OPSD_BOVIN
ID OPSD_BOVIN Reviewed; 348 AA.
AC P02699;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, RETINAL-BINDING SITE AT LYS-296, AND ACETYLATION AT
RP MET-1.
RX PubMed=6759163; DOI=10.1016/0014-5793(82)80805-3;
RA Ovchinnikov Y.A.;
RT "Rhodopsin and bacteriorhodopsin: structure-function relationships.";
RL FEBS Lett. 148:179-191(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6194890; DOI=10.1016/0092-8674(83)90537-8;
RA Nathans J., Hogness D.S.;
RT "Isolation, sequence analysis, and intron-exon arrangement of the gene
RT encoding bovine rhodopsin.";
RL Cell 34:807-814(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
RX PubMed=2950966; DOI=10.1016/0169-328x(86)90031-8;
RA Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N.;
RT "Multiple opsin mRNA species in bovine retina.";
RL Brain Res. 387:251-260(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
RX PubMed=6228228; DOI=10.1016/0006-291x(83)90560-0;
RA Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M.,
RA Tokunaga F.;
RT "Isolation and nucleotide sequence of a partial cDNA clone for bovine
RT opsin.";
RL Biochem. Biophys. Res. Commun. 116:563-567(1983).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9541408; DOI=10.1002/pro.5560070325;
RA Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B.,
RA Galijatovic A., Chen N., Crouch R.K., Knapp D.R.;
RT "Mass spectrometric analysis of integral membrane proteins: application to
RT complete mapping of bacteriorhodopsins and rhodopsin.";
RL Protein Sci. 7:758-764(1998).
RN [6]
RP GLYCOSYLATION AT ASN-2 AND ASN-15.
RX PubMed=468821; DOI=10.1016/s0021-9258(19)86876-x;
RA Fukuda M.N., Papermaster D.S., Hargrave P.A.;
RT "Rhodopsin carbohydrate. Structure of small oligosaccharides attached at
RT two sites near the NH2 terminus.";
RL J. Biol. Chem. 254:8201-8207(1979).
RN [7]
RP RETINAL-BINDING SITE, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6870827; DOI=10.1042/bj2110045;
RA Mullen E., Akhtar M.;
RT "Structural studies on membrane-bound bovine rhodopsin.";
RL Biochem. J. 211:45-54(1983).
RN [8]
RP PALMITOYLATION AT CYS-322 AND CYS-323, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3350146; DOI=10.1016/0014-5793(88)80628-8;
RA Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.;
RT "Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of
RT bovine rhodopsin are palmitylated.";
RL FEBS Lett. 230:1-5(1988).
RN [9]
RP DISULFIDE BOND.
RX PubMed=2145276; DOI=10.1016/s0021-9258(18)38195-x;
RA Karnik S.S., Khorana H.G.;
RT "Assembly of functional rhodopsin requires a disulfide bond between
RT cysteine residues 110 and 187.";
RL J. Biol. Chem. 265:17520-17524(1990).
RN [10]
RP PHOSPHORYLATION AT SER-343, AND FUNCTION.
RX PubMed=1396673; DOI=10.1111/j.1432-1033.1992.tb17232.x;
RA Brown N.G., Fowles C., Sharma R., Akhtar M.;
RT "Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation
RT of C-terminal peptides of rhodopsin.";
RL Eur. J. Biochem. 208:659-667(1992).
RN [11]
RP PALMITOYLATION AT CYS-322 AND CYS-323.
RX PubMed=1512231; DOI=10.1016/s0021-9258(18)41868-6;
RA Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.;
RT "Palmitylation of a G-protein coupled receptor. Direct analysis by tandem
RT mass spectrometry.";
RL J. Biol. Chem. 267:16889-16894(1992).
RN [12]
RP MUTAGENESIS.
RX PubMed=9405601; DOI=10.1073/pnas.94.26.14267;
RA Cai K., Langen R., Hubbell W.L., Khorana H.G.;
RT "Structure and function in rhodopsin: topology of the C-terminal
RT polypeptide chain in relation to the cytoplasmic loops.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997).
RN [13]
RP INTERACTION WITH RCVRN AND GRK1.
RX PubMed=17020884; DOI=10.1074/jbc.m606913200;
RA Ames J.B., Levay K., Wingard J.N., Lusin J.D., Slepak V.Z.;
RT "Structural basis for calcium-induced inhibition of rhodopsin kinase by
RT recoverin.";
RL J. Biol. Chem. 281:37237-37245(2006).
RN [14]
RP SUBUNIT, INTERACTION WITH GNAT1, RETINAL-BINDING, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23303210; DOI=10.1096/fj.12-225383;
RA Jastrzebska B., Orban T., Golczak M., Engel A., Palczewski K.;
RT "Asymmetry of the rhodopsin dimer in complex with transducin.";
RL FASEB J. 27:1572-1584(2013).
RN [15]
RP INTERACTION WITH SAG.
