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 24-JUL-2024, entry version 241. 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 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] RP VARIANTS RP4, AND VARIANTS RP4 LEU-23; LEU-45; VAL-51; ARG-188 AND MET-345. 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 [18] 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 [19] 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 [20] 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 [21] RP VARIANT RP4 CYS-220. RX PubMed=8406457; DOI=10.1006/geno.1993.1309; RA Bunge S., Wedemann H., David D., Terwilliger D.J., van den Born L.I., RA Aulehla-Scholz C., Samanns C., Horn M., Ott J., Schwinger E.; RT "Molecular analysis and genetic mapping of the rhodopsin gene in families RT with autosomal dominant retinitis pigmentosa."; RL Genomics 17:230-233(1993). RN [22] RP VARIANTS RP4 LYS-4; HIS-28; ARG-51; ARG-53; ASP-87; TRP-106; TYR-110; RP ARG-125; LEU-135; CYS-178; LYS-181; PRO-186; ASN-190; GLY-190 AND TYR-190. 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 [23] 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 [24] RP VARIANT RP4 ARG-46. RX PubMed=8364589; DOI=10.1002/humu.1380020309; RA Rodriguez J.A., Herrera C.A., Birch D.G., Daiger S.P.; RT "A leucine to arginine amino acid substitution at codon 46 of rhodopsin is RT responsible for a severe form of autosomal dominant retinitis pigmentosa."; RL Hum. Mutat. 2:205-213(1993). RN [25] 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 [26] RP VARIANTS RP4 ASP-114; GLU-164; ARG-167; LEU-171; SER-171; LEU-345 AND RP GLN-347. 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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:7846071, PubMed:8107847). Required for photoreceptor CC cell viability after birth (PubMed:12566452, PubMed:2215617). 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:26200343, PubMed:28524165, PubMed:28753425, CC PubMed:8107847). Subsequent receptor phosphorylation mediates CC displacement of the bound G-protein alpha subunit by the arrestin SAG CC and terminates signaling (PubMed:26200343, PubMed:28524165). 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:26200343, PubMed:28524165, 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). Forms a CC complex with ASAP1 and ARF4. Forms a complex with ASAP1, RAB11A, CC Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia CC rhodopsin/RHO transport in photoreceptors (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:8364589, CC ECO:0000269|PubMed:8401533, ECO:0000269|PubMed:8406457, CC ECO:0000269|PubMed:8554077, ECO:0000269|PubMed:9452035}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P08100; 2 sites, 23 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; 9606-ENSP00000296271; -. DR PeptideAtlas; P08100; -. DR ProteomicsDB; 52066; -. DR Antibodypedia; 17456; 568 antibodies from 39 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 AGR; HGNC:10012; -. 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; 5350930at2759; -. 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; 10 hits in 1139 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 33 other cell types or tissues. 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:0016020; C:membrane; ISS:UniProtKB. 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:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl. 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:0071800; P:podosome assembly; IEA:Ensembl. DR GO; GO:0009642; P:response to light intensity; IEA:Ensembl. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB. DR GO; GO:1904389; P:rod bipolar cell differentiation; IEA:Ensembl. DR GO; GO:0043052; P:thermotaxis; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd15080; 7tmA_MWS_opsin; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR050125; GPCR_opsins. 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 PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1. 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:1833777" FT /id="VAR_004769" FT VARIANT 28 FT /note="Q -> H (in RP4)" FT /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:1833777" FT /id="VAR_004773" FT VARIANT 46 FT /note="L -> R (in RP4; dbSNP:rs2084757073)" FT /evidence="ECO:0000269|PubMed:8364589" 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 /evidence="ECO:0000269|PubMed:8401533" FT /id="VAR_004776" FT VARIANT 51 FT /note="G -> V (in RP4)" FT /evidence="ECO:0000269|PubMed:1833777" FT /id="VAR_004777" FT VARIANT 53 FT /note="P -> R (in RP4; dbSNP:rs28933395)" FT /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8401533" FT /id="VAR_004781" FT VARIANT 89 FT /note="G -> D (in RP4; dbSNP:rs104893772)" FT /evidence="ECO:0000269|PubMed:8401533" 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 uncertain 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 /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8401533" FT /id="VAR_004790" FT VARIANT 114 FT /note="G -> D (in RP4; dbSNP:rs104893788)" FT /evidence="ECO:0000269|PubMed:8088850" FT /id="VAR_004791" FT VARIANT 125 FT /note="L -> R (in RP4)" FT /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8088850" 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 /evidence="ECO:0000269|PubMed:8088850" FT /id="VAR_004802" FT VARIANT 171 FT /note="P -> L (in RP4; dbSNP:rs2084776162)" FT /evidence="ECO:0000269|PubMed:8088850" 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 /evidence="ECO:0000269|PubMed:8088850" FT /id="VAR_004805" FT VARIANT 178 FT /note="Y -> C (in RP4; dbSNP:rs104893776)" FT /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:8401533" 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 /evidence="ECO:0000269|PubMed:1833777" FT /id="VAR_004812" FT VARIANT 190 FT /note="D -> G (in RP4; dbSNP:rs104893777)" FT /evidence="ECO:0000269|PubMed:8401533" FT /id="VAR_004814" FT VARIANT 190 FT /note="D -> N (in RP4; dbSNP:rs104893779)" FT /evidence="ECO:0000269|PubMed:8401533" FT /id="VAR_004813" FT VARIANT 190 FT /note="D -> Y (in RP4; dbSNP:rs104893779)" FT /evidence="ECO:0000269|PubMed:8401533" 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; uncertain significance; 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 /evidence="ECO:0000269|PubMed:8406457" 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 ECO:0000269|PubMed:8088850" FT /id="VAR_004831" FT VARIANT 345 FT /note="V -> M (in RP4; dbSNP:rs104893795)" FT /evidence="ECO:0000269|PubMed:1833777" 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 /evidence="ECO:0000269|PubMed:8088850" 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 FT A-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 //