OPSD_HUMAN
ID OPSD_HUMAN Reviewed; 348 AA.
AC P08100; Q16414; Q2M249;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Rhodopsin;
DE AltName: Full=Opsin-2;
GN Name=RHO; Synonyms=OPN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6589631; DOI=10.1073/pnas.81.15.4851;
RA Nathans J., Hogness D.S.;
RT "Isolation and nucleotide sequence of the gene encoding human rhodopsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide diskovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
RX PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5;
RA Bennett J., Beller B., Sun D., Kariko K.;
RT "Sequence analysis of the 5.34-kb 5' flanking region of the human
RT rhodopsin-encoding gene.";
RL Gene 167:317-320(1995).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25664179; DOI=10.1186/s13630-015-0013-1;
RA Chuang J.Z., Hsu Y.C., Sung C.H.;
RT "Ultrastructural visualization of trans-ciliary rhodopsin cargoes in
RT mammalian rods.";
RL Cilia 4:4-4(2015).
RN [7]
RP INTERACTION WITH GRK1 AND SAG, FUNCTION, AND MUTAGENESIS OF GLU-113 AND
RP MET-257.
RX PubMed=28524165; DOI=10.1038/cr.2017.72;
RA He Y., Gao X., Goswami D., Hou L., Pal K., Yin Y., Zhao G., Ernst O.P.,
RA Griffin P., Melcher K., Xu H.E.;
RT "Molecular assembly of rhodopsin with G protein-coupled receptor kinases.";
RL Cell Res. 27:728-747(2017).
RN [8] {ECO:0007744|PDB:4ZWJ}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN
RP COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, AND DISULFIDE
RP BONDS.
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 [9] {ECO:0007744|PDB:5W0P}
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION,
RP TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND
RP SER-338, DISULFIDE BOND, AND MUTAGENESIS OF 336-THR--THR-340;
RP 336-THR--SER-338 AND SER-343.
RX PubMed=28753425; DOI=10.1016/j.cell.2017.07.002;
RA Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y.,
RA Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N.,
RA Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V.,
RA Griffin P.R., Ernst O.P., Melcher K., Xu H.E.;
RT "Identification of Phosphorylation Codes for Arrestin Recruitment by G
RT Protein-Coupled Receptors.";
RL Cell 170:457-469(2017).
RN [10]
RP REVIEW ON RP4 VARIANTS.
RX PubMed=8401533; DOI=10.1002/humu.1380020403;
RA Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A., Bhattacharya S.;
RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL Hum. Mutat. 2:249-255(1993).
RN [11]
RP VARIANTS RP4.
RX PubMed=2239971;
RA Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G.,
RA Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., Watty A.,
RA Ludwig M., Schinzel A., Samanns C., Gal A., Bhattacharya S.S.,
RA Humphries P.;
RT "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin
RT proline-->histidine substitution (codon 23) in pedigrees from Europe.";
RL Am. J. Hum. Genet. 47:941-945(1990).
RN [12]
RP VARIANT RP4 HIS-23.
RX PubMed=2137202; DOI=10.1038/343364a0;
RA Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., Yandell D.W.,
RA Sandberg M.A., Berson E.L.;
RT "A point mutation of the rhodopsin gene in one form of retinitis
RT pigmentosa.";
RL Nature 343:364-366(1990).
RN [13]
RP VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347, AND FUNCTION.
RX PubMed=2215617; DOI=10.1056/nejm199011083231903;
RA Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E.,
RA Sandberg M.A., Berson E.L.;
RT "Mutations within the rhodopsin gene in patients with autosomal dominant
RT retinitis pigmentosa.";
RL N. Engl. J. Med. 323:1302-1307(1990).
RN [14]
RP VARIANT RP4 ILE-255 DEL.
RX PubMed=1985460;
RA Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C.,
RA Bhattacharya S.S.;
RT "A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant
RT retinitis pigmentosa.";
RL Am. J. Hum. Genet. 48:26-30(1991).
RN [15]
RP VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
RX PubMed=1897520;
RA Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.;
RT "Identification of novel rhodopsin mutations associated with retinitis
RT pigmentosa by GC-clamped denaturing gradient gel electrophoresis.";
RL Am. J. Hum. Genet. 49:699-706(1991).
RN [16]
RP VARIANT RP4 ARG-347.
RX PubMed=1840561; DOI=10.1016/0888-7543(91)90159-c;
RA Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E.,
RA Schinzel A.;
RT "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis
RT pigmentosa.";
RL Genomics 11:468-470(1991).