RX PubMed=26200343; DOI=10.1038/nature14656;
RA Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A.,
RA White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H.,
RA Zhang C., Moeller A., West G.M., Pascal B.D., Van Eps N., Caro L.N.,
RA Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J.,
RA Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A.,
RA Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H.,
RA Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H.,
RA Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J.,
RA Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H.,
RA Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P.,
RA Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C.,
RA Cherezov V., Melcher K., Xu H.E.;
RT "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray
RT laser.";
RL Nature 523:561-567(2015).
RN [16]
RP INTERACTION WITH PRCD, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27509380; DOI=10.1021/acs.biochem.6b00489;
RA Spencer W.J., Pearring J.N., Salinas R.Y., Loiselle D.R., Skiba N.P.,
RA Arshavsky V.Y.;
RT "Progressive Rod-Cone Degeneration (PRCD) Protein Requires N-Terminal S-
RT Acylation and Rhodopsin Binding for Photoreceptor Outer Segment
RT Localization and Maintaining Intracellular Stability.";
RL Biochemistry 55:5028-5037(2016).
RN [17]
RP SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=28655769; DOI=10.1074/jbc.m117.797100;
RA Gao Y., Westfield G., Erickson J.W., Cerione R.A., Skiniotis G.,
RA Ramachandran S.;
RT "Isolation and structure-function characterization of a signaling-active
RT rhodopsin-G protein complex.";
RL J. Biol. Chem. 292:14280-14289(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP ALL-TRANS-RETINAL, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION
RP AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
RX PubMed=10926528; DOI=10.1126/science.289.5480.739;
RA Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A.,
RA Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., Miyano M.;
RT "Crystal structure of rhodopsin: a G protein-coupled receptor.";
RL Science 289:739-745(2000).
RN [19] {ECO:0007744|PDB:1HZX}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE
RP AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, TOPOLOGY,
RP GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
RX PubMed=11425302; DOI=10.1021/bi0155091;
RA Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
RT "Advances in determination of a high-resolution three-dimensional structure
RT of rhodopsin, a model of G-protein-coupled receptors (GPCRs).";
RL Biochemistry 40:7761-7772(2001).
RN [20]
RP STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
RX PubMed=11570894; DOI=10.1021/bi015543f;
RA Yeagle P.L., Choi G., Albert A.D.;
RT "Studies on the structure of the G-protein-coupled receptor rhodopsin
RT including the putative G-protein binding site in unactivated and activated
RT forms.";
RL Biochemistry 40:11932-11937(2001).
RN [21]
RP STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS IN COMPLEX WITH
RP ALL-TRANS-RETINAL, FUNCTION, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=12044163; DOI=10.1021/bi025507w;
RA Choi G., Landin J., Galan J.F., Birge R.R., Albert A.D., Yeagle P.L.;
RT "Structural studies of metarhodopsin II, the activated form of the G-
RT protein coupled receptor, rhodopsin.";
RL Biochemistry 41:7318-7324(2002).
RN [22] {ECO:0007744|PDB:1L9H}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC AND
RP ALL-TRANS-RETINAL, TOPOLOGY, GLYCOSYLATION AT ASN-15, PALMITOYLATION AT
RP CYS-322 AND CYS-323, AND DISULFIDE BONDS.
RX PubMed=11972040; DOI=10.1073/pnas.082666399;
RA Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y.;
RT "Functional role of internal water molecules in rhodopsin revealed by X-ray
RT crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002).
RN [23]
RP STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH SAG, AND PHOSPHORYLATION AT
RP SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
RX PubMed=15111114; DOI=10.1016/s0014-5793(04)00226-1;
RA Kisselev O.G., McDowell J.H., Hargrave P.A.;
RT "The arrestin-bound conformation and dynamics of the phosphorylated
RT carboxy-terminal region of rhodopsin.";
RL FEBS Lett. 564:307-311(2004).
RN [24] {ECO:0007744|PDB:1NZS}
RP STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH SAG, AND PHOSPHORYLATION AT
RP SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
RX PubMed=15351781; DOI=10.1074/jbc.m407341200;
RA Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.;
RT "Conformational changes in the phosphorylated C-terminal domain of
RT rhodopsin during rhodopsin arrestin interactions.";
RL J. Biol. Chem. 279:51203-51207(2004).
RN [25] {ECO:0007744|PDB:1U19}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC AND
RP ALL-TRANS-RETINAL, TOPOLOGY, PALMITOYLATION AT CYS-322 AND CYS-323,
RP GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BOND.
RX PubMed=15327956; DOI=10.1016/j.jmb.2004.07.044;
RA Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V.;
RT "The retinal conformation and its environment in rhodopsin in light of a
RT new 2.2 A crystal structure.";
RL J. Mol. Biol. 342:571-583(2004).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINAL,
RP TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE BONDS.
