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UniProtKB/Swiss-Prot entry P02699


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name OPSD_BOVIN
Primary accession number P02699
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 105)
Name and origin of the protein
Protein name Rhodopsin
Synonyms None
Gene name
Name: RHO
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
DOI=10.1016/0014-5793(82)80805-3; PubMed=6759163 [NCBI, ExPASy, EBI, Israel, Japan]
Ovchinnikov Y.A.;
"Rhodopsin and bacteriorhodopsin: structure-function relationships.";
FEBS Lett. 148:179-191(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(83)90537-8; PubMed=6194890 [NCBI, ExPASy, EBI, Israel, Japan]
Nathans J., Hogness D.S.;
"Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin.";
Cell 34:807-814(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
PubMed=2950966 [NCBI, ExPASy, EBI, Israel, Japan]
Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N.;
"Multiple opsin mRNA species in bovine retina.";
Brain Res. 387:251-260(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
PubMed=6228228 [NCBI, ExPASy, EBI, Israel, Japan]
Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M., Tokunaga F.;
"Isolation and nucleotide sequence of a partial cDNA clone for bovine opsin.";
Biochem. Biophys. Res. Commun. 116:563-567(1983).
[5]
PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
TISSUE=Retina;
PubMed=9541408 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin.";
Protein Sci. 7:758-764(1998).
[6]
GLYCOSYLATION AT ASN-2 AND ASN-15.
PubMed=468821 [NCBI, ExPASy, EBI, Israel, Japan]
Fukuda M.N., Papermaster D.S., Hargrave P.A.;
"Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus.";
J. Biol. Chem. 254:8201-8207(1979).
[7]
RETINAL-BINDING SITE.
PubMed=6870827 [NCBI, ExPASy, EBI, Israel, Japan]
Mullen E., Akhtar M.;
"Structural studies on membrane-bound bovine rhodopsin.";
Biochem. J. 211:45-54(1983).
[8]
PALMITOYLATION AT CYS-322 AND CYS-323.
DOI=10.1016/0014-5793(88)80628-8; PubMed=3350146 [NCBI, ExPASy, EBI, Israel, Japan]
Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.;
"Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated.";
FEBS Lett. 230:1-5(1988).
[9]
DISULFIDE BOND.
PubMed=2145276 [NCBI, ExPASy, EBI, Israel, Japan]
Karnik S.S., Khorana H.G.;
"Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.";
J. Biol. Chem. 265:17520-17524(1990).
[10]
PHOSPHORYLATION AT SER-343.
PubMed=1396673 [NCBI, ExPASy, EBI, Israel, Japan]
Brown N.G., Fowles C., Sharma R., Akhtar M.;
"Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin.";
Eur. J. Biochem. 208:659-667(1992).
[11]
PALMITOYLATION AT CYS-322 AND CYS-323.
PubMed=1512231 [NCBI, ExPASy, EBI, Israel, Japan]
Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.;
"Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry.";
J. Biol. Chem. 267:16889-16894(1992).
[12]
MUTAGENESIS.
DOI=10.1073/pnas.94.26.14267; PubMed=9405601 [NCBI, ExPASy, EBI, Israel, Japan]
Cai K., Langen R., Hubbell W.L., Khorana H.G.;
"Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops.";
Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1126/science.289.5480.739; PubMed=10926528 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Crystal structure of rhodopsin: a G protein-coupled receptor.";
Science 289:739-745(2000).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1073/pnas.082666399; PubMed=11972040 [NCBI, ExPASy, EBI, Israel, Japan]
Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y.;
"Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography.";
Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1016/j.jmb.2004.07.044; PubMed=15327956 [NCBI, ExPASy, EBI, Israel, Japan]
Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V.;
"The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure.";
J. Mol. Biol. 342:571-583(2004).
[16]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
DOI=10.1016/j.jmb.2004.08.090; PubMed=15491621 [NCBI, ExPASy, EBI, Israel, Japan]
Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F.;
"Structure of bovine rhodopsin in a trigonal crystal form.";
J. Mol. Biol. 343:1409-1438(2004).
[17]
STRUCTURE BY NMR OF 231-252.