RN [17]
RP VARIANTS RP4.
RX PubMed=1862076; DOI=10.1073/pnas.88.15.6481;
RA Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., Jacobson S.G.,
RA Heckenlively J.R., Nowakowski R., Fishman G., Gouras P., Nathans J.;
RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991).
RN [18]
RP VARIANTS RP4.
RX PubMed=1833777; DOI=10.1073/pnas.88.20.9370;
RA Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.;
RT "Mutation spectrum of the rhodopsin gene among patients with autosomal
RT dominant retinitis pigmentosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991).
RN [19]
RP VARIANT RP4 ARG-207.
RX PubMed=1302614; DOI=10.1093/hmg/1.9.769;
RA Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M.,
RA Sharpe E., Humphries P.;
RT "Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin
RT gene in the original 3q linked family.";
RL Hum. Mol. Genet. 1:769-771(1992).
RN [20]
RP VARIANTS RP4 MET-17 AND LEU-347.
RX PubMed=1391967; DOI=10.1007/bf01899733;
RA Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., Sakuma T.,
RA Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., Kanai A.;
RT "Point mutations of rhodopsin gene found in Japanese families with
RT autosomal dominant retinitis pigmentosa (ADRP).";
RL Jpn. J. Hum. Genet. 37:125-132(1992).
RN [21]
RP VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND VARIANTS
RP ALA-51; ILE-104 AND MET-209.
RX PubMed=8317502;
RA Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C.,
RA Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R.,
RA Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.;
RT "Identification of novel rhodopsin mutations responsible for retinitis
RT pigmentosa: implications for the structure and function of rhodopsin.";
RL Am. J. Hum. Genet. 53:80-89(1993).
RN [22]
RP VARIANT RP4 SER-15.
RX PubMed=8353500; DOI=10.1093/hmg/2.6.813;
RA Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P.,
RA Duvigneau C., Gal A.;
RT "Autosomal dominant 'sector' retinitis pigmentosa due to a point mutation
RT predicting an Asn-15-Ser substitution of rhodopsin.";
RL Hum. Mol. Genet. 2:813-814(1993).
RN [23]
RP VARIANT CSNBAD1 GLU-292.
RX PubMed=8358437; DOI=10.1038/ng0793-280;
RA Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.;
RT "Heterozygous missense mutation in the rhodopsin gene as a cause of
RT congenital stationary night blindness.";
RL Nat. Genet. 4:280-283(1993).
RN [24]
RP VARIANTS RP4.
RX PubMed=8088850; DOI=10.1006/geno.1994.1301;
RA Vaithinathan R., Berson E.L., Dryja T.P.;
RT "Further screening of the rhodopsin gene in patients with autosomal
RT dominant retinitis pigmentosa.";
RL Genomics 21:461-463(1994).
RN [25]
RP VARIANT RP4 THR-44.
RX PubMed=8076945; DOI=10.1007/bf00208284;
RA Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C.,
RA Carballo M.;
RT "Identification of a novel rhodopsin mutation (Met-44-Thr) in a simplex
RT case of retinitis pigmentosa.";
RL Hum. Genet. 94:283-286(1994).
RN [26]
RP VARIANTS RP4 PHE-110; PRO-131 AND VAL-164.
RX PubMed=7981701; DOI=10.1093/hmg/3.7.1203;
RA Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S.,
RA Humphries P., Gal A.;
RT "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with
RT autosomal dominant retinitis pigmentosa.";
RL Hum. Mol. Genet. 3:1203-1203(1994).
RN [27]
RP VARIANT RP4 GLN-171.
RX PubMed=7987326; DOI=10.1093/hmg/3.8.1421;
RA Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., Cabeza J.C.;
RT "Identification of a new mutation at codon 171 of rhodopsin gene causing
RT autosomal dominant retinitis pigmentosa.";
RL Hum. Mol. Genet. 3:1421-1421(1994).
RN [28]
RP VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
RX PubMed=7987331; DOI=10.1093/hmg/3.8.1433;
RA Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I.,
RA Philip N., Soubrane G., Coscas G., Munnich A.;
RT "Five novel missense mutations of the rhodopsin gene in autosomal dominant
RT retinitis pigmentosa.";
RL Hum. Mol. Genet. 3:1433-1434(1994).
RN [29]
RP VARIANTS RP4 ARG-40 AND LYS-216.
RX PubMed=8081400; DOI=10.1002/humu.1380030417;
RA Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., Bhattacharya S.;
RT "Two new rhodopsin transversion mutations (L40R; M216K) in families with
RT autosomal dominant retinitis pigmentosa.";
RL Hum. Mutat. 3:409-410(1994).
