a></li> <li><a href="/wiki/Arginine_vasopressin_receptor_2" class="mw-redirect" title="Arginine vasopressin receptor 2">2</a>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;">Miscellaneous</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Taste_receptor" title="Taste receptor">Taste</a>, bitter</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>TAS2R</i> <ul><li><a href="/wiki/TAS2R1" title="TAS2R1">1</a></li> <li><a href="/wiki/TAS2R3" title="TAS2R3">3</a></li> <li><a href="/wiki/TAS2R4" title="TAS2R4">4</a></li> <li><a href="/wiki/TAS2R5" title="TAS2R5">5</a></li> <li><a href="/wiki/TAS2R7" title="TAS2R7">7</a></li> <li><a href="/wiki/TAS2R8" title="TAS2R8">8</a></li> <li><a href="/wiki/TAS2R9" title="TAS2R9">9</a></li> <li><a href="/wiki/TAS2R10" title="TAS2R10">10</a></li> <li><a href="/wiki/TAS2R13" title="TAS2R13">13</a></li> <li><a href="/wiki/TAS2R14" title="TAS2R14">14</a></li> <li><a href="/wiki/TAS2R16" title="TAS2R16">16</a></li> <li><a href="/wiki/TAS2R19" title="TAS2R19">19</a></li> <li><a href="/wiki/TAS2R20" title="TAS2R20">20</a></li> <li><a href="/wiki/TAS2R30" title="TAS2R30">30</a></li> <li><a href="/wiki/TAS2R31" title="TAS2R31">31</a></li> <li><a href="/wiki/TAS2R38" title="TAS2R38">38</a></li> <li><a href="/wiki/TAS2R39" title="TAS2R39">39</a></li> <li><a href="/wiki/TAS2R40" title="TAS2R40">40</a></li> <li><a href="/wiki/TAS2R41" title="TAS2R41">41</a></li> <li><a href="/wiki/TAS2R42" title="TAS2R42">42</a></li> <li><a href="/wiki/TAS2R43" title="TAS2R43">43</a></li> <li><a href="/wiki/TAS2R45" title="TAS2R45">45</a></li> <li><a href="/wiki/TAS2R46" title="TAS2R46">46</a></li> <li><a href="/wiki/TAS2R50" title="TAS2R50">50</a></li> <li><a href="/wiki/TAS2R60" title="TAS2R60">60</a></li></ul></li> <li><a href="/wiki/Vomeronasal_receptor" title="Vomeronasal receptor">Vomeronasal receptor</a> type 1</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><a href="/wiki/Orphan_receptor" title="Orphan receptor">Orphan</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>GPR</i> (<a href="/wiki/GPR1" title="GPR1">1</a></li> <li><a href="/wiki/GPR3" title="GPR3">3</a></li> <li><a href="/wiki/GPR4" title="GPR4">4</a></li> <li><a href="/wiki/GPR6" title="GPR6">6</a></li> <li><a href="/wiki/GPR12" title="GPR12">12</a></li> <li><a href="/wiki/GPR15" title="GPR15">15</a></li> <li><a href="/wiki/GPR17" title="GPR17">17</a></li> <li><a href="/wiki/GPR18" class="mw-redirect" title="GPR18">18</a></li> <li><a href="/wiki/GPR19" title="GPR19">19</a></li> <li><a href="/wiki/GPR20" title="GPR20">20</a></li> <li><a href="/wiki/GPR21" title="GPR21">21</a></li> <li><a href="/wiki/GPR22" title="GPR22">22</a></li> <li><a href="/wiki/LPAR4" title="LPAR4">23</a></li> <li><a href="/wiki/GPR25" title="GPR25">25</a></li> <li><a href="/wiki/GPR26" title="GPR26">26</a></li> <li><a href="/wiki/GPR27" title="GPR27">27</a></li> <li><a href="/wiki/GPR31" title="GPR31">31</a></li> <li><a href="/wiki/GPR32" title="GPR32">32</a></li> <li><a href="/wiki/GPR33" title="GPR33">33</a></li> <li><a href="/wiki/GPR34" title="GPR34">34</a></li> <li><a href="/wiki/GPR35" title="GPR35">35</a></li> <li><a href="/wiki/GPR37" title="GPR37">37</a></li> <li><a href="/wiki/GPR39" title="GPR39">39</a></li> <li><a href="/wiki/GPR42" title="GPR42">42</a></li> <li><a href="/wiki/GPR44" class="mw-redirect" title="GPR44">44</a></li> <li><a href="/wiki/GPR45" title="GPR45">45</a></li> <li><a href="/wiki/GPR50" title="GPR50">50</a></li> <li><a href="/wiki/GPR52" title="GPR52">52</a></li> <li><a href="/wiki/GPR55" title="GPR55">55</a></li> <li><a href="/wiki/GPR61" title="GPR61">61</a></li> <li><a href="/wiki/GPR62" title="GPR62">62</a></li> <li><a href="/wiki/GPR63" title="GPR63">63</a></li> <li><a