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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.
23-MAY-2018, entry version 189.
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, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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, AND PARTIAL PROTEIN SEQUENCE.
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, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
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, AND FUNCTION.
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]
SUBUNIT, INTERACTION WITH GNAT1, RETINAL-BINDING, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23303210; DOI=10.1096/fj.12-225383;
Jastrzebska B., Orban T., Golczak M., Engel A., Palczewski K.;
"Asymmetry of the rhodopsin dimer in complex with transducin.";
FASEB J. 27:1572-1584(2013).
[14]
INTERACTION WITH SAG.
PubMed=26200343; DOI=10.1038/nature14656;
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A.,
White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J.,
Tan M.H., Zhang C., Moeller A., West G.M., Pascal B.D., Van Eps N.,
Caro L.N., Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X.,
Pal K., Ma J., Zhi X., Boutet S., Williams G.J., Messerschmidt M.,
Gati C., Zatsepin N.A., Wang D., James D., Basu S., Roy-Chowdhury S.,
Conrad C.E., Coe J., Liu H., Lisova S., Kupitz C., Grotjohann I.,
Fromme R., Jiang Y., Tan M., Yang H., Li J., Wang M., Zheng Z., Li D.,
Howe N., Zhao Y., Standfuss J., Diederichs K., Dong Y., Potter C.S.,
Carragher B., Caffrey M., Jiang H., Chapman H.N., Spence J.C.,
Fromme P., Weierstall U., Ernst O.P., Katritch V., Gurevich V.V.,
Griffin P.R., Hubbell W.L., Stevens R.C., Cherezov V., Melcher K.,
Xu H.E.;
"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray
laser.";
Nature 523:561-567(2015).
[15]
SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=28655769; DOI=10.1074/jbc.M117.797100;
Gao Y., Westfield G., Erickson J.W., Cerione R.A., Skiniotis G.,
Ramachandran S.;
"Isolation and structure-function characterization of a signaling-
active rhodopsin-G protein complex.";
J. Biol. Chem. 292:14280-14289(2017).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
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).
[17] {ECO:0000244|PDB:1HZX}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL
CHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323,
TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
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).
[18]
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).
[19]
STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS IN COMPLEX WITH
ALL-TRANS-RETINAL, FUNCTION, TOPOLOGY, AND DISULFIDE BOND.
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).
[20] {ECO:0000244|PDB:1L9H}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC AND
ALL-TRANS-RETINAL, TOPOLOGY, GLYCOSYLATION AT ASN-15, PALMITOYLATION
AT CYS-322 AND CYS-323, AND DISULFIDE BONDS.
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).
[21]
STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH SAG, 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).
[22] {ECO:0000244|PDB:1NZS}
STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH SAG, 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).
[23] {ECO:0000244|PDB:1U19}
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC AND
ALL-TRANS-RETINAL, TOPOLOGY, PALMITOYLATION AT CYS-322 AND CYS-323,
GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH
ALL-TRANS-RETINAL, TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15, AND
DISULFIDE BONDS.
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).
[25]
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).
[26]
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).
[27]
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).
[28]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL
CHROMOPHORE, FUNCTION, AND TOPOLOGY.
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).
[29] {ECO:0000244|PDB:2HPY}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF INACTIVATED AND ACTIVATED
FORMS IN COMPLEX WITH RETINAL CHROMOPHORE, FUNCTION, TOPOLOGY,
PALMITOYLATION AT CYS-322 AND CYS-323, GLYCOSYLATION AT ASN-2 AND
ASN-15, AND DISULFIDE BONDS.
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).
[30]
X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED
FORMS, FUNCTION, AND TOPOLOGY.
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).
[31]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS
IN COMPLEX WITH RETINAL CHROMOPHORE, FUNCTION, AND TOPOLOGY.
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).
[32]
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, TOPOLOGY, 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).
[33]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), AND TOPOLOGY.
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).
[34]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DIMERIZATION, SUBUNIT, AND
TOPOLOGY.
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).
