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P02699 (OPSD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhodopsin
Gene names
Name:RHO
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal By similarity. Ref.26 Ref.27

Subunit structure

Homodimer. Ref.31

Subcellular location

Membrane; Multi-pass membrane protein. Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia By similarity.

Tissue specificity

Rod shaped photoreceptor cells which mediates vision in dim light.

Post-translational modification

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. Ref.10 Ref.18 Ref.19

Contains one covalently linked retinal chromophore.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.

Biophysicochemical properties

Absorption:

Abs(max)=495 nm

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandChromophore
Metal-binding
Zinc
   Molecular functionG-protein coupled receptor
Photoreceptor protein
Receptor
Retinal protein
Transducer
   PTMAcetylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to light stimulus

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Inferred from direct assay PubMed 22066464. Source: AgBase

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of GTPase activity

Traceable author statement. Source: GOC

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay PubMed 22066464. Source: AgBase

photoreceptor disc membrane

Traceable author statement. Source: Reactome

photoreceptor inner segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionG-protein coupled photoreceptor activity

Inferred from direct assay PubMed 22066464. Source: AgBase

guanyl-nucleotide exchange factor activity

Traceable author statement. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10399916. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Rhodopsin
PRO_0000197653

Regions

Topological domain1 – 3636Extracellular
Transmembrane37 – 6327Helical; Name=1
Topological domain64 – 7310Cytoplasmic
Transmembrane74 – 9623Helical; Name=2
Topological domain97 – 11014Extracellular
Transmembrane111 – 13323Helical; Name=3
Topological domain134 – 15219Cytoplasmic
Transmembrane153 – 17321Helical; Name=4
Topological domain174 – 20229Extracellular
Transmembrane203 – 22422Helical; Name=5
Topological domain225 – 24925Cytoplasmic
Transmembrane250 – 27425Helical; Name=6
Topological domain275 – 28612Extracellular
Transmembrane287 – 30822Helical; Name=7
Topological domain309 – 34840Cytoplasmic
Region113 – 12513Retinal chromophore binding
Region207 – 2126Retinal chromophore binding
Motif134 – 1374'Ionic lock' involved in activated form stabilization

Sites

Metal binding2011Zinc
Metal binding2791Zinc
Binding site2651Retinal chromophore

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue2961N6-(retinylidene)lysine
Modified residue3341Phosphoserine By similarity
Modified residue3351Phosphothreonine Ref.18 Ref.19
Modified residue3361Phosphothreonine Ref.18 Ref.19
Modified residue3381Phosphoserine By similarity
Modified residue3401Phosphothreonine Ref.18 Ref.19
Modified residue3421Phosphothreonine Ref.18 Ref.19
Modified residue3431Phosphoserine; by RK and GRK7 Ref.10 Ref.18 Ref.19
Lipidation3221S-palmitoyl cysteine Ref.8 Ref.11 Ref.14
Lipidation3231S-palmitoyl cysteine Ref.8 Ref.11 Ref.14
Glycosylation21N-linked (GlcNAc...) Ref.1 Ref.6 Ref.14
Glycosylation151N-linked (GlcNAc...) Ref.1 Ref.6 Ref.14
Disulfide bond110 ↔ 187 Ref.9

Experimental info

Mutagenesis21N → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. Ref.29
Mutagenesis151N → D: Normal light absorption; when associated with C-2 and C-282. Ref.29
Mutagenesis2821D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. Ref.29
Sequence conflict2811S → F in AAA30675. Ref.3

Secondary structure

............................................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02699 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 33FDA196803E81F3

FASTA34839,008
        10         20         30         40         50         60 
MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML GFPINFLTLY 

        70         80         90        100        110        120 
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG 

       130        140        150        160        170        180 
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP 

       190        200        210        220        230        240 
EGMQCSCGID YYTPHEETNN ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES 

       250        260        270        280        290        300 
ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV 

       310        320        330        340 
YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA 