RX PubMed=15491621; DOI=10.1016/j.jmb.2004.08.090;
RA Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F.;
RT "Structure of bovine rhodopsin in a trigonal crystal form.";
RL J. Mol. Biol. 343:1409-1438(2004).
RN [27]
RP STRUCTURE BY NMR OF 231-252.
RX PubMed=7578070; DOI=10.1021/bi00045a002;
RA Yeagle P.L., Alderfer J.L., Albert A.D.;
RT "Structure of the third cytoplasmic loop of bovine rhodopsin.";
RL Biochemistry 34:14621-14625(1995).
RN [28]
RP STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
RX PubMed=10888202; DOI=10.1034/j.1399-3011.2000.00707.x;
RA Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G.,
RA Alderfer J.L., Albert A.D.;
RT "Structures of the intradiskal loops and amino terminus of the G-protein
RT receptor, rhodopsin.";
RL J. Pept. Res. 55:455-465(2000).
RN [29]
RP STRUCTURE BY NMR OF 291-315.
RX PubMed=10930473;
RA Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D.;
RT "Three dimensional structure of the seventh transmembrane helical domain of
RT the G-protein receptor, rhodopsin.";
RL Mol. Vis. 6:125-131(2000).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE,
RP FUNCTION, AND TOPOLOGY.
RX PubMed=16586416; DOI=10.1002/anie.200600595;
RA Nakamichi H., Okada T.;
RT "Crystallographic analysis of primary visual photochemistry.";
RL Angew. Chem. Int. Ed. 45:4270-4273(2006).
RN [31] {ECO:0007744|PDB:2HPY}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF INACTIVATED AND ACTIVATED FORMS
RP IN COMPLEX WITH RETINAL CHROMOPHORE, FUNCTION, TOPOLOGY, PALMITOYLATION AT
RP CYS-322 AND CYS-323, GLYCOSYLATION AT ASN-2 AND ASN-15, AND DISULFIDE
RP BONDS.
RX PubMed=16908857; DOI=10.1073/pnas.0601765103;
RA Nakamichi H., Okada T.;
RT "Local peptide movement in the photoreaction intermediate of rhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12729-12734(2006).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS,
RP FUNCTION, AND TOPOLOGY.
RX PubMed=17060607; DOI=10.1073/pnas.0608022103;
RA Salom D., Lodowski D.T., Stenkamp R.E., Le Trong I., Golczak M.,
RA Jastrzebska B., Harris T., Ballesteros J.A., Palczewski K.;
RT "Crystal structure of a photoactivated deprotonated intermediate of
RT rhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16123-16128(2006).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS IN
RP COMPLEX WITH RETINAL CHROMOPHORE, FUNCTION, AND TOPOLOGY.
RX PubMed=17449675; DOI=10.1529/biophysj.107.108225;
RA Nakamichi H., Buss V., Okada T.;
RT "Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by
RT x-ray crystallography.";
RL Biophys. J. 92:L106-L108(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, TOPOLOGY, AND MUTAGENESIS
RP OF ASN-2; ASN-15 AND ASP-282.
RX PubMed=17825322; DOI=10.1016/j.jmb.2007.03.007;
RA Standfuss J., Xie G., Edwards P.C., Burghammer M., Oprian D.D.,
RA Schertler G.F.;
RT "Crystal structure of a thermally stable rhodopsin mutant.";
RL J. Mol. Biol. 372:1179-1188(2007).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), AND TOPOLOGY.
RX PubMed=18645239; DOI=10.1107/s0907444908017162;
RA Stenkamp R.E.;
RT "Alternative models for two crystal structures of bovine rhodopsin.";
RL Acta Crystallogr. D 64:902-904(2008).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DIMERIZATION, SUBUNIT, AND
RP TOPOLOGY.
RX PubMed=18563085; DOI=10.1038/nature07063;
RA Park J.H., Scheerer P., Hofmann K.P., Choe H.-W., Ernst O.P.;
RT "Crystal structure of the ligand-free G-protein-coupled receptor opsin.";
RL Nature 454:183-187(2008).
RN [37] {ECO:0007744|PDB:3DQB}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH GNAT1, FUNCTION,
RP ACTIVATION MECHANISM, TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15,
RP PALMITOYLATION AT CYS-322 AND CYS-323, AND DISULFIDE BONDS.
RX PubMed=18818650; DOI=10.1038/nature07330;
RA Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.-W.,
RA Hofmann K.P., Ernst O.P.;
RT "Crystal structure of opsin in its G-protein-interacting conformation.";
RL Nature 455:497-502(2008).
RN [38] {ECO:0007744|PDB:2X72}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF MUTANT GLN-113 IN COMPLEX WITH
RP GNAT1, FUNCTION, GLYCOSYLATION AT ASN-15, DISULFIDE BONDS, AND MUTAGENESIS
RP OF GLU-113.