DOI=10.1021/bi00045a002; PubMed=7578070 [NCBI, ExPASy, EBI, Israel, Japan]
Yeagle P.L., Alderfer J.L., Albert A.D.;
"Structure of the third cytoplasmic loop of bovine rhodopsin.";
Biochemistry 34:14621-14625(1995).
[18]
STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
DOI=10.1034/j.1399-3011.2000.00707.x; PubMed=10888202 [NCBI, ExPASy, EBI, Israel, Japan]
Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G., Alderfer J.L., Albert A.D.;
"Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin.";
J. Pept. Res. 55:455-465(2000).
[19]
STRUCTURE BY NMR OF 291-315.
PubMed=10930473 [NCBI, ExPASy, EBI, Israel, Japan]
Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D.;
"Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin.";
Mol. Vis. 6:125-131(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K00506; AAA30674.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00502; AAA30674.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00503; AAA30674.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00504; AAA30674.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00505; AAA30674.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21606; AAA30675.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A90840; OOBO.
RefSeq NP_001014890.1; -.
UniGene Bt.12753
3D structure databases
PDB
1BOJ; Model; -; A=1-348.[ExPASy / RCSB / EBI]
1BOK; Model; -; A=1-348.[ExPASy / RCSB / EBI]
1EDS; NMR; -; A=93-123.[ExPASy / RCSB / EBI]
1EDV; NMR; -; A=172-205.[ExPASy / RCSB / EBI]
1EDW; NMR; -; A=268-293.[ExPASy / RCSB / EBI]
1EDX; NMR; -; A=1-40.[ExPASy / RCSB / EBI]
1F88; X-ray; 2.80 A; A/B=1-348.[ExPASy / RCSB / EBI]
1FDF; NMR; -; A=291-315.[ExPASy / RCSB / EBI]
1GZM; X-ray; 2.65 A; A/B=1-348.[ExPASy / RCSB / EBI]
1HZX; X-ray; 2.80 A; A/B=1-348.[ExPASy / RCSB / EBI]
1JFP; NMR; -; A=1-348.[ExPASy / RCSB / EBI]
1L9H; X-ray; 2.60 A; A/B=1-348.[ExPASy / RCSB / EBI]
1LN6; NMR; -; A=1-348.[ExPASy / RCSB / EBI]
1N3M; Model; -; A/B/C/D/E/F=1-348.[ExPASy / RCSB / EBI]
1NZS; NMR; -; A=330-348.[ExPASy / RCSB / EBI]
1OV0; Model; -; A=1-348.[ExPASy / RCSB / EBI]
1OV1; Model; -; A=1-348.[ExPASy / RCSB / EBI]
1U19; X-ray; 2.20 A; A/B=1-348.[ExPASy / RCSB / EBI]
1VQX; NMR; -; A=330-348.[ExPASy / RCSB / EBI]
2G87; X-ray; 2.60 A; A/B=1-348.[ExPASy / RCSB / EBI]
2HPY; X-ray; 2.80 A; A/B=1-348.[ExPASy / RCSB / EBI]
2I35; X-ray; 3.80 A; A=1-348.[ExPASy / RCSB / EBI]
2I36; X-ray; 4.10 A; A/B/C=1-348.[ExPASy / RCSB / EBI]
2I37; X-ray; 4.15 A; A/B/C=1-348.[ExPASy / RCSB / EBI]
2IQK; Model; -; A=1-348.[ExPASy / RCSB / EBI]
2J4Y; X-ray; 3.40 A; A/B=1-348.[ExPASy / RCSB / EBI]
2PED; X-ray; 2.95 A; A/B=1-348.[ExPASy / RCSB / EBI]
3CAP; X-ray; 2.90 A; A/B=1-348.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BOJ; -.
1BOK; -.
1EDS; -.
1EDV; -.
1EDW; -.
1EDX; -.
1F88; -.
1FDF; -.
1GZM; -.
1HZX; -.
1JFP; -.
1L9H; -.