href="/wiki/GPR65" title="GPR65">65</a></li> <li><a href="/wiki/GPR68" title="GPR68">68</a></li> <li><a href="/wiki/GPR75" title="GPR75">75</a></li> <li><a href="/wiki/GPR78" title="GPR78">78</a></li> <li><a href="/wiki/GPR81" class="mw-redirect" title="GPR81">81</a></li> <li><a href="/wiki/GPR82" title="GPR82">82</a></li> <li><a href="/wiki/GPR83" title="GPR83">83</a></li> <li><a href="/wiki/GPR84" title="GPR84">84</a></li> <li><a href="/wiki/GPR85" title="GPR85">85</a></li> <li><a href="/wiki/GPR87" title="GPR87">87</a></li> <li><a href="/wiki/GPR88" title="GPR88">88</a></li> <li><a href="/wiki/LPAR5" title="LPAR5">92</a></li> <li><a href="/wiki/GPR101" title="GPR101">101</a></li> <li><a href="/wiki/Pyroglutamylated_RFamide_peptide_receptor" title="Pyroglutamylated RFamide peptide receptor">103</a></li> <li><a href="/wiki/Niacin_receptor_1" class="mw-redirect" title="Niacin receptor 1">109A</a></li> <li><a href="/wiki/Niacin_receptor_2" class="mw-redirect" title="Niacin receptor 2">109B</a></li> <li><a href="/wiki/GPR119" title="GPR119">119</a></li> <li><a href="/wiki/GPR120" class="mw-redirect" title="GPR120">120</a></li> <li><a href="/wiki/GPR132" title="GPR132">132</a></li> <li><a href="/wiki/GPR135" title="GPR135">135</a></li> <li><a href="/wiki/GPR137B" title="GPR137B">137B</a></li> <li><a href="/wiki/GPR139" title="GPR139">139</a></li> <li><a href="/wiki/GPR141" title="GPR141">141</a></li> <li><a href="/wiki/GPR142" title="GPR142">142</a></li> <li><a href="/wiki/GPR146" title="GPR146">146</a></li> <li><a href="/wiki/GPR148" title="GPR148">148</a></li> <li><a href="/wiki/GPR149" title="GPR149">149</a></li> <li><a href="/wiki/GPR150" title="GPR150">150</a></li> <li><a href="/wiki/GPR151" title="GPR151">151</a></li> <li><a href="/wiki/GPR152" title="GPR152">152</a></li> <li><a href="/wiki/GPR153" title="GPR153">153</a></li> <li><a href="/wiki/GPR160" title="GPR160">160</a></li> <li><a href="/wiki/GPR161" title="GPR161">161</a></li> <li><a href="/wiki/GPR162" title="GPR162">162</a></li> <li><a href="/wiki/GPR171" title="GPR171">171</a></li> <li><a href="/wiki/GPR173" title="GPR173">173</a></li> <li><a href="/wiki/GPR174" title="GPR174">174</a></li> <li><a href="/wiki/GPR176" title="GPR176">176</a></li> <li><a href="/wiki/GPR177" class="mw-redirect" title="GPR177">177</a></li> <li><a href="/wiki/GPR182" title="GPR182">182</a></li> <li><a href="/wiki/GPR183" title="GPR183">183</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:7em;text-align:left;"><i>Other</i></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/GPR182" title="GPR182">Adrenomedullin</a></li> <li><a href="/wiki/Olfactory_receptor" title="Olfactory receptor">Olfactory</a></li> <li><a class="mw-selflink selflink">Opsin</a> (<a href="/wiki/OPN3" title="OPN3">3</a></li> <li><a href="/wiki/Melanopsin" title="Melanopsin">4</a></li> <li><a href="/wiki/OPN5" title="OPN5">5</a></li> <li><a href="/wiki/OPN1LW" title="OPN1LW">1LW</a></li> <li><a href="/wiki/OPN1MW" title="OPN1MW">1MW</a></li> <li><a href="/wiki/OPN1SW" title="OPN1SW">1SW</a></li> <li><a href="/wiki/Retinal_G_protein_coupled_receptor" title="Retinal G protein coupled receptor">RGR</a></li> <li><a href="/wiki/RRH" title="RRH">RRH</a>)</li> <li><a href="/wiki/Protease-activated_receptor" title="Protease-activated receptor">Protease-activated</a> (<a href="/wiki/Coagulation_factor_II_receptor" class="mw-redirect" title="Coagulation factor II receptor">1</a></li> <li><a href="/wiki/Protease_activated_receptor_2" class="mw-redirect" title="Protease activated receptor 2">2</a></li> <li><a href="/wiki/F2RL2" title="F2RL2">3</a></li> <li><a href="/wiki/F2RL3" title="F2RL3">4</a>)</li> <li><a