RX PubMed=21389983; DOI=10.1038/nature09795;
RA Standfuss J., Edwards P.C., D'Antona A., Fransen M., Xie G., Oprian D.D.,
RA Schertler G.F.;
RT "The structural basis of agonist-induced activation in constitutively
RT active rhodopsin.";
RL Nature 471:656-660(2011).
RN [39] {ECO:0007744|PDB:4A4M}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT TYR-257 IN COMPLEX WITH
RP ALL-TRANS-RETINAL AND GNAT3, FUNCTION, PALMITOYLATION AT CYS-323,
RP GLYCOSYLATION AT ASN-15, DISULFIDE BOND, AND MUTAGENESIS OF MET-257.
RX PubMed=22198838; DOI=10.1073/pnas.1114089108;
RA Deupi X., Edwards P., Singhal A., Nickle B., Oprian D., Schertler G.,
RA Standfuss J.;
RT "Stabilized G protein binding site in the structure of constitutively
RT active metarhodopsin-II.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:119-124(2012).
RN [40] {ECO:0007744|PDB:4BEY, ECO:0007744|PDB:4BEZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF MUTANT ASP-90 IN COMPLEX WITH
RP GNAT1, INTERACTION WITH GNAT1 AND SAG, TOPOLOGY, GLYCOSYLATION AT ASN-15,
RP PALMITOYLATION AT CYS-323, DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF GLY-90.
RX PubMed=23579341; DOI=10.1038/embor.2013.44;
RA Singhal A., Ostermaier M.K., Vishnivetskiy S.A., Panneels V., Homan K.T.,
RA Tesmer J.J., Veprintsev D., Deupi X., Gurevich V.V., Schertler G.F.,
RA Standfuss J.;
RT "Insights into congenital stationary night blindness based on the structure
RT of G90D rhodopsin.";
RL EMBO Rep. 14:520-526(2013).
RN [41] {ECO:0007744|PDB:4PXF}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAG PEPTIDE,
RP FUNCTION, INTERACTION WITH SAG AND GNAT1, TOPOLOGY, GLYCOSYLATION AT
RP ASN-15, AND DISULFIDE BONDS.
RX PubMed=25205354; DOI=10.1038/ncomms5801;
RA Szczepek M., Beyriere F., Hofmann K.P., Elgeti M., Kazmin R., Rose A.,
RA Bartl F.J., von Stetten D., Heck M., Sommer M.E., Hildebrand P.W.,
RA Scheerer P.;
RT "Crystal structure of a common GPCR-binding interface for G protein and
RT arrestin.";
RL Nat. Commun. 5:4801-4801(2014).
RN [42] {ECO:0007744|PDB:4X1H}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH GNAT1 PEPTIDE,
RP TOPOLOGY, GLYCOSYLATION AT ASN-2 AND ASN-15, PALMITOYLATION AT CYS-322 AND
RP CYS-323, AND DISULFIDE BOND.
RX PubMed=26526852; DOI=10.1016/j.str.2015.09.015;
RA Blankenship E., Vahedi-Faridi A., Lodowski D.T.;
RT "The High-Resolution Structure of Activated Opsin Reveals a Conserved
RT Solvent Network in the Transmembrane Region Essential for Activation.";
RL Structure 23:2358-2364(2015).
RN [43] {ECO:0007744|PDB:5DYS, ECO:0007744|PDB:5EN0}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ILE-94 IN COMPLEX WITH
RP ALL-TRANS-RETINAL AND GNAT3, FUNCTION, TOPOLOGY, GLYCOSYLATION AT ASN-15,
RP PALMITOYLATION AT CYS-322 AND CYS-323, DISULFIDE BONDS, AND MUTAGENESIS OF
RP THR-94.
RX PubMed=27458239; DOI=10.15252/embr.201642671;
RA Singhal A., Guo Y., Matkovic M., Schertler G., Deupi X., Yan E.C.,
RA Standfuss J.;
RT "Structural role of the T94I rhodopsin mutation in congenital stationary
RT night blindness.";
RL EMBO Rep. 17:1431-1440(2016).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Required for photoreceptor cell viability after birth (By
CC similarity). Light-induced isomerization of 11-cis to all-trans retinal
CC triggers a conformational change that activates signaling via G-
CC proteins (PubMed:10926528, PubMed:12044163, PubMed:11972040,
CC PubMed:16908857, PubMed:16586416, PubMed:17060607, PubMed:17449675,
CC PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341,
CC PubMed:25205354, PubMed:27458239). Subsequent receptor phosphorylation
CC mediates displacement of the bound G-protein alpha subunit by the
CC arrestin SAG and terminates signaling (PubMed:1396673,
CC PubMed:15111114). {ECO:0000250|UniProtKB:P08100,
CC ECO:0000269|PubMed:1396673, ECO:0000269|PubMed:16586416,
CC ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
CC ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:18818650,
CC ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838,
CC ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354,
CC ECO:0000269|PubMed:27458239, ECO:0000305|PubMed:10926528,
CC ECO:0000305|PubMed:11972040, ECO:0000305|PubMed:12044163,
CC ECO:0000305|PubMed:15111114, ECO:0000305|PubMed:26526852}.