1LN6; -.
1N3M; -.
1NZS; -.
1OV0; -.
1OV1; -.
1U19; -.
1VQX; -.
2G87; -.
2HPY; -.
2I35; -.
2I36; -.
2I37; -.
2IQK; -.
2J4Y; -.
2PED; -.
3CAP; -.
DisProt DP00271; -.
ModBase P02699.
Protein family/group databases
GPCRDB P02699; OPSD_BOVIN.
PTM databases
GlycoSuiteDB P02699; -.
Enzyme and pathway databases
BioCyc MetaCyc:RHODOPSIN-MON; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0004930; Molecular function: G-protein coupled receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0009881; Molecular function: photoreceptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (inferred from electronic annotation from InterPro).
GO:0007602; Biological process: phototransduction (inferred from electronic annotation from InterPro).
GO:0018298; Biological process: protein-chromophore linkage (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000276; GPCR_Rhodpsn.
IPR017452; GPCR_Rhodpsn_supfam.
IPR001760; Opsin.
IPR000732; Rhodopsin.
Graphical view of domain structure.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00237; GPCRRHODOPSN.
PR00238; OPSIN.
PR00579; RHODOPSIN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PS00238; OPSIN; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P02699.
Genome annotation databases
Ensembl ENSBTAG00000001310; Bos taurus. [Contig view]
GeneID 509933; -.
KEGG bta:509933; -.
Phylogenomic databases
HOVERGEN P02699; -.
Other
LinkHub P02699; -.
GPCRDB-Snakes P02699.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Chromophore; Direct protein sequencing; G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane; Vision.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   348  348     Rhodopsin. PRO_0000197653
TOPO_DOM   1    36  36     Extracellular. 
TRANSMEM   37    63  27     1. 
TOPO_DOM   64    73  10     Cytoplasmic. 
TRANSMEM   74    96  23     2. 
TOPO_DOM   97   110  14     Extracellular. 
TRANSMEM   111   133  23     3. 
TOPO_DOM   134   152  19     Cytoplasmic. 
TRANSMEM   153   173  21     4. 
TOPO_DOM   174   202  29     Extracellular. 
TRANSMEM   203   224  22     5. 
TOPO_DOM   225   249  25     Cytoplasmic. 
TRANSMEM   250   274  25     6. 
TOPO_DOM   275   286  12     Extracellular. 
TRANSMEM   287   308  22     7. 
TOPO_DOM   309   348  40     Cytoplasmic. 
BINDING   296   296        Retinal chromophore (covalent). 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   334   334        Phosphoserine (By similarity). 
MOD_RES   338   338        Phosphoserine (By similarity). 
MOD_RES   343   343        Phosphoserine; by RK. 
LIPID   322   322        S-palmitoyl cysteine. 
LIPID   323   323        S-palmitoyl cysteine. 
CARBOHYD   2     2        N-linked (GlcNAc...). 
CARBOHYD   15    15        N-linked (GlcNAc...). 
DISULFID   110   187         
CONFLICT   281   281        S -> F (in Ref. 3; AAA30675). 
STRAND   3     5  3      
STRAND   10    13  4      
TURN   23    25  3      
HELIX   29    31  3      
HELIX   34    64  31      
HELIX   71    89  19      
HELIX   91   100  10      
HELIX   106   139  34      
STRAND   143   145  3      
HELIX   150   168  19      
HELIX   170   172  3      
STRAND   178   181  4      
TURN   182   185  4      
STRAND   186   189  4      
TURN   196   199  4      
HELIX   200   210  11      
HELIX   213   225  13      
HELIX   246   254  9      
HELIX   256   277  22      
HELIX   285   295  11      
HELIX   296   299  4      
HELIX   301   309  9      
HELIX   311   321  11      
TURN   322   324  3      
STRAND   338   342  5      
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 39008 Da [This is the MW of the unprocessed precursor] CRC64: 33FDA196803E81F3 [This is a checksum on the sequence]
        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 

P02699 in FASTA format

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View entry in raw text format (no links)
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