href="/wiki/Super_Conserved_Receptor_Expressed_in_Brain" title="Super Conserved Receptor Expressed in Brain">SREB</a> (<a href="/wiki/GPR27" title="GPR27">1</a></li> <li><a href="/wiki/GPR85" title="GPR85">2</a></li> <li><a href="/wiki/GPR173" title="GPR173">3</a>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Class_B:_Secretin-like58" style="font-size:114%;margin:0 4em"><a href="/wiki/Secretin_receptor_family" title="Secretin receptor family">Class B</a>: <a href="/wiki/Secretin_receptor" title="Secretin receptor">Secretin</a>-like</div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;"><a href="/wiki/Adhesion_G_protein-coupled_receptor" title="Adhesion G protein-coupled receptor">Adhesion</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>ADGRB</i> <ul><li><a href="/wiki/Brain-specific_angiogenesis_inhibitor" title="Brain-specific angiogenesis inhibitor">Brain-specific angiogenesis inhibitor</a> <ul><li><a href="/wiki/Brain-specific_angiogenesis_inhibitor_1" title="Brain-specific angiogenesis inhibitor 1">1</a></li> <li><a href="/wiki/Brain-specific_angiogenesis_inhibitor_2" title="Brain-specific angiogenesis inhibitor 2">2</a></li> <li><a href="/wiki/Brain-specific_angiogenesis_inhibitor_3" title="Brain-specific angiogenesis inhibitor 3">3</a></li></ul></li></ul></li> <li><i>ADGRC</i> <ul><li><a href="/wiki/Flamingo_(protein)" title="Flamingo (protein)">Cadherin</a> <ul><li><a href="/wiki/CELSR1" title="CELSR1">1</a></li> <li><a href="/wiki/CELSR2" title="CELSR2">2</a></li> <li><a href="/wiki/CELSR3" title="CELSR3">3</a></li></ul></li></ul></li> <li><i>ADGRE</i> <ul><li><a href="/wiki/EGF_module-containing_mucin-like_hormone_receptor" title="EGF module-containing mucin-like hormone receptor">EMR</a> <ul><li><a href="/wiki/EMR1" title="EMR1">1</a></li> <li><a href="/wiki/EMR2" title="EMR2">2</a></li> <li><a href="/wiki/EMR3" title="EMR3">3</a></li></ul></li> <li><a href="/wiki/CD97" title="CD97">CD97</a></li></ul></li> <li><i>ADGRG</i> <ul><li><a href="/wiki/GPR56" title="GPR56">1</a></li> <li><a href="/wiki/GPR64" title="GPR64">2</a></li> <li><a href="/wiki/GPR97" title="GPR97">3</a></li> <li><a href="/wiki/GPR112" title="GPR112">4</a></li> <li><a href="/wiki/GPR114" title="GPR114">5</a></li> <li><a href="/wiki/GPR126" title="GPR126">6</a></li> <li><a href="/wiki/GPR128" title="GPR128">7</a></li></ul></li> <li><i>ADGRL</i> <ul><li><a href="/wiki/Latrophilin_receptor" class="mw-redirect" title="Latrophilin receptor">Latrophilin</a> <ul><li><a href="/wiki/Latrophilin_1" title="Latrophilin 1">1</a></li> <li><a href="/wiki/Latrophilin_2" title="Latrophilin 2">2</a></li> <li><a href="/wiki/Latrophilin_3" title="Latrophilin 3">3</a></li></ul></li> <li><a href="/wiki/ELTD1" class="mw-redirect" title="ELTD1">ELTD1</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;"><a href="/wiki/Orphan_receptor" title="Orphan receptor">Orphan</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>GPR</i> (<a href="/wiki/GPR56" title="GPR56">56</a></li> <li><a href="/wiki/GPR64" title="GPR64">64</a></li> <li><a href="/wiki/GPR97" title="GPR97">97</a></li> <li><a href="/wiki/GPR98" title="GPR98">98</a></li> <li><a href="/wiki/GPR110" title="GPR110">110</a></li> <li><a href="/wiki/GPR111" title="GPR111">111</a></li> <li><a href="/wiki/GPR112" title="GPR112">112</a></li> <li><a href="/wiki/GPR113" title="GPR113">113</a></li> <li><a href="/wiki/GPR114" title="GPR114">114</a></li> <li><a href="/wiki/GPR115" title="GPR115">115</a></li> <li><a href="/wiki/GPR116" title="GPR116">116</a></li> <li><a href="/wiki/GPR123" title="GPR123">123</a></li> <li><a href="/wiki/GPR124" title="GPR124">124</a></li> <li><a href="/wiki/GPR125" title="GPR125">125</a></li> <li><a href="/wiki/GPR126" title="GPR126">126</a></li> <li><a