[35] {ECO:0000244|PDB:3DQB}
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH GNAT1,
FUNCTION, ACTIVATION MECHANISM, TOPOLOGY, GLYCOSYLATION AT ASN-2 AND
ASN-15, PALMITOYLATION AT CYS-322 AND CYS-323, AND DISULFIDE BONDS.
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).
[36] {ECO:0000244|PDB:2X72}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF MUTANT GLN-113 IN COMPLEX
WITH GNAT1, FUNCTION, GLYCOSYLATION AT ASN-15, DISULFIDE BONDS, AND
MUTAGENESIS OF GLU-113.
PubMed=21389983; DOI=10.1038/NATURE09795;
Standfuss J., Edwards P.C., D'Antona A., Fransen M., Xie G.,
Oprian D.D., Schertler G.F.;
"The structural basis of agonist-induced activation in constitutively
active rhodopsin.";
Nature 471:656-660(2011).
[37] {ECO:0000244|PDB:4A4M}
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT TYR-257 IN COMPLEX
WITH ALL-TRANS-RETINAL AND GNAT3, FUNCTION, PALMITOYLATION AT CYS-323,
GLYCOSYLATION AT ASN-15, DISULFIDE BOND, AND MUTAGENESIS OF MET-257.
PubMed=22198838; DOI=10.1073/PNAS.1114089108;
Deupi X., Edwards P., Singhal A., Nickle B., Oprian D., Schertler G.,
Standfuss J.;
"Stabilized G protein binding site in the structure of constitutively
active metarhodopsin-II.";
Proc. Natl. Acad. Sci. U.S.A. 109:119-124(2012).
[38] {ECO:0000244|PDB:4BEY, ECO:0000244|PDB:4BEZ}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF MUTANT ASP-90 IN COMPLEX
WITH GNAT1, INTERACTION WITH GNAT1 AND SAG, TOPOLOGY, GLYCOSYLATION AT
ASN-15, PALMITOYLATION AT CYS-323, DISULFIDE BONDS, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF GLY-90.
PubMed=23579341; DOI=10.1038/EMBOR.2013.44;
Singhal A., Ostermaier M.K., Vishnivetskiy S.A., Panneels V.,
Homan K.T., Tesmer J.J., Veprintsev D., Deupi X., Gurevich V.V.,
Schertler G.F., Standfuss J.;
"Insights into congenital stationary night blindness based on the
structure of G90D rhodopsin.";
EMBO Rep. 14:520-526(2013).
[39] {ECO:0000244|PDB:4PXF}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAG PEPTIDE,
FUNCTION, INTERACTION WITH SAG AND GNAT1, TOPOLOGY, GLYCOSYLATION AT
ASN-15, AND DISULFIDE BONDS.
PubMed=25205354; DOI=10.1038/ncomms5801;
Szczepek M., Beyriere F., Hofmann K.P., Elgeti M., Kazmin R., Rose A.,
Bartl F.J., von Stetten D., Heck M., Sommer M.E., Hildebrand P.W.,
Scheerer P.;
"Crystal structure of a common GPCR-binding interface for G protein
and arrestin.";
Nat. Commun. 5:4801-4801(2014).
[40] {ECO:0000244|PDB:4X1H}
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH GNAT1 PEPTIDE,
TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15, PALMITOYLATION AT CYS-322
AND CYS-323, AND DISULFIDE BOND.
PubMed=26526852; DOI=10.1016/j.str.2015.09.015;
Blankenship E., Vahedi-Faridi A., Lodowski D.T.;
"The High-Resolution Structure of Activated Opsin Reveals a Conserved
Solvent Network in the Transmembrane Region Essential for
Activation.";
Structure 23:2358-2364(2015).
[41] {ECO:0000244|PDB:5DYS, ECO:0000244|PDB:5EN0}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ILE-94 IN COMPLEX
WITH ALL-TRANS-RETINAL AND GNAT3, FUNCTION, TOPOLOGY, GLYCOSYLATION AT
ASN-15, PALMITOYLATION AT CYS-322 AND CYS-323, DISULFIDE BONDS, AND
MUTAGENESIS OF THR-94.
PubMed=27458239; DOI=10.15252/embr.201642671;
Singhal A., Guo Y., Matkovic M., Schertler G., Deupi X., Yan E.C.,
Standfuss J.;
"Structural role of the T94I rhodopsin mutation in congenital
stationary night blindness.";
EMBO Rep. 17:1431-1440(2016).
