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Rhodopsin

 OPSD_BOVIN              Reviewed;         348 AA.
P02699;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 181.
RecName: Full=Rhodopsin;
Name=RHO;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
PROTEIN SEQUENCE, RETINAL-BINDING SITE AT LYS-296, AND ACETYLATION AT
MET-1.
PubMed=6759163; DOI=10.1016/0014-5793(82)80805-3;
Ovchinnikov Y.A.;
"Rhodopsin and bacteriorhodopsin: structure-function relationships.";
FEBS Lett. 148:179-191(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6194890; DOI=10.1016/0092-8674(83)90537-8;
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;
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;
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 IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Retina;
PubMed=9541408; DOI=10.1002/pro.5560070325;
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;
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; DOI=10.1042/bj2110045;
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.
PubMed=3350146; DOI=10.1016/0014-5793(88)80628-8;
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;
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; DOI=10.1111/j.1432-1033.1992.tb17232.x;
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;
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.
PubMed=9405601; DOI=10.1073/pnas.94.26.14267;
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) IN COMPLEX WITH ZINC ION, AND
GLYCOSYLATION AT ASN-2 AND ASN-15.
PubMed=10926528; DOI=10.1126/science.289.5480.739;
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 (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL
CHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, AND
GLYCOSYLATION AT ASN-2 AND ASN-15.
PubMed=11425302; DOI=10.1021/bi0155091;
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
"Advances in determination of a high-resolution three-dimensional
structure of rhodopsin, a model of G-protein-coupled receptors
(GPCRs).";
Biochemistry 40:7761-7772(2001).
[15]
STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
PubMed=11570894; DOI=10.1021/bi015543f;
Yeagle P.L., Choi G., Albert A.D.;
"Studies on the structure of the G-protein-coupled receptor rhodopsin
including the putative G-protein binding site in unactivated and
activated forms.";
Biochemistry 40:11932-11937(2001).
[16]
STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
PubMed=12044163; DOI=10.1021/bi025507w;
Choi G., Landin J., Galan J.F., Birge R.R., Albert A.D., Yeagle P.L.;
"Structural studies of metarhodopsin II, the activated form of the G-
protein coupled receptor, rhodopsin.";
Biochemistry 41:7318-7324(2002).
[17]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=11972040; DOI=10.1073/pnas.082666399;
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).
[18]
STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL
ARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;
THR-340; THR-342 AND SER-343.
PubMed=15111114; DOI=10.1016/S0014-5793(04)00226-1;
Kisselev O.G., McDowell J.H., Hargrave P.A.;
"The arrestin-bound conformation and dynamics of the phosphorylated
carboxy-terminal region of rhodopsin.";
FEBS Lett. 564:307-311(2004).
[19]
STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL
ARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;
THR-340; THR-342 AND SER-343.
PubMed=15351781; DOI=10.1074/jbc.M407341200;
Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.;
"Conformational changes in the phosphorylated C-terminal domain of
rhodopsin during rhodopsin arrestin interactions.";
J. Biol. Chem. 279:51203-51207(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=15327956; DOI=10.1016/j.jmb.2004.07.044;
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
PubMed=15491621; DOI=10.1016/j.jmb.2004.08.090;
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).
[22]
STRUCTURE BY NMR OF 231-252.
PubMed=7578070; DOI=10.1021/bi00045a002;
Yeagle P.L., Alderfer J.L., Albert A.D.;
"Structure of the third cytoplasmic loop of bovine rhodopsin.";
Biochemistry 34:14621-14625(1995).
[23]
STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
PubMed=10888202; DOI=10.1034/j.1399-3011.2000.00707.x;
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).
[24]
STRUCTURE BY NMR OF 291-315.
PubMed=10930473;
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL
CHROMOPHORE.
PubMed=16586416; DOI=10.1002/anie.200600595;
Nakamichi H., Okada T.;
"Crystallographic analysis of primary visual photochemistry.";
Angew. Chem. Int. Ed. 45:4270-4273(2006).