CC -!- SUBUNIT: Homodimer (PubMed:23303210, PubMed:18563085). May form a
CC complex composed of RHO, GRK1 and RCVRN in a Ca(2+)-dependent manner;
CC RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884).
CC Interacts with GRK1 (By similarity). Interacts (phosphorylated form)
CC with SAG (PubMed:26200343, PubMed:15111114, PubMed:15351781,
CC PubMed:23579341, PubMed:25205354). Interacts with GNAT1
CC (PubMed:23303210, PubMed:28655769, PubMed:18818650, PubMed:21389983,
CC PubMed:23579341, PubMed:26526852). Interacts with GNAT3
CC (PubMed:22198838, PubMed:27458239). SAG and G-proteins compete for a
CC common binding site (By similarity). Interacts with PRCD; the
CC interaction promotes PRCD stability (PubMed:27509380).
CC {ECO:0000250|UniProtKB:P08100, ECO:0000269|PubMed:11425302,
CC ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781,
CC ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:17020884,
CC ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:18563085,
CC ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
CC ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
CC ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:26526852,
CC ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:27509380,
CC ECO:0000269|PubMed:28655769}.
CC -!- INTERACTION:
CC P02699; P04695: GNAT1; NbExp=3; IntAct=EBI-8592832, EBI-7052221;
CC P02699; P02699: RHO; NbExp=6; IntAct=EBI-8592832, EBI-8592832;
CC P02699; P08168-1: SAG; NbExp=23; IntAct=EBI-8592832, EBI-15575296;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10926528,
CC ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
CC ECO:0000269|PubMed:27509380, ECO:0000269|PubMed:3350146,
CC ECO:0000269|PubMed:9541408}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302,
CC ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:15327956,
CC ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
CC ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
CC ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
CC ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
CC ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
CC ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
CC ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
CC ECO:0000269|PubMed:27458239}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:27509380,
CC ECO:0000269|PubMed:28655769, ECO:0000269|PubMed:3350146,
CC ECO:0000269|PubMed:9541408}. Note=Synthesized in the inner segment (IS)
CC of rod photoreceptor cells before vectorial transport to disk membranes
CC in the rod outer segment (OS) photosensory cilia.
CC {ECO:0000250|UniProtKB:P08100}.
CC -!- TISSUE SPECIFICITY: Expressed in rod-shaped photoreceptor cells in the
CC retina that mediate vision in dim light (at protein level).
CC {ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:28655769,
CC ECO:0000269|PubMed:3350146, ECO:0000269|PubMed:9541408}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000269|PubMed:1396673,
CC ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal. After hydrolysis of the Schiff base and release of the
CC covalently bound all-trans-retinal, active rhodopsin is regenerated by
CC binding of a fresh molecule of 11-cis-retinal.
CC {ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302,
CC ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163,
CC ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621,
CC ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857,
CC ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:21389983,
CC ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
CC ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:6870827,
CC ECO:0000305|PubMed:6759163}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; K00506; AAA30674.1; -; Genomic_DNA.
DR EMBL; K00502; AAA30674.1; JOINED; Genomic_DNA.
DR EMBL; K00503; AAA30674.1; JOINED; Genomic_DNA.
DR EMBL; K00504; AAA30674.1; JOINED; Genomic_DNA.
DR EMBL; K00505; AAA30674.1; JOINED; Genomic_DNA.
DR EMBL; M21606; AAA30675.1; -; mRNA.
DR PIR; A90840; OOBO.
DR RefSeq; NP_001014890.1; NM_001014890.2.
DR PDB; 1EDS; NMR; -; A=93-123.
DR PDB; 1EDV; NMR; -; A=172-205.
DR PDB; 1EDW; NMR; -; A=268-293.
DR PDB; 1EDX; NMR; -; A=1-40.
DR PDB; 1F88; X-ray; 2.80 A; A/B=1-348.
DR PDB; 1FDF; NMR; -; A=291-315.
DR PDB; 1GZM; X-ray; 2.65 A; A/B=1-348.
DR PDB; 1HZX; X-ray; 2.80 A; A/B=1-348.
DR PDB; 1JFP; NMR; -; A=1-348.
DR PDB; 1L9H; X-ray; 2.60 A; A/B=1-348.
DR PDB; 1LN6; NMR; -; A=1-348.
DR PDB; 1NZS; NMR; -; A=330-348.
DR PDB; 1U19; X-ray; 2.20 A; A/B=1-348.
DR PDB; 1VQX; NMR; -; A=330-348.
DR PDB; 2G87; X-ray; 2.60 A; A/B=1-348.
DR PDB; 2HPY; X-ray; 2.80 A; A/B=1-348.