RN [30]
RP VARIANT RP4 LEU-345.
RX PubMed=8045708;
RA Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.;
RT "Autosomal dominant retinitis pigmentosa in a large family: a clinical and
RT molecular genetic study.";
RL Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994).
RN [31]
RP CHARACTERIZATION OF VARIANT CSNBAD1 ASP-90, AND FUNCTION.
RX PubMed=8107847; DOI=10.1038/367639a0;
RA Rao V.R., Cohen G.B., Oprian D.D.;
RT "Rhodopsin mutation G90D and a molecular mechanism for congenital night
RT blindness.";
RL Nature 367:639-642(1994).
RN [32]
RP VARIANT ARRP LYS-150.
RX PubMed=7987385; DOI=10.1038/ng0994-10;
RA Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R., Orth U.,
RA Oehlmann R., Gal A.;
RT "Missense rhodopsin mutation in a family with recessive RP.";
RL Nat. Genet. 8:10-11(1994).
RN [33]
RP VARIANT RP4 ALA-347.
RX PubMed=7633434; DOI=10.1093/hmg/4.4.775;
RA Macke J.P., Hennessey J.C., Nathans J.;
RT "Rhodopsin mutation proline347-to-alanine in a family with autosomal
RT dominant retinitis pigmentosa indicates an important role for proline at
RT position 347.";
RL Hum. Mol. Genet. 4:775-776(1995).
RN [34]
RP VARIANT CSNBAD1 ASP-90, AND FUNCTION.
RX PubMed=7846071; DOI=10.1073/pnas.92.3.880;
RA Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K.,
RA Alpern M.;
RT "Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp
RT mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995).
RN [35]
RP VARIANT RP4 TRP-135.
RX PubMed=8554077; DOI=10.1016/s0002-9394(14)70530-6;
RA Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., Munnich A.,
RA Kaplan J.;
RT "Retinitis punctata albescens associated with the Arg135Trp mutation in the
RT rhodopsin gene.";
RL Am. J. Ophthalmol. 121:19-25(1996).
RN [36]
RP VARIANT RP4 ARG-109.
RX PubMed=9452035; DOI=10.1002/humu.1380110114;
RA Goliath R., Bardien S., September A., Martin R., Ramesar R., Greenberg J.;
RT "Rhodopsin mutation G109R in a family with autosomal dominant retinitis
RT pigmentosa.";
RL Hum. Mutat. Suppl. 1:S40-S41(1998).
RN [37]
RP VARIANT CSNBAD1 ILE-94.
RX PubMed=9888392;
RX DOI=10.1002/(sici)1098-1004(1999)13:1<75::aid-humu9>3.0.co;2-4;
RA Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N.,
RA Findlay J.B.C., Humphries P., Kenna P.F.;
RT "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal
RT dominant congenital stationary night blindness.";
RL Hum. Mutat. 13:75-81(1999).
RN [38]
RP CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12566452; DOI=10.1074/jbc.m300087200;
RA Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K.,
RA Kaushal S.;
RT "Pharmacological chaperone-mediated in vivo folding and stabilization of
RT the P23H-opsin mutant associated with autosomal dominant retinitis
RT pigmentosa.";
RL J. Biol. Chem. 278:14442-14450(2003).
RN [39]
RP CHARACTERIZATION OF VARIANT RP4 HIS-23, AND SUBCELLULAR LOCATION.
RX PubMed=19934218; DOI=10.1242/jcs.055228;
RA Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.;
RT "A dual role for EDEM1 in the processing of rod opsin.";
RL J. Cell Sci. 122:4465-4472(2009).
RN [40]
RP VARIANT RP4 LYS-150.
RX PubMed=19960070;
RA Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., Sadeque A.,
RA Bokhari H., Collin R.W., Orth U., van Genderen M.M., den Hollander A.I.,
RA Cremers F.P., Qamar R.;
RT "A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani
RT families with autosomal recessive retinitis pigmentosa.";
RL Mol. Vis. 15:2526-2534(2009).
RN [41]
RP VARIANTS RP4 TRP-135; SER-180 AND ASN-214.
RX PubMed=22334370; DOI=10.1002/humu.22045;
RA Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
RA Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
RA Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E.,
RA den Hollander A.I., Hoischen A., Hoyng C., Klevering B.J.,
RA van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.;
RT "Next-generation genetic testing for retinitis pigmentosa.";
RL Hum. Mutat. 33:963-972(2012).
RN [42]
RP VARIANT ILE-104.
RX PubMed=28837730; DOI=10.1167/iovs.16-20941;
RA Wang B., Liu Y., Chen S., Wu Y., Lin S., Duan Y., Zheng K., Zhang L.,
RA Gu X., Hong W., Shao H., Zeng X., Sun B., Duan S.;
RT "A novel potentially causative variant of NDUFAF7 revealed by mutation
RT screening in a chinese family with pathologic myopia.";
RL Invest. Ophthalmol. Vis. Sci. 58:4182-4192(2017).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity (PubMed:8107847, PubMed:7846071). Required for photoreceptor
CC cell viability after birth (PubMed:2215617, PubMed:12566452). Light-
CC induced isomerization of the chromophore 11-cis-retinal to all-trans-
CC retinal triggers a conformational change that activates signaling via
CC G-proteins (PubMed:8107847, PubMed:28524165, PubMed:26200343,
CC PubMed:28753425). Subsequent receptor phosphorylation mediates
CC displacement of the bound G-protein alpha subunit by the arrestin SAG
CC and terminates signaling (PubMed:28524165, PubMed:26200343).
CC {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:2215617,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425,
CC ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847,
CC ECO:0000305|PubMed:28524165}.
CC -!- SUBUNIT: Homodimer (By similarity). May form a complex composed of RHO,
CC GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the
CC interaction between GRK1 and RHO (By similarity). Interacts with GRK1
CC (PubMed:28524165). Interacts (phosphorylated form) with SAG
CC (PubMed:28524165, PubMed:26200343, PubMed:28753425). Interacts with
CC GNAT1 (PubMed:26200343). Interacts with GNAT3. SAG and G-proteins
CC compete for a common binding site (PubMed:26200343). Interacts with
CC PRCD; the interaction promotes PRCD stability (By similarity).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P15409,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28524165,
CC ECO:0000269|PubMed:28753425}.
CC -!- INTERACTION:
CC P08100; P11912: CD79A; NbExp=3; IntAct=EBI-1394177, EBI-7797864;
CC P08100; O95405: ZFYVE9; NbExp=2; IntAct=EBI-1394177, EBI-296817;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12566452,
CC ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25664179,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19934218,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:25664179}. Note=Synthesized in the inner segment
CC (IS) of rod photoreceptor cells before vectorial transport to disk
CC membranes in the rod outer segment (OS) photosensory cilia.
CC {ECO:0000269|PubMed:25664179}.
CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediate vision
CC in dim light.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region (By similarity). After activation by
CC light, phosphorylated by GRK1 (in vitro) (PubMed:28524165).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:28524165}.
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(PubMed:12566452).
CC {ECO:0000269|PubMed:12566452}.
CC -!- DISEASE: Retinitis pigmentosa 4 (RP4) [MIM:613731]: A retinal dystrophy
CC belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:12566452,
CC ECO:0000269|PubMed:1302614, ECO:0000269|PubMed:1391967,
CC ECO:0000269|PubMed:1833777, ECO:0000269|PubMed:1840561,
CC ECO:0000269|PubMed:1862076, ECO:0000269|PubMed:1897520,
CC ECO:0000269|PubMed:1985460, ECO:0000269|PubMed:19934218,
CC ECO:0000269|PubMed:19960070, ECO:0000269|PubMed:2137202,
CC ECO:0000269|PubMed:2215617, ECO:0000269|PubMed:22334370,
CC ECO:0000269|PubMed:2239971, ECO:0000269|PubMed:7633434,
CC ECO:0000269|PubMed:7981701, ECO:0000269|PubMed:7987326,
CC ECO:0000269|PubMed:7987331, ECO:0000269|PubMed:8045708,
CC ECO:0000269|PubMed:8076945, ECO:0000269|PubMed:8081400,
CC ECO:0000269|PubMed:8088850, ECO:0000269|PubMed:8317502,
CC ECO:0000269|PubMed:8353500, ECO:0000269|PubMed:8554077,
CC ECO:0000269|PubMed:9452035}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Night blindness, congenital stationary, autosomal dominant 1
CC (CSNBAD1) [MIM:610445]: A non-progressive retinal disorder
CC characterized by impaired night vision, often associated with nystagmus
CC and myopia. {ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847,
CC ECO:0000269|PubMed:8358437, ECO:0000269|PubMed:9888392}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Mutations of the RHO gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/rhomut.htm";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Rhodopsin entry;
CC URL="https://en.wikipedia.org/wiki/Rhodopsin";
CC ---------------------------------------------------------------------------
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DR EMBL; U49742; AAC31763.1; -; Genomic_DNA.
DR EMBL; AB065668; BAC05894.1; -; Genomic_DNA.
DR EMBL; BX537381; CAD97623.1; -; mRNA.
DR EMBL; BC112104; AAI12105.1; -; mRNA.
DR EMBL; BC112106; AAI12107.1; -; mRNA.
DR EMBL; U16824; AAA97436.1; -; Genomic_DNA.
DR EMBL; S81166; AAB35906.1; -; Genomic_DNA.
DR CCDS; CCDS3063.1; -.
DR PIR; A41200; OOHU.
DR RefSeq; NP_000530.1; NM_000539.3.
DR PDB; 4ZWJ; X-ray; 3.30 A; A/B/C/D=1-348.
DR PDB; 5DGY; X-ray; 7.70 A; A/B/C/D=1-348.
DR PDB; 5W0P; X-ray; 3.01 A; A/B/C/D=1-348.
DR PDB; 6CMO; EM; 4.50 A; R=3-323.
DR PDBsum; 4ZWJ; -.
DR PDBsum; 5DGY; -.
DR PDBsum; 5W0P; -.
DR PDBsum; 6CMO; -.
DR AlphaFoldDB; P08100; -.
DR SMR; P08100; -.
DR BioGRID; 111942; 12.
DR IntAct; P08100; 4.
DR STRING; 9606.ENSP00000296271; -.
DR ChEMBL; CHEMBL4296308; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB01728; 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB02451; B-nonylglucoside.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB01159; Halothane.
DR DrugBank; DB04079; Heptane-1,2,3-Triol.
DR DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DR DrugBank; DB03381; Hexadecanal.
DR DrugBank; DB01646; N-Acetylmethionine.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB02482; Phosphonothreonine.
DR TCDB; 9.A.14.1.2; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 525; 12 N-Linked glycans.
DR GlyGen; P08100; 3 sites, 23 N-linked glycans (1 site).
DR iPTMnet; P08100; -.
DR PhosphoSitePlus; P08100; -.
DR SwissPalm; P08100; -.
DR BioMuta; RHO; -.
DR DMDM; 129207; -.
DR MassIVE; P08100; -.
DR PaxDb; P08100; -.
DR PeptideAtlas; P08100; -.
DR PRIDE; P08100; -.
DR ProteomicsDB; 52066; -.
DR Antibodypedia; 17456; 527 antibodies from 38 providers.
DR DNASU; 6010; -.
DR Ensembl; ENST00000296271.4; ENSP00000296271.3; ENSG00000163914.5.
DR GeneID; 6010; -.
DR KEGG; hsa:6010; -.
DR MANE-Select; ENST00000296271.4; ENSP00000296271.3; NM_000539.3; NP_000530.1.
DR UCSC; uc003emt.4; human.
DR CTD; 6010; -.
DR DisGeNET; 6010; -.
DR GeneCards; RHO; -.
DR GeneReviews; RHO; -.
DR HGNC; HGNC:10012; RHO.
DR HPA; ENSG00000163914; Tissue enriched (retina).
DR MalaCards; RHO; -.
DR MIM; 180380; gene.
DR MIM; 610445; phenotype.
DR MIM; 613731; phenotype.
DR neXtProt; NX_P08100; -.
DR OpenTargets; ENSG00000163914; -.
DR Orphanet; 215; Congenital stationary night blindness.
DR Orphanet; 791; Retinitis pigmentosa.
DR Orphanet; 52427; Retinitis punctata albescens.
DR PharmGKB; PA34390; -.
DR VEuPathDB; HostDB:ENSG00000163914; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P08100; -.
DR OMA; VICGFTT; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P08100; -.
DR TreeFam; TF324998; -.
DR PathwayCommons; P08100; -.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-419771; Opsins.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; P08100; -.
DR SIGNOR; P08100; -.
DR BioGRID-ORCS; 6010; 7 hits in 1061 CRISPR screens.
DR ChiTaRS; RHO; human.
DR GeneWiki; Rhodopsin; -.
DR GenomeRNAi; 6010; -.
DR Pharos; P08100; Tbio.
DR PRO; PR:P08100; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P08100; protein.
DR Bgee; ENSG00000163914; Expressed in optic choroid and 32 other tissues.
DR Genevisible; P08100; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA: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; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
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; IMP:UniProtKB.
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; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Congenital stationary night blindness; Disease variant; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Retinitis pigmentosa;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197677"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 275..284
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT TOPO_DOM 310..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT REGION 330..348
FT /note="Interaction with SAG"
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28753425"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000305|PubMed:26200343"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000269|PubMed:26200343"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28753425"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28753425"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28753425"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28753425"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"
FT VARIANT 4
FT /note="T -> K (in RP4)"
FT /id="VAR_004765"
FT VARIANT 15
FT /note="N -> S (in RP4; dbSNP:rs104893786)"
FT /evidence="ECO:0000269|PubMed:8353500"
FT /id="VAR_004766"
FT VARIANT 17
FT /note="T -> M (in RP4; dbSNP:rs104893769)"
FT /evidence="ECO:0000269|PubMed:1391967,
FT ECO:0000269|PubMed:1897520"
FT /id="VAR_004767"
FT VARIANT 23
FT /note="P -> H (in RP4; most common variant; impairs protein
FT folding; leads to interaction with EDEM1 followed by
FT degradation by the ERAD system; dbSNP:rs104893768)"
FT /evidence="ECO:0000269|PubMed:12566452,
FT ECO:0000269|PubMed:1897520, ECO:0000269|PubMed:19934218,
FT ECO:0000269|PubMed:2137202, ECO:0000269|PubMed:2215617"
FT /id="VAR_004768"
FT VARIANT 23
FT /note="P -> L (in RP4)"
FT /id="VAR_004769"
FT VARIANT 28
FT /note="Q -> H (in RP4)"
FT /id="VAR_004770"
FT VARIANT 40
FT /note="L -> R (in RP4)"
FT /evidence="ECO:0000269|PubMed:8081400"
FT /id="VAR_004771"
FT VARIANT 44
FT /note="M -> T (in RP4; dbSNP:rs774336493)"
FT /evidence="ECO:0000269|PubMed:8076945"
FT /id="VAR_004772"
FT VARIANT 45
FT /note="F -> L (in RP4; dbSNP:rs104893770)"
FT /id="VAR_004773"
FT VARIANT 46
FT /note="L -> R (in RP4)"
FT /id="VAR_004774"
FT VARIANT 51
FT /note="G -> A (in dbSNP:rs149079952)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004775"
FT VARIANT 51
FT /note="G -> R (in RP4; dbSNP:rs104893792)"
FT /id="VAR_004776"
FT VARIANT 51
FT /note="G -> V (in RP4)"
FT /id="VAR_004777"
FT VARIANT 53
FT /note="P -> R (in RP4; dbSNP:rs28933395)"
FT /id="VAR_004778"
FT VARIANT 58
FT /note="T -> R (in RP4; dbSNP:rs28933394)"
FT /evidence="ECO:0000269|PubMed:1897520,
FT ECO:0000269|PubMed:2215617"
FT /id="VAR_004779"
FT VARIANT 68..71
FT /note="Missing (in RP4)"
FT /id="VAR_004780"
FT VARIANT 87
FT /note="V -> D (in RP4; dbSNP:rs104893771)"
FT /id="VAR_004781"
FT VARIANT 89
FT /note="G -> D (in RP4; dbSNP:rs104893772)"
FT /id="VAR_004782"
FT VARIANT 90
FT /note="G -> D (in CSNBAD1; constitutive activity in the
FT absence of bound retinal; dbSNP:rs104893790)"
FT /evidence="ECO:0000269|PubMed:7846071,
FT ECO:0000269|PubMed:8107847"
FT /id="VAR_004783"
FT VARIANT 94
FT /note="T -> I (in CSNBAD1; dbSNP:rs104893796)"
FT /evidence="ECO:0000269|PubMed:9888392"
FT /id="VAR_004784"
FT VARIANT 104
FT /note="V -> I (found in patients with pathologic myopia;
FT unknown pathological significance; dbSNP:rs144317206)"
FT /evidence="ECO:0000269|PubMed:28837730,
FT ECO:0000269|PubMed:8317502"
FT /id="VAR_004785"
FT VARIANT 106
FT /note="G -> R (in RP4; dbSNP:rs104893773)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004786"
FT VARIANT 106
FT /note="G -> W (in RP4; dbSNP:rs104893773)"
FT /id="VAR_004787"
FT VARIANT 109
FT /note="G -> R (in RP4; dbSNP:rs1415160298)"
FT /evidence="ECO:0000269|PubMed:9452035"
FT /id="VAR_004788"
FT VARIANT 110
FT /note="C -> F (in RP4)"
FT /evidence="ECO:0000269|PubMed:7981701"
FT /id="VAR_004789"
FT VARIANT 110
FT /note="C -> Y (in RP4; dbSNP:rs104893787)"
FT /id="VAR_004790"
FT VARIANT 114
FT /note="G -> D (in RP4; dbSNP:rs104893788)"
FT /id="VAR_004791"
FT VARIANT 125
FT /note="L -> R (in RP4)"
FT /id="VAR_004792"
FT VARIANT 127
FT /note="S -> F (in RP4)"
FT /evidence="ECO:0000269|PubMed:7987331"
FT /id="VAR_004793"
FT VARIANT 131
FT /note="L -> P (in RP4; dbSNP:rs1553781140)"
FT /evidence="ECO:0000269|PubMed:7981701,
FT ECO:0000269|PubMed:7987331"
FT /id="VAR_004794"
FT VARIANT 135
FT /note="R -> G (in RP4)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004795"
FT VARIANT 135
FT /note="R -> L (in RP4; dbSNP:rs104893774)"
FT /id="VAR_004796"
FT VARIANT 135
FT /note="R -> W (in RP4; dbSNP:rs104893775)"
FT /evidence="ECO:0000269|PubMed:22334370,
FT ECO:0000269|PubMed:8554077"
FT /id="VAR_004797"
FT VARIANT 140
FT /note="C -> S (in RP4)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004798"
FT VARIANT 150
FT /note="E -> K (in RP4; autosomal recessive;
FT dbSNP:rs104893791)"
FT /evidence="ECO:0000269|PubMed:19960070,
FT ECO:0000269|PubMed:7987385"
FT /id="VAR_004799"
FT VARIANT 164
FT /note="A -> E (in RP4; dbSNP:rs104893793)"
FT /id="VAR_004800"
FT VARIANT 164
FT /note="A -> V (in RP4; dbSNP:rs104893793)"
FT /evidence="ECO:0000269|PubMed:7981701"
FT /id="VAR_004801"
FT VARIANT 167
FT /note="C -> R (in RP4)"
FT /id="VAR_004802"
FT VARIANT 171
FT /note="P -> L (in RP4)"
FT /id="VAR_004803"
FT VARIANT 171
FT /note="P -> Q (in RP4)"
FT /evidence="ECO:0000269|PubMed:7987326"
FT /id="VAR_004804"
FT VARIANT 171
FT /note="P -> S (in RP4; dbSNP:rs104893794)"
FT /id="VAR_004805"
FT VARIANT 178
FT /note="Y -> C (in RP4; dbSNP:rs104893776)"
FT /id="VAR_004806"
FT VARIANT 178
FT /note="Y -> N (in RP4)"
FT /evidence="ECO:0000269|PubMed:7987331"
FT /id="VAR_004807"
FT VARIANT 180
FT /note="P -> S (in RP4)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068359"
FT VARIANT 181
FT /note="E -> K (in RP4; dbSNP:rs775557680)"
FT /id="VAR_004808"
FT VARIANT 182
FT /note="G -> S (in RP4; dbSNP:rs104893780)"
FT /evidence="ECO:0000269|PubMed:1897520"
FT /id="VAR_004809"
FT VARIANT 186
FT /note="S -> P (in RP4)"
FT /id="VAR_004810"
FT VARIANT 188
FT /note="G -> E (in RP4; dbSNP:rs1424131846)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004811"
FT VARIANT 188
FT /note="G -> R (in RP4; dbSNP:rs527236100)"
FT /id="VAR_004812"
FT VARIANT 190
FT /note="D -> G (in RP4; dbSNP:rs104893777)"
FT /id="VAR_004814"
FT VARIANT 190
FT /note="D -> N (in RP4; dbSNP:rs104893779)"
FT /id="VAR_004813"
FT VARIANT 190
FT /note="D -> Y (in RP4; dbSNP:rs104893779)"
FT /id="VAR_004815"
FT VARIANT 207
FT /note="M -> R (in RP4; dbSNP:rs104893782)"
FT /evidence="ECO:0000269|PubMed:1302614"
FT /id="VAR_004816"
FT VARIANT 209
FT /note="V -> M (found in a patient with retinitis
FT pigmentosa; unknown pathological significance;
FT dbSNP:rs567288669)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004817"
FT VARIANT 211
FT /note="H -> P (in RP4; dbSNP:rs28933993)"
FT /id="VAR_004818"
FT VARIANT 211
FT /note="H -> R (in RP4)"
FT /evidence="ECO:0000269|PubMed:8317502"
FT /id="VAR_004819"