[26]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) INACTIVATED AND ACTIVATED
FORMS, AND FUNCTION.
PubMed=16908857; DOI=10.1073/pnas.0601765103;
Nakamichi H., Okada T.;
"Local peptide movement in the photoreaction intermediate of
rhodopsin.";
Proc. Natl. Acad. Sci. U.S.A. 103:12729-12734(2006).
[27]
X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED
FORMS, AND FUNCTION.
PubMed=17060607; DOI=10.1073/pnas.0608022103;
Salom D., Lodowski D.T., Stenkamp R.E., Le Trong I., Golczak M.,
Jastrzebska B., Harris T., Ballesteros J.A., Palczewski K.;
"Crystal structure of a photoactivated deprotonated intermediate of
rhodopsin.";
Proc. Natl. Acad. Sci. U.S.A. 103:16123-16128(2006).
[28]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS
IN COMPLEX WITH RETINAL CHROMOPHORE.
PubMed=17449675; DOI=10.1529/biophysj.107.108225;
Nakamichi H., Buss V., Okada T.;
"Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin
revealed by x-ray crystallography.";
Biophys. J. 92:L106-L108(2007).
[29]
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, AND MUTAGENESIS OF
ASN-2; ASN-15 AND ASP-282.
PubMed=17825322; DOI=10.1016/j.jmb.2007.03.007;
Standfuss J., Xie G., Edwards P.C., Burghammer M., Oprian D.D.,
Schertler G.F.;
"Crystal structure of a thermally stable rhodopsin mutant.";
J. Mol. Biol. 372:1179-1188(2007).
[30]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
PubMed=18645239; DOI=10.1107/S0907444908017162;
Stenkamp R.E.;
"Alternative models for two crystal structures of bovine rhodopsin.";
Acta Crystallogr. D 64:902-904(2008).
[31]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND DIMERIZATION.
PubMed=18563085; DOI=10.1038/nature07063;
Park J.H., Scheerer P., Hofmann K.P., Choe H.-W., Ernst O.P.;
"Crystal structure of the ligand-free G-protein-coupled receptor
opsin.";
Nature 454:183-187(2008).
[32]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), AND ACTIVATION MECHANISM.
PubMed=18818650; DOI=10.1038/nature07330;
Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N.,
Choe H.-W., Hofmann K.P., Ernst O.P.;
"Crystal structure of opsin in its G-protein-interacting
conformation.";
Nature 455:497-502(2008).
-!- 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). {ECO:0000250,
ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=~495 nm;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781,
ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:17449675}.
-!- 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
vision in dim light.
-!- PTM: Phosphorylated on some or all of the serine and threonine
residues present in the C-terminal region.
{ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
-!- PTM: Contains one covalently linked retinal chromophore.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Opsin subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; K00506; AAA30674.1; -; Genomic_DNA.
EMBL; K00502; AAA30674.1; JOINED; Genomic_DNA.
EMBL; K00503; AAA30674.1; JOINED; Genomic_DNA.
EMBL; K00504; AAA30674.1; JOINED; Genomic_DNA.
EMBL; K00505; AAA30674.1; JOINED; Genomic_DNA.
EMBL; M21606; AAA30675.1; -; mRNA.
PIR; A90840; OOBO.
RefSeq; NP_001014890.1; NM_001014890.2.
UniGene; Bt.12753; -.
PDB; 1BOJ; Model; -; A=1-348.
PDB; 1BOK; Model; -; A=1-348.
PDB; 1EDS; NMR; -; A=93-123.
PDB; 1EDV; NMR; -; A=172-205.
PDB; 1EDW; NMR; -; A=268-293.
PDB; 1EDX; NMR; -; A=1-40.
PDB; 1F88; X-ray; 2.80 A; A/B=1-348.
PDB; 1FDF; NMR; -; A=291-315.
PDB; 1GZM; X-ray; 2.65 A; A/B=1-348.
PDB; 1HZX; X-ray; 2.80 A; A/B=1-348.
PDB; 1JFP; NMR; -; A=1-348.
PDB; 1L9H; X-ray; 2.60 A; A/B=1-348.