« Hide

References

[1]"Rhodopsin and bacteriorhodopsin: structure-function relationships."
Ovchinnikov Y.A.
FEBS Lett. 148:179-191(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, RETINAL-BINDING SITE AT LYS-296.
[2]"Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin."
Nathans J., Hogness D.S.
Cell 34:807-814(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Multiple opsin mRNA species in bovine retina."
Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N.
Brain Res. 387:251-260(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
[4]"Isolation and nucleotide sequence of a partial cDNA clone for bovine opsin."
Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M., Tokunaga F.
Biochem. Biophys. Res. Commun. 116:563-567(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
[5]"Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin."
Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B., Galijatovic A., Chen N., Crouch R.K., Knapp D.R.
Protein Sci. 7:758-764(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Retina.
[6]"Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus."
Fukuda M.N., Papermaster D.S., Hargrave P.A.
J. Biol. Chem. 254:8201-8207(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
[7]"Structural studies on membrane-bound bovine rhodopsin."
Mullen E., Akhtar M.
Biochem. J. 211:45-54(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: RETINAL-BINDING SITE.
[8]"Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated."
Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.
FEBS Lett. 230:1-5(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[9]"Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187."
Karnik S.S., Khorana H.G.
J. Biol. Chem. 265:17520-17524(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[10]"Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin."
Brown N.G., Fowles C., Sharma R., Akhtar M.
Eur. J. Biochem. 208:659-667(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-343.
[11]"Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry."
Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.
J. Biol. Chem. 267:16889-16894(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
[12]"Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops."
Cai K., Langen R., Hubbell W.L., Khorana H.G.
Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"Crystal structure of rhodopsin: a G protein-coupled receptor."
Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., Miyano M.
Science 289:739-745(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]"Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)."
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.
Biochemistry 40:7761-7772(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, GLYCOSYLATION AT ASN-2 AND ASN-15.
[15]"Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms."
Yeagle P.L., Choi G., Albert A.D.
Biochemistry 40:11932-11937(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
[16]"Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin."
Choi G., Landin J., Galan J.F., Birge R.R., Albert A.D., Yeagle P.L.
Biochemistry 41:7318-7324(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
[17]"Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography."
Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y.
Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[18]"The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin."
Kisselev O.G., McDowell J.H., Hargrave P.A.
FEBS Lett. 564:307-311(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
[19]"Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions."
Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.
J. Biol. Chem. 279:51203-51207(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
[20]"The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure."
Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V.
J. Mol. Biol. 342:571-583(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[21]"Structure of bovine rhodopsin in a trigonal crystal form."
Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F.
J. Mol. Biol. 343:1409-1438(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[22]"Structure of the third cytoplasmic loop of bovine rhodopsin."
Yeagle P.L., Alderfer J.L., Albert A.D.
Biochemistry 34:14621-14625(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 231-252.
[23]"Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin."
Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G., Alderfer J.L., Albert A.D.
J. Pept. Res. 55:455-465(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
[24]"Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin."
Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D.
Mol. Vis. 6:125-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 291-315.
[25]"Crystallographic analysis of primary visual photochemistry."
Nakamichi H., Okada T.
Angew. Chem. Int. Ed. 45:4270-4273(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE.
[26]"Local peptide movement in the photoreaction intermediate of rhodopsin."
Nakamichi H., Okada T.
Proc. Natl. Acad. Sci. U.S.A. 103:12729-12734(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
[27]"Crystal structure of a photoactivated deprotonated intermediate of rhodopsin."
Salom D., Lodowski D.T., Stenkamp R.E., Le Trong I., Golczak M., Jastrzebska B., Harris T., Ballesteros J.A., Palczewski K.
Proc. Natl. Acad. Sci. U.S.A. 103:16123-16128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
[28]"Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography."
Nakamichi H., Buss V., Okada T.
Biophys. J. 92:L106-L108(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS IN COMPLEX WITH RETINAL CHROMOPHORE.
[29]"Crystal structure of a thermally stable rhodopsin mutant."
Standfuss J., Xie G., Edwards P.C., Burghammer M., Oprian D.D., Schertler G.F.
J. Mol. Biol. 372:1179-1188(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, MUTAGENESIS OF ASN-2; ASN-15 AND ASP-282.
[30]"Alternative models for two crystal structures of bovine rhodopsin."
Stenkamp R.E.
Acta Crystallogr. D 64:902-904(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[31]"Crystal structure of the ligand-free G-protein-coupled receptor opsin."
Park J.H., Scheerer P., Hofmann K.P., Choe H.-W., Ernst O.P.
Nature 454:183-187(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DIMERIZATION.
[32]"Crystal structure of opsin in its G-protein-interacting conformation."
Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.-W., Hofmann K.P., Ernst O.P.
Nature 455:497-502(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), ACTIVATION MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00506 expand/collapse EMBL AC list , K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.
PIROOBO. A90840.
RefSeqNP_001014890.1. NM_001014890.1.
UniGeneBt.12753.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOJmodel-A1-348[»]
1BOKmodel-A1-348[»]
1EDSNMR-A93-123[»]
1EDVNMR-A172-205[»]
1EDWNMR-A268-293[»]
1EDXNMR-A1-40[»]
1F88X-ray2.80A/B1-348[»]
1FDFNMR-A291-315[»]
1GZMX-ray2.65A/B1-348[»]
1HZXX-ray2.80A/B1-348[»]
1JFPNMR-A1-348[»]
1L9HX-ray2.60A/B1-348[»]
1LN6NMR-A1-348[»]
1N3Mmodel-A/B/C/D/E/F1-348[»]
1NZSNMR-A330-348[»]
1OV0model-A1-348[»]
1OV1model-A1-348[»]
1U19X-ray2.20A/B1-348[»]
1VQXNMR-A330-348[»]
2G87X-ray2.60A/B1-348[»]
2HPYX-ray2.80A/B1-348[»]
2I35X-ray3.80A1-348[»]
2I36X-ray4.10A/B/C1-348[»]
2I37X-ray4.15A/B/C1-348[»]
2IQKmodel-A1-348[»]
2J4YX-ray3.40A/B1-348[»]
2PEDX-ray2.95A/B1-348[»]
2X72X-ray3.00A1-348[»]
3C9LX-ray2.65A1-348[»]
3C9MX-ray3.40A1-348[»]
3CAPX-ray2.90A/B1-348[»]
3DQBX-ray3.20A1-348[»]
3OAXX-ray2.60A/B1-348[»]
3PQRX-ray2.85A1-348[»]
3PXOX-ray3.00A1-348[»]
4A4MX-ray3.30A1-348[»]
4BEYX-ray2.90A1-348[»]
4BEZX-ray3.30A1-348[»]
4J4QX-ray2.65A1-348[»]
DisProtDP00271.
ProteinModelPortalP02699.
SMRP02699. Positions 1-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29225N.
IntActP02699. 3 interactions.
MINTMINT-1507462.
STRING9913.ENSBTAP00000001730.

Chemistry

BindingDBP02699.
ChEMBLCHEMBL5739.

Protein family/group databases

GPCRDBSearch...

PTM databases

UniCarbKBP02699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneID509933.
KEGGbta:509933.

Organism-specific databases

CTD6010.

Phylogenomic databases

eggNOGNOG311294.
GeneTreeENSGT00710000106574.
HOGENOMHOG000253932.
HOVERGENHBG107442.
InParanoidP02699.
KOK04250.
OMALAAYMFM.
OrthoDBEOG72NRQJ.
TreeFamTF324998.

Enzyme and pathway databases

ReactomeREACT_207087. Disease.
REACT_214353. Signal Transduction.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
4.10.840.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02699.
NextBio20869202.

Entry information

Entry nameOPSD_BOVIN
AccessionPrimary (citable) accession number: P02699
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries