UniProtKB - P31356 (OPSD_TODPA)
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>sp|P31356|OPSD_TODPA Rhodopsin OS=Todarodes pacificus OX=6637 GN=RHO PE=1 SV=2 MGRDLRDNETWWYNPSIVVHPHWREFDQVPDAVYYSLGIFIGICGIIGCGGNGIVIYLFT KTKSLQTPANMFIINLAFSDFTFSLVNGFPLMTISCFLKKWIFGFAACKVYGFIGGIFGF MSIMTMAMISIDRYNVIGRPMAASKKMSHRRAFIMIIFVWLWSVLWAIGPIFGWGAYTLE GVLCNCSFDYISRDSTTRSNILCMFILGFFGPILIIFFCYFNIVMSVSNHEKEMAAMAKR LNAKELRKAQAGANAEMRLAKISIVIVSQFLLSWSPYAVVALLAQFGPLEWVTPYAAQLP VMFAKASAIHNPMIYSVSHPKFREAISQTFPWVLTCCQFDDKETEDDKDAETEIPAGESS DAAPSADAAQMKEMMAMMQKMQQQQAAYPPQGYAPPPQGYPPQGYPPQGYPPQGYPPQGY PPPPQGAPPQGAPPAAPPQGVDNQAYQACommunity curation ()Add a publicationFeedback
Rhodopsin
RHO
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Photoreceptor required for image-forming vision at low light intensity (Probable). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling mediates the activation of phospholipase C (Probable). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Curated<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY. - Ref.6"Crystallographic analysis of the primary photochemical reaction of squid rhodopsin."
Murakami M., Kouyama T.
J. Mol. Biol. 413:615-627(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS. - Ref.7"Crystallographic Study of the LUMI Intermediate of Squid Rhodopsin."
Murakami M., Kouyama T.
PLoS ONE 10:E0126970-E0126970(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 9-358 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- G protein-coupled receptor activity Source: UniProtKB-KW
- photoreceptor activity Source: UniProtKB-KW
- retinal binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
GO - Biological processi
- phototransduction Source: UniProtKB-KW
- protein-chromophore linkage Source: UniProtKB-KW
- visual perception Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer |
Biological process | Sensory transduction, Vision |
Ligand | Chromophore |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Rhodopsin |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:RHO |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 6637 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Spiralia › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Decapodiformes › Teuthida › Oegopsina › Ommastrephidae › Todarodes |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Membrane 5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY. - Ref.6"Crystallographic analysis of the primary photochemical reaction of squid rhodopsin."
Murakami M., Kouyama T.
J. Mol. Biol. 413:615-627(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS. - Ref.7"Crystallographic Study of the LUMI Intermediate of Squid Rhodopsin."
Murakami M., Kouyama T.
PLoS ONE 10:E0126970-E0126970(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 9-358 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS.
Manual assertion based on experiment ini
- Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY. - Ref.6"Crystallographic analysis of the primary photochemical reaction of squid rhodopsin."
Murakami M., Kouyama T.
J. Mol. Biol. 413:615-627(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS. - Ref.7"Crystallographic Study of the LUMI Intermediate of Squid Rhodopsin."
Murakami M., Kouyama T.
PLoS ONE 10:E0126970-E0126970(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 9-358 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS.
Note: Detected on the rhabdomere membrane in the photoreceptor outer segment.4 Publications- Membrane 5 Publications
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY. - Ref.6"Crystallographic analysis of the primary photochemical reaction of squid rhodopsin."
Murakami M., Kouyama T.