PDB; 1LN6; NMR; -; A=1-348.
PDB; 1N3M; Model; -; A/B/C/D/E/F=1-348.
PDB; 1NZS; NMR; -; A=330-348.
PDB; 1OV0; Model; -; A=1-348.
PDB; 1OV1; Model; -; A=1-348.
PDB; 1U19; X-ray; 2.20 A; A/B=1-348.
PDB; 1VQX; NMR; -; A=330-348.
PDB; 2G87; X-ray; 2.60 A; A/B=1-348.
PDB; 2HPY; X-ray; 2.80 A; A/B=1-348.
PDB; 2I35; X-ray; 3.80 A; A=1-348.
PDB; 2I36; X-ray; 4.10 A; A/B/C=1-348.
PDB; 2I37; X-ray; 4.15 A; A/B/C=1-348.
PDB; 2IQK; Model; -; A=1-348.
PDB; 2J4Y; X-ray; 3.40 A; A/B=1-348.
PDB; 2PED; X-ray; 2.95 A; A/B=1-348.
PDB; 2X72; X-ray; 3.00 A; A=1-348.
PDB; 3C9L; X-ray; 2.65 A; A=1-348.
PDB; 3C9M; X-ray; 3.40 A; A=1-348.
PDB; 3CAP; X-ray; 2.90 A; A/B=1-348.
PDB; 3DQB; X-ray; 3.20 A; A=1-348.
PDB; 3OAX; X-ray; 2.60 A; A/B=1-348.
PDB; 3PQR; X-ray; 2.85 A; A=1-348.
PDB; 3PXO; X-ray; 3.00 A; A=1-348.
PDB; 4A4M; X-ray; 3.30 A; A=1-348.
PDB; 4BEY; X-ray; 2.90 A; A=1-348.
PDB; 4BEZ; X-ray; 3.30 A; A=1-348.
PDB; 4J4Q; X-ray; 2.65 A; A=1-348.
PDB; 4PXF; X-ray; 2.75 A; A=1-348.
PDB; 4X1H; X-ray; 2.29 A; A=1-348.
PDB; 5DYS; X-ray; 2.30 A; A=1-348.
PDB; 5EN0; X-ray; 2.81 A; A=1-348.
PDB; 5TE3; X-ray; 2.70 A; A=1-348.
PDB; 5TE5; X-ray; 4.01 A; A=1-348.
PDBsum; 1BOJ; -.
PDBsum; 1BOK; -.
PDBsum; 1EDS; -.
PDBsum; 1EDV; -.
PDBsum; 1EDW; -.
PDBsum; 1EDX; -.
PDBsum; 1F88; -.
PDBsum; 1FDF; -.
PDBsum; 1GZM; -.
PDBsum; 1HZX; -.
PDBsum; 1JFP; -.
PDBsum; 1L9H; -.
PDBsum; 1LN6; -.
PDBsum; 1N3M; -.
PDBsum; 1NZS; -.
PDBsum; 1OV0; -.
PDBsum; 1OV1; -.
PDBsum; 1U19; -.
PDBsum; 1VQX; -.
PDBsum; 2G87; -.
PDBsum; 2HPY; -.
PDBsum; 2I35; -.
PDBsum; 2I36; -.
PDBsum; 2I37; -.
PDBsum; 2IQK; -.
PDBsum; 2J4Y; -.
PDBsum; 2PED; -.
PDBsum; 2X72; -.
PDBsum; 3C9L; -.
PDBsum; 3C9M; -.
PDBsum; 3CAP; -.
PDBsum; 3DQB; -.
PDBsum; 3OAX; -.
PDBsum; 3PQR; -.
PDBsum; 3PXO; -.
PDBsum; 4A4M; -.
PDBsum; 4BEY; -.
PDBsum; 4BEZ; -.
PDBsum; 4J4Q; -.
PDBsum; 4PXF; -.
PDBsum; 4X1H; -.
PDBsum; 5DYS; -.
PDBsum; 5EN0; -.
PDBsum; 5TE3; -.