DR PDB; 2I35; X-ray; 3.80 A; A=1-348.
DR PDB; 2I36; X-ray; 4.10 A; A/B/C=1-348.
DR PDB; 2I37; X-ray; 4.15 A; A/B/C=1-348.
DR PDB; 2J4Y; X-ray; 3.40 A; A/B=1-348.
DR PDB; 2PED; X-ray; 2.95 A; A/B=1-348.
DR PDB; 2X72; X-ray; 3.00 A; A=1-348.
DR PDB; 3C9L; X-ray; 2.65 A; A=1-348.
DR PDB; 3C9M; X-ray; 3.40 A; A=1-348.
DR PDB; 3CAP; X-ray; 2.90 A; A/B=1-348.
DR PDB; 3DQB; X-ray; 3.20 A; A=1-348.
DR PDB; 3OAX; X-ray; 2.60 A; A/B=1-348.
DR PDB; 3PQR; X-ray; 2.85 A; A=1-348.
DR PDB; 3PXO; X-ray; 3.00 A; A=1-348.
DR PDB; 4A4M; X-ray; 3.30 A; A=1-348.
DR PDB; 4BEY; X-ray; 2.90 A; A=1-348.
DR PDB; 4BEZ; X-ray; 3.30 A; A=1-348.
DR PDB; 4J4Q; X-ray; 2.65 A; A=1-348.
DR PDB; 4PXF; X-ray; 2.75 A; A=1-348.
DR PDB; 4X1H; X-ray; 2.29 A; A=1-348.
DR PDB; 5DYS; X-ray; 2.30 A; A=1-348.
DR PDB; 5EN0; X-ray; 2.81 A; A=1-348.
DR PDB; 5TE3; X-ray; 2.70 A; A=1-348.
DR PDB; 5TE5; X-ray; 4.01 A; A=1-348.
DR PDB; 5WKT; X-ray; 3.20 A; A=1-348.
DR PDB; 6FK6; X-ray; 2.36 A; A=1-326.
DR PDB; 6FK7; X-ray; 2.62 A; A=1-348.
DR PDB; 6FK8; X-ray; 2.87 A; A=1-348.
DR PDB; 6FK9; X-ray; 2.63 A; A=1-348.
DR PDB; 6FKA; X-ray; 2.70 A; A=1-348.
DR PDB; 6FKB; X-ray; 3.03 A; A=1-328.
DR PDB; 6FKC; X-ray; 2.46 A; A=1-348.
DR PDB; 6FKD; X-ray; 2.49 A; A=1-348.
DR PDB; 6FUF; X-ray; 3.12 A; A=2-317.
DR PDB; 6NWE; X-ray; 2.71 A; A=1-348.
DR PDB; 6OFJ; EM; 4.50 A; A/B=1-348.
DR PDB; 6OY9; EM; 3.90 A; R=1-348.
DR PDB; 6OYA; EM; 3.30 A; R=1-348.
DR PDB; 6PEL; X-ray; 3.19 A; A=1-348.
DR PDB; 6PGS; X-ray; 2.90 A; A=1-348.
DR PDB; 6PH7; X-ray; 2.90 A; A=1-348.
DR PDB; 6QNO; EM; 4.38 A; R=1-348.
DR PDB; 7MT8; EM; 5.80 A; R=1-348.
DR PDB; 7MT9; EM; 7.00 A; R=1-348.
DR PDB; 7MTA; EM; 4.10 A; R=1-348.
DR PDB; 7MTB; EM; 4.00 A; R=1-348.
DR PDBsum; 1EDS; -.
DR PDBsum; 1EDV; -.
DR PDBsum; 1EDW; -.
DR PDBsum; 1EDX; -.
DR PDBsum; 1F88; -.
DR PDBsum; 1FDF; -.
DR PDBsum; 1GZM; -.
DR PDBsum; 1HZX; -.
DR PDBsum; 1JFP; -.
DR PDBsum; 1L9H; -.
DR PDBsum; 1LN6; -.
DR PDBsum; 1NZS; -.
DR PDBsum; 1U19; -.
DR PDBsum; 1VQX; -.
DR PDBsum; 2G87; -.
DR PDBsum; 2HPY; -.
DR PDBsum; 2I35; -.
DR PDBsum; 2I36; -.
DR PDBsum; 2I37; -.
DR PDBsum; 2J4Y; -.
DR PDBsum; 2PED; -.
DR PDBsum; 2X72; -.
DR PDBsum; 3C9L; -.
DR PDBsum; 3C9M; -.
DR PDBsum; 3CAP; -.
DR PDBsum; 3DQB; -.
DR PDBsum; 3OAX; -.
DR PDBsum; 3PQR; -.
DR PDBsum; 3PXO; -.
DR PDBsum; 4A4M; -.
DR PDBsum; 4BEY; -.
DR PDBsum; 4BEZ; -.