-!- FUNCTION: Photoreceptor required for image-forming vision at low
light intensity. Required for photoreceptor cell viability after
birth (By similarity). Light-induced isomerization of 11-cis to
all-trans retinal triggers a conformational change that activates
signaling via G-proteins (PubMed:10926528, PubMed:12044163,
PubMed:11972040, PubMed:16908857, PubMed:16586416,
PubMed:17060607, PubMed:17449675, PubMed:18818650,
PubMed:21389983, PubMed:22198838, PubMed:23579341,
PubMed:25205354, PubMed:27458239). Subsequent receptor
phosphorylation mediates displacement of the bound G-protein alpha
subunit by the arrestin SAG and terminates signaling
(PubMed:1396673, PubMed:15111114). {ECO:0000250|UniProtKB:P08100,
ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:27458239, ECO:0000305|PubMed:10926528,
ECO:0000305|PubMed:11972040, ECO:0000305|PubMed:12044163,
ECO:0000305|PubMed:15111114, ECO:0000305|PubMed:26526852}.
-!- SUBUNIT: Homodimer (PubMed:23303210, PubMed:18563085). Interacts
(phosphorylated form) with SAG (PubMed:26200343, PubMed:15111114,
PubMed:15351781, PubMed:23579341, PubMed:25205354). Interacts with
GNAT1 (PubMed:23303210, PubMed:28655769, PubMed:18818650,
PubMed:21389983, PubMed:23579341, PubMed:26526852), Interacts with
GNAT3 (PubMed:22198838, PubMed:27458239). SAG and G-proteins
compete for a common binding site (PubMed:25205354). Interacts
with GRK1 (By similarity). {ECO:0000250|UniProtKB:P08100,
ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:15111114,
ECO:0000269|PubMed:15351781, ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:28655769}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-8592832, EBI-8592832;
P04695:GNAT1; NbExp=3; IntAct=EBI-8592832, EBI-7052221;
P08168-1:SAG; NbExp=23; IntAct=EBI-8592832, EBI-15575296;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
ECO:0000269|PubMed:3350146, ECO:0000269|PubMed:9541408}; Multi-
pass membrane protein {ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239}. Cell
projection, cilium, photoreceptor outer segment
{ECO:0000269|PubMed:28655769, ECO:0000269|PubMed:3350146,
ECO:0000269|PubMed:9541408}. Note=Synthesized in the inner segment
(IS) of rod photoreceptor cells before vectorial transport to disk
membranes in the rod outer segment (OS) photosensory cilia.
{ECO:0000250|UniProtKB:P08100}.
-!- TISSUE SPECIFICITY: Expressed in rod-shaped photoreceptor cells in
the retina that mediate vision in dim light (at protein level).
{ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769,
ECO:0000269|PubMed:3350146, ECO:0000269|PubMed:9541408}.
-!- 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. Upon
light absorption, the covalently bound 11-cis-retinal is converted
to all-trans-retinal. After hydrolysis of the Schiff base and
release of the covalently bound all-trans-retinal, active
rhodopsin is regenerated by binding of a fresh molecule of 11-cis-
retinal. {ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:27458239,
ECO:0000269|PubMed:6870827, ECO:0000305|PubMed:6759163}.
-!- 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.
PDB; 5WKT; X-ray; 3.20 A; A=1-348.
PDB; 6FK6; X-ray; 2.36 A; A=1-326.
PDB; 6FK7; X-ray; 2.62 A; A=1-348.
PDB; 6FK8; X-ray; 2.87 A; A=1-348.
PDB; 6FK9; X-ray; 2.63 A; A=1-348.
PDB; 6FKA; X-ray; 2.70 A; A=1-348.
PDB; 6FKB; X-ray; 3.03 A; A=1-328.
PDB; 6FKC; X-ray; 2.46 A; A=1-348.
PDB; 6FKD; X-ray; 2.49 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; -.
PDBsum; 5WKT; -.
PDBsum; 6FK6; -.
PDBsum; 6FK7; -.
PDBsum; 6FK8; -.
PDBsum; 6FK9; -.
PDBsum; 6FKA; -.
PDBsum; 6FKB; -.
PDBsum; 6FKC; -.
PDBsum; 6FKD; -.
DisProt; DP00271; -.
ProteinModelPortal; P02699; -.
SMR; P02699; -.
BioGrid; 166570; 2.
DIP; DIP-29225N; -.
ELM; P02699; -.
IntAct; P02699; 5.
MINT; P02699; -.
STRING; 9913.ENSBTAP00000001730; -.
BindingDB; P02699; -.
ChEMBL; CHEMBL5739; -.
GlyConnect; 523; -.
iPTMnet; P02699; -.
SwissPalm; P02699; -.
UniCarbKB; P02699; -.
PaxDb; P02699; -.
Ensembl; ENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneID; 509933; -.
KEGG; bta:509933; -.
CTD; 6010; -.
VGNC; VGNC:33942; RHO.
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:0016021; C:integral component of membrane; IDA:UniProtKB.
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; ISS:UniProtKB.
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:UniProtKB.
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:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:UniProtKB.
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: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; IDA:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; Cell projection; 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.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 37 61 Helical; Name=1.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 62 73 Cytoplasmic.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 74 96 Helical; Name=2.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 97 110 Extracellular.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 111 133 Helical; Name=3.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 134 152 Cytoplasmic.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 153 173 Helical; Name=4.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 174 202 Extracellular.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 203 224 Helical; Name=5.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 225 252 Cytoplasmic.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 253 274 Helical; Name=6.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 275 286 Extracellular.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TRANSMEM 287 308 Helical; Name=7.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
TOPO_DOM 309 348 Cytoplasmic.
{ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17060607,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:17825322,
ECO:0000269|PubMed:18563085,
ECO:0000269|PubMed:18645239,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239}.
REGION 330 348 Interaction with SAG.
{ECO:0000269|PubMed:15111114}.
MOTIF 134 136 'Ionic lock' involved in activated form
stabilization.
{ECO:0000305|PubMed:21389983,
ECO:0000305|PubMed:22198838,
ECO:0000305|PubMed:26526852,
ECO:0000305|PubMed:27458239}.
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}.
SITE 113 113 Plays an important role in the
conformation switch to the active
conformation.
{ECO:0000269|PubMed:21389983,
ECO:0000305|PubMed:22198838,
ECO:0000305|PubMed:23579341,
ECO:0000305|PubMed:27458239}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000305|PubMed:6759163}.
MOD_RES 296 296 N6-(retinylidene)lysine.
{ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1GZM,
ECO:0000244|PDB:1HZX,
ECO:0000244|PDB:1JFP,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:3C9L,
ECO:0000244|PDB:3OAX,
ECO:0000244|PDB:3PQR,
ECO:0000244|PDB:3PXO,
ECO:0000244|PDB:5DYS,
ECO:0000269|PubMed:10926528,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16586416,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:17449675,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23303210,
ECO:0000269|PubMed:27458239,
ECO:0000269|PubMed:6870827,
ECO:0000305|PubMed:6759163}.
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:0000244|PDB:1HZX,
ECO:0000244|PDB:1L9H,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:4X1H,
ECO:0000244|PDB:5DYS,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:1512231,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239,
ECO:0000269|PubMed:3350146}.
LIPID 323 323 S-palmitoyl cysteine.