PDBsum; 5TE5; -.
DisProt; DP00271; -.
ProteinModelPortal; P02699; -.
SMR; P02699; -.
BioGrid; 166570; 2.
DIP; DIP-29225N; -.
ELM; P02699; -.
IntAct; P02699; 4.
MINT; MINT-1507462; -.
STRING; 9913.ENSBTAP00000001730; -.
BindingDB; P02699; -.
ChEMBL; CHEMBL5739; -.
iPTMnet; P02699; -.
SwissPalm; P02699; -.
UniCarbKB; P02699; -.
PaxDb; P02699; -.
Ensembl; ENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneID; 509933; -.
KEGG; bta:509933; -.
CTD; 6010; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118977; -.
HOGENOM; HOG000253932; -.
HOVERGEN; HBG107442; -.
InParanoid; P02699; -.
KO; K04250; -.
OMA; LAAYMFM; -.
OrthoDB; EOG091G0BDA; -.
TreeFam; TF324998; -.
Reactome; R-BTA-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-BTA-2485179; Activation of the phototransduction cascade.
Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-BTA-418594; G alpha (i) signalling events.
Reactome; R-BTA-419771; Opsins.
Reactome; R-BTA-5620916; VxPx cargo-targeting to cilium.
EvolutionaryTrace; P02699; -.
PRO; PR:P02699; -.
Proteomes; UP000009136; Chromosome 22.
Bgee; ENSBTAG00000001310; -.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0097648; C:G-protein coupled receptor complex; IDA:CAFA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:AgBase.
GO; GO:0019867; C:outer membrane; IDA:CAFA.
GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005502; F:11-cis retinal binding; IDA:CAFA.
GO; GO:1990763; F:arrestin family protein binding; IPI:CAFA.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:CAFA.
GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA:AgBase.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0002046; F:opsin binding; IDA:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0016038; P:absorption of visible light; IDA:CAFA.
GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
GO; GO:0007603; P:phototransduction, visible light; IDA:AgBase.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
GO; GO:0009416; P:response to light stimulus; IDA:CAFA.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 4.10.840.10; -; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR001760; Opsin.
InterPro; IPR027430; Retinal_BS.
InterPro; IPR000732; Rhodopsin.
InterPro; IPR019477; Rhodopsin_N.
Pfam; PF00001; 7tm_1; 1.
Pfam; PF10413; Rhodopsin_N; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00238; OPSIN.
PRINTS; PR00579; RHODOPSIN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE; PS00238; OPSIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromophore; Complete proteome;
Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate;
Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
Retinal protein; Sensory transduction; Transducer; Transmembrane;
Transmembrane helix; Vision; Zinc.
CHAIN 1 348 Rhodopsin.
/FTId=PRO_0000197653.
TOPO_DOM 1 36 Extracellular.
TRANSMEM 37 63 Helical; Name=1.
TOPO_DOM 64 73 Cytoplasmic.
TRANSMEM 74 96 Helical; Name=2.
TOPO_DOM 97 110 Extracellular.
TRANSMEM 111 133 Helical; Name=3.
TOPO_DOM 134 152 Cytoplasmic.
TRANSMEM 153 173 Helical; Name=4.
TOPO_DOM 174 202 Extracellular.
TRANSMEM 203 224 Helical; Name=5.
TOPO_DOM 225 249 Cytoplasmic.
TRANSMEM 250 274 Helical; Name=6.
TOPO_DOM 275 286 Extracellular.
TRANSMEM 287 308 Helical; Name=7.
TOPO_DOM 309 348 Cytoplasmic.
REGION 113 125 Retinal chromophore binding.
REGION 207 212 Retinal chromophore binding.
MOTIF 134 137 'Ionic lock' involved in activated form
stabilization.
METAL 201 201 Zinc. {ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1HZX,
ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302}.
METAL 279 279 Zinc. {ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1HZX,
ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302}.
BINDING 265 265 Retinal chromophore.
{ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:17449675}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:6759163}.
MOD_RES 296 296 N6-(retinylidene)lysine.