DR PDBsum; 4J4Q; -.
DR PDBsum; 4PXF; -.
DR PDBsum; 4X1H; -.
DR PDBsum; 5DYS; -.
DR PDBsum; 5EN0; -.
DR PDBsum; 5TE3; -.
DR PDBsum; 5TE5; -.
DR PDBsum; 5WKT; -.
DR PDBsum; 6FK6; -.
DR PDBsum; 6FK7; -.
DR PDBsum; 6FK8; -.
DR PDBsum; 6FK9; -.
DR PDBsum; 6FKA; -.
DR PDBsum; 6FKB; -.
DR PDBsum; 6FKC; -.
DR PDBsum; 6FKD; -.
DR PDBsum; 6FUF; -.
DR PDBsum; 6NWE; -.
DR PDBsum; 6OFJ; -.
DR PDBsum; 6OY9; -.
DR PDBsum; 6OYA; -.
DR PDBsum; 6PEL; -.
DR PDBsum; 6PGS; -.
DR PDBsum; 6PH7; -.
DR PDBsum; 6QNO; -.
DR PDBsum; 7MT8; -.
DR PDBsum; 7MT9; -.
DR PDBsum; 7MTA; -.
DR PDBsum; 7MTB; -.
DR AlphaFoldDB; P02699; -.
DR BMRB; P02699; -.
DR SMR; P02699; -.
DR BioGRID; 166570; 2.
DR DIP; DIP-29225N; -.
DR ELM; P02699; -.
DR IntAct; P02699; 5.
DR MINT; P02699; -.
DR STRING; 9913.ENSBTAP00000001730; -.
DR BindingDB; P02699; -.
DR ChEMBL; CHEMBL5739; -.
DR TCDB; 9.A.14.1.17; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 523; 4 N-Linked glycans.
DR iPTMnet; P02699; -.
DR SwissPalm; P02699; -.
DR PaxDb; P02699; -.
DR ABCD; P02699; 1 sequenced antibody.
DR Ensembl; ENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
DR GeneID; 509933; -.
DR KEGG; bta:509933; -.
DR CTD; 6010; -.
DR VEuPathDB; HostDB:ENSBTAG00000001310; -.
DR VGNC; VGNC:33942; RHO.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P02699; -.
DR OMA; QYYLVNP; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Reactome; R-BTA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-BTA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-419771; Opsins.
DR Reactome; R-BTA-5620916; VxPx cargo-targeting to cilium.
DR EvolutionaryTrace; P02699; -.
DR PRO; PR:P02699; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000001310; Expressed in retina and 12 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0097648; C:G protein-coupled receptor complex; IDA:CAFA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:AgBase.
DR GO; GO:0019867; C:outer membrane; IDA:CAFA.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0005502; F:11-cis retinal binding; IDA:UniProtKB.
DR GO; GO:1990763; F:arrestin family protein binding; IPI:CAFA.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:CAFA.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002046; F:opsin binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0016038; P:absorption of visible light; IDA:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; IDA:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IDA:CAFA.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR DisProt; DP00271; -.
DR IDEAL; IID50247; -.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Chromophore;
KW Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197653"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT TOPO_DOM 309..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607,
FT ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322,
FT ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239"
FT REGION 330..348
FT /note="Interaction with SAG"
FT /evidence="ECO:0000269|PubMed:15111114"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000305|PubMed:21389983,
FT ECO:0000305|PubMed:22198838, ECO:0000305|PubMed:26526852,
FT ECO:0000305|PubMed:27458239"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0007744|PDB:1F88,
FT ECO:0007744|PDB:1HZX"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0007744|PDB:1F88,
FT ECO:0007744|PDB:1HZX"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000269|PubMed:21389983,
FT ECO:0000305|PubMed:22198838, ECO:0000305|PubMed:23579341,
FT ECO:0000305|PubMed:27458239"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000305|PubMed:6759163"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000269|PubMed:10926528,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17449675,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210,
FT ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:6870827,
FT ECO:0000305|PubMed:6759163, ECO:0007744|PDB:1F88,
FT ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX,
FT ECO:0007744|PDB:1JFP, ECO:0007744|PDB:2HPY,
FT ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3OAX,
FT ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO,
FT ECO:0007744|PDB:5DYS"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15111114,
FT ECO:0000269|PubMed:15351781"
FT MOD_RES 343
FT /note="Phosphoserine; by RK and GRK7"
FT /evidence="ECO:0000269|PubMed:1396673,
FT ECO:0000269|PubMed:15111114, ECO:0000269|PubMed:15351781"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:11425302,
FT ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:1512231,
FT ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:16908857,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:3350146,
FT ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H,
FT ECO:0007744|PDB:2HPY, ECO:0007744|PDB:4X1H,
FT ECO:0007744|PDB:5DYS"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:11425302,
FT ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:1512231,
FT ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:16908857,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:3350146,
FT ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H,
FT ECO:0007744|PDB:2HPY, ECO:0007744|PDB:4BEY,
FT ECO:0007744|PDB:4PXF, ECO:0007744|PDB:4X1H,
FT ECO:0007744|PDB:5DYS"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11425302,