href="/wiki/GPR128" title="GPR128">128</a></li> <li><a href="/wiki/GPR133" title="GPR133">133</a></li> <li><a href="/wiki/GPR143" title="GPR143">143</a></li> <li><a href="/wiki/GPR144" title="GPR144">144</a></li> <li><a href="/wiki/GPR155" title="GPR155">155</a></li> <li><a href="/wiki/GPR157" title="GPR157">157</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;"><i>Other</i></th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Calcitonin_receptor" title="Calcitonin receptor">Calcitonin</a></li> <li><a href="/wiki/CALCRL" title="CALCRL">CALCRL</a></li> <li><a href="/wiki/Corticotropin-releasing_hormone_receptor" title="Corticotropin-releasing hormone receptor">Corticotropin-releasing hormone</a> (<a href="/wiki/Corticotropin-releasing_hormone_receptor_1" title="Corticotropin-releasing hormone receptor 1">1</a></li> <li><a href="/wiki/Corticotropin-releasing_hormone_receptor_2" title="Corticotropin-releasing hormone receptor 2">2</a>)</li> <li><a href="/wiki/Glucagon_receptor_family" title="Glucagon receptor family">Glucagon</a> (<a href="/wiki/Glucagon_receptor" title="Glucagon receptor">GR</a></li> <li><a href="/wiki/Gastric_inhibitory_polypeptide_receptor" title="Gastric inhibitory polypeptide receptor">GIPR</a></li> <li><a href="/wiki/Glucagon-like_peptide-1_receptor" title="Glucagon-like peptide-1 receptor">GLP1R</a></li> <li><a href="/wiki/Glucagon-like_peptide-2_receptor" title="Glucagon-like peptide-2 receptor">GLP2R</a>)</li> <li><a href="/wiki/Growth-hormone-releasing_hormone_receptor" title="Growth-hormone-releasing hormone receptor">Growth-hormone-releasing hormone</a></li> <li><a href="/wiki/ADCYAP1R1" title="ADCYAP1R1">PACAPR1</a></li> <li><a href="/wiki/Orphan_receptor" title="Orphan receptor">GPR</a></li> <li><a href="/wiki/Methuselah-like_proteins" title="Methuselah-like proteins">Methuselah-like proteins</a></li> <li><a href="/wiki/Parathyroid_hormone_receptor" title="Parathyroid hormone receptor">Parathyroid hormone</a> (<a href="/wiki/Parathyroid_hormone_1_receptor" title="Parathyroid hormone 1 receptor">1</a></li> <li><a href="/wiki/Parathyroid_hormone_2_receptor" title="Parathyroid hormone 2 receptor">2</a>)</li> <li><a href="/wiki/Secretin_receptor" title="Secretin receptor">Secretin</a></li> <li><a href="/wiki/Vasoactive_intestinal_peptide_receptor" title="Vasoactive intestinal peptide receptor">Vasoactive intestinal peptide</a> (<a href="/wiki/VIPR1" title="VIPR1">1</a></li> <li><a href="/wiki/VIPR2" title="VIPR2">2</a>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Class_C:_Metabotropic_glutamate_/_pheromone58" style="font-size:114%;margin:0 4em"><a href="/wiki/Class_C_GPCR" title="Class C GPCR">Class C</a>: <a href="/wiki/Metabotropic_receptor" title="Metabotropic receptor">Metabotropic</a> <a href="/wiki/Metabotropic_glutamate_receptor" title="Metabotropic glutamate receptor">glutamate</a> / <a href="/wiki/Pheromone" title="Pheromone">pheromone</a></div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;"><a href="/wiki/Taste_receptor" title="Taste receptor">Taste</a>, sweet</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><i>TAS1R</i> <ul><li><a href="/wiki/TAS1R1" title="TAS1R1">1</a></li> <li><a href="/wiki/TAS1R2" title="TAS1R2">2</a></li> <li><a href="/wiki/TAS1R3" title="TAS1R3">3</a></li></ul></li> <li><a href="/wiki/Vomeronasal_receptor" title="Vomeronasal receptor">Vomeronasal receptor</a>, type 2</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;"><i>Other</i></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Calcium-sensing_receptor" title="Calcium-sensing receptor">Calcium-sensing receptor</a></li> <li><a href="/wiki/GABA_receptor" title="GABA receptor">GABA<sub>B</sub></a> (<a