J. Mol. Biol. 413:615-627(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS.
Manual assertion based on experiment ini
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- integral component of membrane Source: UniProtKBInferred from direct assayi
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- integral component of membrane Source: UniProtKBInferred from direct assayi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 2 – 33 | Extracellular4 Publications Manual assertion based on experiment ini
| 32 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 34 – 58 | Helical; Name=14 Publications Manual assertion based on experiment ini
| 25 | |
Topological domaini | 59 – 70 | Cytoplasmic4 Publications Manual assertion based on experiment ini
| 12 | |
Transmembranei | 71 – 97 | Helical; Name=24 Publications Manual assertion based on experiment ini
| 27 | |
Topological domaini | 98 – 109 | Extracellular4 Publications Manual assertion based on experiment ini
| 12 | |
Transmembranei | 110 – 131 | Helical; Name=34 Publications Manual assertion based on experiment ini
| 22 | |
Topological domaini | 132 – 151 | Cytoplasmic4 Publications Manual assertion based on experiment ini
| 20 | |
Transmembranei | 152 – 172 | Helical; Name=44 Publications Manual assertion based on experiment ini
| 21 | |
Topological domaini | 173 – 199 | Extracellular4 Publications Manual assertion based on experiment ini
| 27 | |
Transmembranei | 200 – 224 | Helical; Name=54 Publications Manual assertion based on experiment ini
| 25 | |
Topological domaini | 225 – 261 | Cytoplasmic4 Publications Manual assertion based on experiment ini
| 37 | |
Transmembranei | 262 – 283 | Helical; Name=64 Publications Manual assertion based on experiment ini
| 22 | |
Topological domaini | 284 – 293 | Extracellular4 Publications Manual assertion based on experiment ini
| 10 | |
Transmembranei | 294 – 315 | Helical; Name=74 Publications Manual assertion based on experiment ini
| 22 | |
Topological domaini | 316 – 448 | Cytoplasmic4 Publications Manual assertion based on experiment ini
| 133 |
Keywords - Cellular componenti
Membrane<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000197748 | 2 – 448 | RhodopsinAdd BLAST | 447 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 8 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 108 ↔ 186 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Combined sources<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| ||
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 305 | N6-(retinylidene)lysineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 336 | S-palmitoyl cysteineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Lipidationi | 337 | S-palmitoyl cysteineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Manual assertion inferred from sequence similarity toi
5 PublicationsManual assertion based on experiment ini
- Ref.2"Amino acid sequence of the retinal binding site of squid visual pigment."
Seidou M., Kubota I., Hiraki K., Kito Y.
Biochim. Biophys. Acta 957:318-321(1988) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 303-313, RETINAL-CHROMOPHORE BINDING AT LYS-305. - Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY. - Ref.6"Crystallographic analysis of the primary photochemical reaction of squid rhodopsin."
Murakami M., Kouyama T.
J. Mol. Biol. 413:615-627(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS. - Ref.7"Crystallographic Study of the LUMI Intermediate of Squid Rhodopsin."
Murakami M., Kouyama T.
PLoS ONE 10:E0126970-E0126970(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 9-358 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS.
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
PRoteomics IDEntifications database More...PRIDEi | P31356 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 524, 4 N-Linked glycans |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P31356 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion based on experiment ini
- Ref.3"Crystallization and crystal properties of squid rhodopsin."
Murakami M., Kitahara R., Gotoh T., Kouyama T.
Acta Crystallogr. F 63:475-479(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CRYSTALLIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.4"Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region."
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M., Miyano M.
J. Biol. Chem. 283:17753-17756(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-373 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, DISULFIDE BONDS, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PALMITOYLATION AT CYS-336 AND CYS-337. - Ref.5"Crystal structure of squid rhodopsin."
Murakami M., Kouyama T.