FT ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621,
FT ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650,
FT ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:468821,
FT ECO:0000269|PubMed:6759163, ECO:0007744|PDB:1F88,
FT ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX,
FT ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87,
FT ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35,
FT ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37,
FT ECO:0007744|PDB:2PED, ECO:0007744|PDB:3C9L,
FT ECO:0007744|PDB:3CAP, ECO:0007744|PDB:3DQB,
FT ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR,
FT ECO:0007744|PDB:3PXO, ECO:0007744|PDB:4X1H"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11425302,
FT ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16908857,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341,
FT ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852,
FT ECO:0000269|PubMed:468821, ECO:0000269|PubMed:6759163,
FT ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM,
FT ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1L9H,
FT ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87,
FT ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35,
FT ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37,
FT ECO:0007744|PDB:2J4Y, ECO:0007744|PDB:2PED,
FT ECO:0007744|PDB:2X72, ECO:0007744|PDB:3C9L,
FT ECO:0007744|PDB:3C9M, ECO:0007744|PDB:3CAP,
FT ECO:0007744|PDB:3DQB, ECO:0007744|PDB:3OAX,
FT ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO,
FT ECO:0007744|PDB:4A4M, ECO:0007744|PDB:4BEY,
FT ECO:0007744|PDB:4BEZ, ECO:0007744|PDB:4J4Q,
FT ECO:0007744|PDB:4PXF, ECO:0007744|PDB:4X1H,
FT ECO:0007744|PDB:5DYS, ECO:0007744|PDB:5EN0,
FT ECO:0007744|PDB:5TE3"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040,
FT ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956,
FT ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16908857,
FT ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983,
FT ECO:0000269|PubMed:2145276, ECO:0000269|PubMed:22198838,
FT ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:26526852,
FT ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM,
FT ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1JFP,
FT ECO:0007744|PDB:1L9H, ECO:0007744|PDB:1LN6,
FT ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87,
FT ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35,
FT ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37,
FT ECO:0007744|PDB:2J4Y, ECO:0007744|PDB:2PED,
FT ECO:0007744|PDB:2X72, ECO:0007744|PDB:3C9L,
FT ECO:0007744|PDB:3C9M, ECO:0007744|PDB:3CAP,
FT ECO:0007744|PDB:3DQB, ECO:0007744|PDB:3OAX,
FT ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO,
FT ECO:0007744|PDB:4A4M, ECO:0007744|PDB:4BEY,
FT ECO:0007744|PDB:4BEZ, ECO:0007744|PDB:4J4Q,
FT ECO:0007744|PDB:4PXF, ECO:0007744|PDB:4X1H,
FT ECO:0007744|PDB:5DYS, ECO:0007744|PDB:5EN0,
FT ECO:0007744|PDB:5TE3, ECO:0007744|PDB:5TE5"
FT MUTAGEN 2
FT /note="N->C: Stabilized by a disulfide bond and normal
FT light absorption; when associated with C-282 and D-15."
FT /evidence="ECO:0000269|PubMed:17825322"
FT MUTAGEN 15
FT /note="N->D: Normal light absorption; when associated with
FT C-2 and C-282."
FT /evidence="ECO:0000269|PubMed:17825322"
FT MUTAGEN 90
FT /note="G->D: Increased thermal stability and decreased
FT retinal uptake. Decreases stability of the inactive
FT conformation."
FT /evidence="ECO:0000269|PubMed:23579341"
FT MUTAGEN 94
FT /note="T->I: Stabilizes the activated conformation and
FT hinders hydrolysis of the covalent bond that retains all-
FT trans-retinol."
FT /evidence="ECO:0000269|PubMed:27458239"
FT MUTAGEN 113
FT /note="E->Q: Causes shift to the activated conformation."
FT /evidence="ECO:0000269|PubMed:21389983"
FT MUTAGEN 257
FT /note="M->Y: Causes shift to the activated conformation."
FT /evidence="ECO:0000269|PubMed:22198838"
FT MUTAGEN 282
FT /note="D->C: Stabilized by a disulfide bond and normal
FT light absorption; when associated with C-2 and D-15."
FT /evidence="ECO:0000269|PubMed:17825322"
FT CONFLICT 281
FT /note="S -> F (in Ref. 3; AAA30675)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1U19"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4PXF"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 34..64
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4X1H"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1EDS"
FT HELIX 106..139
FT /evidence="ECO:0007829|PDB:1U19"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 150..168
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1EDV"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:1U19"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1EDV"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3C9M"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:3C9L"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 242..277
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:1U19"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:1U19"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4X1H"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1U19"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1NZS"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1JFP"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1U19"
SQ 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