href="/wiki/GABBR1" title="GABBR1">1</a></li> <li><a href="/wiki/GABBR2" title="GABBR2">2</a>)</li> <li><a href="/wiki/Glutamate_receptor" title="Glutamate receptor">Glutamate receptor</a> (<a href="/wiki/Metabotropic_glutamate_receptor" title="Metabotropic glutamate receptor">Metabotropic glutamate</a> (<a href="/wiki/Metabotropic_glutamate_receptor_1" title="Metabotropic glutamate receptor 1">1</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_2" title="Metabotropic glutamate receptor 2">2</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_3" title="Metabotropic glutamate receptor 3">3</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_4" title="Metabotropic glutamate receptor 4">4</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_5" title="Metabotropic glutamate receptor 5">5</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_6" title="Metabotropic glutamate receptor 6">6</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_7" title="Metabotropic glutamate receptor 7">7</a></li> <li><a href="/wiki/Metabotropic_glutamate_receptor_8" title="Metabotropic glutamate receptor 8">8</a>))</li> <li><a href="/wiki/GPRC6A" title="GPRC6A">GPRC6A</a></li> <li><a href="/wiki/Orphan_receptor" title="Orphan receptor">GPR</a> (<a href="/wiki/GPR156" title="GPR156">156</a></li> <li><a href="/wiki/GPR158" title="GPR158">158</a></li> <li><a href="/wiki/GPR179" title="GPR179">179</a>)</li> <li><a href="/wiki/Retinoic_acid-inducible_orphan_G_protein-coupled_receptor" title="Retinoic acid-inducible orphan G protein-coupled receptor">RAIG</a> (<a href="/wiki/GPRC5A" title="GPRC5A">1</a></li> <li><a href="/wiki/GPRC5B" title="GPRC5B">2</a></li> <li><a href="/wiki/GPRC5C" title="GPRC5C">3</a></li> <li><a href="/wiki/GPRC5D" title="GPRC5D">4</a>)</li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks mw-collapsible mw-collapsed navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Class_F:_Frizzled_&amp;amp;_Smoothened58" style="font-size:114%;margin:0 4em">Class F: <a href="/wiki/Frizzled" title="Frizzled">Frizzled</a> &amp; <a href="/wiki/Smoothened" title="Smoothened">Smoothened</a></div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;">Frizzled</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Frizzled" title="Frizzled">Frizzled</a> (<a href="/wiki/FZD1" class="mw-redirect" title="FZD1">1</a></li> <li><a href="/wiki/FZD2" class="mw-redirect" title="FZD2">2</a></li> <li><a href="/wiki/FZD3" class="mw-redirect" title="FZD3">3</a></li> <li><a href="/wiki/FZD4" class="mw-redirect" title="FZD4">4</a></li> <li><a href="/wiki/FZD5" class="mw-redirect" title="FZD5">5</a></li> <li><a href="/wiki/FZD6" class="mw-redirect" title="FZD6">6</a></li> <li><a href="/wiki/FZD7" class="mw-redirect" title="FZD7">7</a></li> <li><a href="/wiki/FZD8" class="mw-redirect" title="FZD8">8</a></li> <li><a href="/wiki/FZD9" class="mw-redirect" title="FZD9">9</a></li> <li><a href="/wiki/FZD10" class="mw-redirect" title="FZD10">10</a>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:10em;text-align:left;">Smoothened</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Smoothened" title="Smoothened">Smoothened</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <!-- NewPP limit report Parsed by mw‐web.eqiad.main‐8669bc5c8‐gngdm Cached time: 20250318160106 Cache expiry: 2592000 Reduced expiry: false Complications: [vary‐revision‐sha1, show‐toc] CPU time usage: 1.695 seconds Real time usage: 2.089 seconds Preprocessor visited node count: 7935/1000000 Post‐expand include size: 507544/2097152 bytes Template argument size: 518/2097152 bytes Highest expansion depth: 8/100 Expensive parser function count: 3/500 Unstrip recursion 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