Nature 453:363-367(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-337, GLYCOSYLATION AT ASN-8, DISULFIDE BONDS, TOPOLOGY.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-60624N |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 15 – 17 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 24 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 31 – 61 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 31 | |
Helixi | 63 – 65 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 70 – 87 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
Helixi | 91 – 97 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 104 – 136 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 33 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 141 – 143 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 149 – 167 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
Helixi | 169 – 172 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 177 – 179 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 183 – 188 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 195 – 207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 210 – 224 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
Helixi | 227 – 238 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Turni | 239 – 241 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 246 – 286 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 41 | |
Helixi | 289 – 291 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 294 – 306 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 307 – 309 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 311 – 318 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 320 – 329 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 331 – 334 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 341 – 344 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 345 – 351 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 355 – 357 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | P31356 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P31356 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P31356 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 343 – 448 | DisorderedSequence analysis <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More...</a></p> Automatic assertion according to sequence analysisi Add BLAST | 106 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 390 – 436 | Pro residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 47 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Manual assertion according to rulesi
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000276, GPCR_Rhodpsn IPR017452, GPCR_Rhodpsn_7TM IPR001760, Opsin IPR027430, Retinal_BS IPR006031, XYPPX |
Pfam protein domain database More...Pfami | View protein in Pfam PF00001, 7tm_1, 1 hit PF02162, XYPPX, 5 hits |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00237, GPCRRHODOPSN PR00238, OPSIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01381, 7TM_GPCR_Srsx, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00237, G_PROTEIN_RECEP_F1_1, 1 hit PS50262, G_PROTEIN_RECEP_F1_2, 1 hit PS00238, OPSIN, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MGRDLRDNET WWYNPSIVVH PHWREFDQVP DAVYYSLGIF IGICGIIGCG
60 70 80 90 100
GNGIVIYLFT KTKSLQTPAN MFIINLAFSD FTFSLVNGFP LMTISCFLKK
110 120 130 140 150
WIFGFAACKV YGFIGGIFGF MSIMTMAMIS IDRYNVIGRP MAASKKMSHR
160 170 180 190 200
RAFIMIIFVW LWSVLWAIGP IFGWGAYTLE GVLCNCSFDY ISRDSTTRSN
210 220 230 240 250
ILCMFILGFF GPILIIFFCY FNIVMSVSNH EKEMAAMAKR LNAKELRKAQ
260 270 280 290 300
AGANAEMRLA KISIVIVSQF LLSWSPYAVV ALLAQFGPLE WVTPYAAQLP
310 320 330 340 350
VMFAKASAIH NPMIYSVSHP KFREAISQTF PWVLTCCQFD DKETEDDKDA
360 370 380 390 400
ETEIPAGESS DAAPSADAAQ MKEMMAMMQK MQQQQAAYPP QGYAPPPQGY
410 420 430 440
PPQGYPPQGY PPQGYPPQGY PPPPQGAPPQ GAPPAAPPQG VDNQAYQA
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X70498 mRNA Translation: CAA49906.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S29483 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X70498 mRNA Translation: CAA49906.1 |
PIRi | S29483 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2Z73 | X-ray | 2.50 | A/B | 1-448 | [»] | |
2ZIY | X-ray | 3.70 | A | 2-373 | [»] | |
3AYM | X-ray | 2.80 | A/B | 1-448 | [»] | |
3AYN | X-ray | 2.70 | A/B | 1-448 | [»] | |
4WW3 | X-ray | 2.80 | A/B | 9-358 | [»] | |
AlphaFoldDBi | P31356 | |||||
SMRi | P31356 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-60624N |
Protein family/group databases
Information system for G protein-coupled receptors (GPCRs) More...GPCRDBi | Search... |
PTM databases
GlyConnecti | 524, 4 N-Linked glycans |
iPTMneti | P31356 |
Proteomic databases
PRIDEi | P31356 |
Miscellaneous databases
EvolutionaryTracei | P31356 |
Family and domain databases
InterProi | View protein in InterPro IPR000276, GPCR_Rhodpsn IPR017452, GPCR_Rhodpsn_7TM IPR001760, Opsin IPR027430, Retinal_BS IPR006031, XYPPX |
Pfami | View protein in Pfam PF00001, 7tm_1, 1 hit PF02162, XYPPX, 5 hits |
PRINTSi | PR00237, GPCRRHODOPSN PR00238, OPSIN |
SMARTi | View protein in SMART SM01381, 7TM_GPCR_Srsx, 1 hit |
PROSITEi | View protein in PROSITE PS00237, G_PROTEIN_RECEP_F1_1, 1 hit PS50262, G_PROTEIN_RECEP_F1_2, 1 hit PS00238, OPSIN, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | OPSD_TODPA | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P31356Primary (citable) accession number: P31356 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 103 of the entry and version 2 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- 7-transmembrane G-linked receptors
List of 7-transmembrane G-linked receptor entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families