{ECO:0000244|PDB:1HZX,
ECO:0000244|PDB:1L9H,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:4BEY,
ECO:0000244|PDB:4PXF,
ECO:0000244|PDB:4X1H,
ECO:0000244|PDB:5DYS,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:1512231,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:27458239,
ECO:0000269|PubMed:3350146}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1GZM,
ECO:0000244|PDB:1HZX,
ECO:0000244|PDB:1U19,
ECO:0000244|PDB:2G87,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:2I35,
ECO:0000244|PDB:2I36,
ECO:0000244|PDB:2I37,
ECO:0000244|PDB:2PED,
ECO:0000244|PDB:3C9L,
ECO:0000244|PDB:3CAP,
ECO:0000244|PDB:3DQB,
ECO:0000244|PDB:3OAX,
ECO:0000244|PDB:3PQR,
ECO:0000244|PDB:3PXO,
ECO:0000244|PDB:4X1H,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:468821,
ECO:0000269|PubMed:6759163}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1GZM,
ECO:0000244|PDB:1HZX,
ECO:0000244|PDB:1L9H,
ECO:0000244|PDB:1U19,
ECO:0000244|PDB:2G87,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:2I35,
ECO:0000244|PDB:2I36,
ECO:0000244|PDB:2I37,
ECO:0000244|PDB:2J4Y,
ECO:0000244|PDB:2PED,
ECO:0000244|PDB:2X72,
ECO:0000244|PDB:3C9L,
ECO:0000244|PDB:3C9M,
ECO:0000244|PDB:3CAP,
ECO:0000244|PDB:3DQB,
ECO:0000244|PDB:3OAX,
ECO:0000244|PDB:3PQR,
ECO:0000244|PDB:3PXO,
ECO:0000244|PDB:4A4M,
ECO:0000244|PDB:4BEY,
ECO:0000244|PDB:4BEZ,
ECO:0000244|PDB:4J4Q,
ECO:0000244|PDB:4PXF,
ECO:0000244|PDB:4X1H,
ECO:0000244|PDB:5DYS,
ECO:0000244|PDB:5EN0,
ECO:0000244|PDB:5TE3,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:25205354,
ECO:0000269|PubMed:26526852,
ECO:0000269|PubMed:468821,
ECO:0000269|PubMed:6759163}.
DISULFID 110 187 {ECO:0000244|PDB:1F88,
ECO:0000244|PDB:1GZM,
ECO:0000244|PDB:1HZX,
ECO:0000244|PDB:1JFP,
ECO:0000244|PDB:1L9H,
ECO:0000244|PDB:1LN6,
ECO:0000244|PDB:1U19,
ECO:0000244|PDB:2G87,
ECO:0000244|PDB:2HPY,
ECO:0000244|PDB:2I35,
ECO:0000244|PDB:2I36,
ECO:0000244|PDB:2I37,
ECO:0000244|PDB:2J4Y,
ECO:0000244|PDB:2PED,
ECO:0000244|PDB:2X72,
ECO:0000244|PDB:3C9L,
ECO:0000244|PDB:3C9M,
ECO:0000244|PDB:3CAP,
ECO:0000244|PDB:3DQB,
ECO:0000244|PDB:3OAX,
ECO:0000244|PDB:3PQR,
ECO:0000244|PDB:3PXO,
ECO:0000244|PDB:4A4M,
ECO:0000244|PDB:4BEY,
ECO:0000244|PDB:4BEZ,
ECO:0000244|PDB:4J4Q,
ECO:0000244|PDB:4PXF,
ECO:0000244|PDB:4X1H,
ECO:0000244|PDB:5DYS,
ECO:0000244|PDB:5EN0,
ECO:0000244|PDB:5TE3,
ECO:0000244|PDB:5TE5,
ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:11425302,
ECO:0000269|PubMed:11972040,
ECO:0000269|PubMed:12044163,
ECO:0000269|PubMed:15327956,
ECO:0000269|PubMed:15491621,
ECO:0000269|PubMed:16908857,
ECO:0000269|PubMed:18818650,
ECO:0000269|PubMed:21389983,
ECO:0000269|PubMed:2145276,
ECO:0000269|PubMed:22198838,
ECO:0000269|PubMed:23579341,
ECO:0000269|PubMed:26526852}.
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 90 90 G->D: Increased thermal stability and
decreased retinal uptake. Decreases
stability of the inactive conformation.
{ECO:0000269|PubMed:23579341}.
MUTAGEN 94 94 T->I: Stabilizes the activated
conformation and hinders hydrolysis of
the covalent bond that retains all-trans-
retinol. {ECO:0000269|PubMed:27458239}.
MUTAGEN 113 113 E->Q: Causes shift to the activated
conformation.
{ECO:0000269|PubMed:21389983}.
MUTAGEN 257 257 M->Y: Causes shift to the activated
conformation.
{ECO:0000269|PubMed:22198838}.
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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