FT VARIANT 214
FT /note="I -> N (in RP4)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068360"
FT VARIANT 216
FT /note="M -> K (in RP4)"
FT /evidence="ECO:0000269|PubMed:8081400"
FT /id="VAR_004820"
FT VARIANT 220
FT /note="F -> C (in RP4; dbSNP:rs766161322)"
FT /id="VAR_004821"
FT VARIANT 222
FT /note="C -> R (in RP4)"
FT /id="VAR_004822"
FT VARIANT 255
FT /note="Missing (in RP4)"
FT /evidence="ECO:0000269|PubMed:1985460"
FT /id="VAR_004823"
FT VARIANT 264
FT /note="Missing (in RP4)"
FT /id="VAR_004824"
FT VARIANT 267
FT /note="P -> L (in RP4; dbSNP:rs104893781)"
FT /evidence="ECO:0000269|PubMed:1897520"
FT /id="VAR_004825"
FT VARIANT 267
FT /note="P -> R (in RP4)"
FT /evidence="ECO:0000269|PubMed:7987331"
FT /id="VAR_004826"
FT VARIANT 292
FT /note="A -> E (in CSNBAD1; dbSNP:rs104893789)"
FT /evidence="ECO:0000269|PubMed:8358437"
FT /id="VAR_004827"
FT VARIANT 296
FT /note="K -> E (in RP4; dbSNP:rs29001653)"
FT /id="VAR_004828"
FT VARIANT 297
FT /note="S -> R (in RP4; dbSNP:rs142285818)"
FT /evidence="ECO:0000269|PubMed:7987331"
FT /id="VAR_004829"
FT VARIANT 342
FT /note="T -> M (in RP4; dbSNP:rs183318466)"
FT /id="VAR_004830"
FT VARIANT 345
FT /note="V -> L (in RP4; dbSNP:rs104893795)"
FT /evidence="ECO:0000269|PubMed:8045708"
FT /id="VAR_004831"
FT VARIANT 345
FT /note="V -> M (in RP4; dbSNP:rs104893795)"
FT /id="VAR_004832"
FT VARIANT 347
FT /note="P -> A (in RP4)"
FT /evidence="ECO:0000269|PubMed:7633434"
FT /id="VAR_004833"
FT VARIANT 347
FT /note="P -> L (in RP4; common variant; dbSNP:rs29001566)"
FT /evidence="ECO:0000269|PubMed:1391967,
FT ECO:0000269|PubMed:2215617"
FT /id="VAR_004834"
FT VARIANT 347
FT /note="P -> Q (in RP4; dbSNP:rs29001566)"
FT /id="VAR_004835"
FT VARIANT 347
FT /note="P -> R (in RP4; dbSNP:rs29001566)"
FT /evidence="ECO:0000269|PubMed:1840561"
FT /id="VAR_004836"
FT VARIANT 347
FT /note="P -> S (in RP4; dbSNP:rs29001637)"
FT /evidence="ECO:0000269|PubMed:2215617"
FT /id="VAR_004837"
FT MUTAGEN 113
FT /note="E->Q: Induces a conformation change that promotes
FT interaction with GRK1 and SAG; when associated with Y-257."
FT /evidence="ECO:0000269|PubMed:26200343"
FT MUTAGEN 257
FT /note="M->Y: Induces a conformation change that promotes
FT interaction with GRK1 and SAG; when associated with Q-113."
FT /evidence="ECO:0000269|PubMed:26200343,
FT ECO:0000269|PubMed:28524165"
FT MUTAGEN 336..340
FT /note="TVSKT->AVAKA: Loss of phosphorylation sites and
FT decreased interaction with SAG."
FT /evidence="ECO:0000269|PubMed:28753425"
FT MUTAGEN 336..338
FT /note="TVS->AVA: Loss of phosphorylation sites and
FT decreased interaction with SAG; when associated with A-
FT 343."
FT /evidence="ECO:0000269|PubMed:28753425"
FT MUTAGEN 343
FT /note="S->A: Loss of phosphorylation sites and decreased
FT interaction with SAG; when associated with 336-A--A-338."
FT /evidence="ECO:0000269|PubMed:28753425"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4ZWJ"
FT HELIX 35..64
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 106..140
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 150..168
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4ZWJ"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 213..236
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 241..277
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 285..306
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4ZWJ"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5W0P"
SQ SEQUENCE 348 AA; 38893 MW; 6F4F6FCBA34265B2 CRC64;
MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