MOD_RES 334 334 Phosphoserine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 335 335 Phosphothreonine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 336 336 Phosphothreonine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 342 342 Phosphothreonine.
{ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
MOD_RES 343 343 Phosphoserine; by RK and GRK7.
{ECO:0000269|PubMed:1396673,
ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781}.
LIPID 322 322 S-palmitoyl cysteine.
{ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:1512231,
ECO:0000269|PubMed:3350146}.
LIPID 323 323 S-palmitoyl cysteine.
{ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:1512231,
ECO:0000269|PubMed:3350146}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:468821,
ECO:0000269|PubMed:6759163}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:468821,
ECO:0000269|PubMed:6759163}.
DISULFID 110 187 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:2145276}.
MUTAGEN 2 2 N->C: Stabilized by a disulfide bond and
normal light absorption; when associated
with C-282 and D-15.
{ECO:0000269|PubMed:17825322}.
MUTAGEN 15 15 N->D: Normal light absorption; when
associated with C-2 and C-282.
{ECO:0000269|PubMed:17825322}.
MUTAGEN 282 282 D->C: Stabilized by a disulfide bond and
normal light absorption; when associated
with C-2 and D-15.
{ECO:0000269|PubMed:17825322}.
CONFLICT 281 281 S -> F (in Ref. 3; AAA30675).
{ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:1U19}.
STRAND 10 13 {ECO:0000244|PDB:1U19}.
HELIX 15 17 {ECO:0000244|PDB:4PXF}.
TURN 23 25 {ECO:0000244|PDB:1U19}.
TURN 29 31 {ECO:0000244|PDB:1U19}.
HELIX 34 64 {ECO:0000244|PDB:1U19}.
HELIX 66 68 {ECO:0000244|PDB:4X1H}.
HELIX 71 89 {ECO:0000244|PDB:1U19}.
HELIX 91 100 {ECO:0000244|PDB:1U19}.
HELIX 103 105 {ECO:0000244|PDB:1EDS}.
HELIX 106 139 {ECO:0000244|PDB:1U19}.
STRAND 143 145 {ECO:0000244|PDB:1U19}.
HELIX 150 168 {ECO:0000244|PDB:1U19}.
HELIX 170 172 {ECO:0000244|PDB:1U19}.
TURN 175 177 {ECO:0000244|PDB:1EDV}.
STRAND 179 181 {ECO:0000244|PDB:1U19}.
TURN 182 185 {ECO:0000244|PDB:1U19}.
STRAND 186 188 {ECO:0000244|PDB:1U19}.
HELIX 192 195 {ECO:0000244|PDB:1EDV}.
HELIX 196 198 {ECO:0000244|PDB:1U19}.
HELIX 200 210 {ECO:0000244|PDB:1U19}.
HELIX 213 223 {ECO:0000244|PDB:1U19}.
TURN 224 228 {ECO:0000244|PDB:1U19}.
TURN 229 231 {ECO:0000244|PDB:3C9M}.
TURN 235 238 {ECO:0000244|PDB:3C9L}.
STRAND 239 241 {ECO:0000244|PDB:1U19}.
HELIX 242 277 {ECO:0000244|PDB:1U19}.
TURN 278 280 {ECO:0000244|PDB:1U19}.
HELIX 285 294 {ECO:0000244|PDB:1U19}.
HELIX 295 299 {ECO:0000244|PDB:1U19}.
HELIX 301 308 {ECO:0000244|PDB:1U19}.
HELIX 311 321 {ECO:0000244|PDB:1U19}.
TURN 322 324 {ECO:0000244|PDB:4X1H}.
TURN 328 330 {ECO:0000244|PDB:1U19}.
STRAND 332 334 {ECO:0000244|PDB:1NZS}.
STRAND 336 338 {ECO:0000244|PDB:1JFP}.
STRAND 339 342 {ECO:0000244|PDB:1U19}.
SEQUENCE 348 AA; 39008 MW; 33FDA196803E81F3 CRC64;
MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP
EGMQCSCGID YYTPHEETNN ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV
YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA


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