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Rhodopsin (Opsin-2)

 OPSD_HUMAN              Reviewed;         348 AA.
P08100; Q16414; Q2M249;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
26-FEB-2020, entry version 219.
RecName: Full=Rhodopsin;
AltName: Full=Opsin-2;
Name=RHO; Synonyms=OPN2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6589631; DOI=10.1073/pnas.81.15.4851;
Nathans J., Hogness D.S.;
"Isolation and nucleotide sequence of the gene encoding human rhodopsin.";
Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide diskovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5;
Bennett J., Beller B., Sun D., Kariko K.;
"Sequence analysis of the 5.34-kb 5' flanking region of the human
rhodopsin-encoding gene.";
Gene 167:317-320(1995).
[6]
SUBCELLULAR LOCATION.
PubMed=25664179; DOI=10.1186/s13630-015-0013-1;
Chuang J.Z., Hsu Y.C., Sung C.H.;
"Ultrastructural visualization of trans-ciliary rhodopsin cargoes in
mammalian rods.";
Cilia 4:4-4(2015).
[7]
INTERACTION WITH GRK1 AND SAG, FUNCTION, AND MUTAGENESIS OF GLU-113 AND
MET-257.
PubMed=28524165; DOI=10.1038/cr.2017.72;
He Y., Gao X., Goswami D., Hou L., Pal K., Yin Y., Zhao G., Ernst O.P.,
Griffin P., Melcher K., Xu H.E.;
"Molecular assembly of rhodopsin with G protein-coupled receptor kinases.";
Cell Res. 27:728-747(2017).
[8] {ECO:0000244|PDB:4ZWJ}
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN
COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR
LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, AND DISULFIDE
BONDS.
PubMed=26200343; DOI=10.1038/nature14656;
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A.,
White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H.,
Zhang C., Moeller A., West G.M., Pascal B.D., Van Eps N., Caro L.N.,
Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J.,
Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A.,
Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H.,
Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H.,
Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J.,
Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H.,
Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P.,
Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C.,
Cherezov V., Melcher K., Xu H.E.;
"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray
laser.";
Nature 523:561-567(2015).
[9] {ECO:0000244|PDB:5W0P}
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION,
TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND
SER-338, DISULFIDE BOND, AND MUTAGENESIS OF 336-THR--THR-340;
336-THR--SER-338 AND SER-343.
PubMed=28753425; DOI=10.1016/j.cell.2017.07.002;
Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y.,
Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N.,
Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V.,
Griffin P.R., Ernst O.P., Melcher K., Xu H.E.;
"Identification of Phosphorylation Codes for Arrestin Recruitment by G
Protein-Coupled Receptors.";
Cell 170:457-469(2017).
[10]
REVIEW ON RP4 VARIANTS.
PubMed=8401533; DOI=10.1002/humu.1380020403;
Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A., Bhattacharya S.;
"Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
Hum. Mutat. 2:249-255(1993).
[11]
VARIANTS RP4.
PubMed=2239971;
Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G.,
Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., Watty A.,
Ludwig M., Schinzel A., Samanns C., Gal A., Bhattacharya S.S.,
Humphries P.;
"Autosomal dominant retinitis pigmentosa: absence of the rhodopsin
proline-->histidine substitution (codon 23) in pedigrees from Europe.";
Am. J. Hum. Genet. 47:941-945(1990).
[12]
VARIANT RP4 HIS-23.
PubMed=2137202; DOI=10.1038/343364a0;
Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., Yandell D.W.,
Sandberg M.A., Berson E.L.;
"A point mutation of the rhodopsin gene in one form of retinitis
pigmentosa.";
Nature 343:364-366(1990).
[13]
VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347, AND FUNCTION.
PubMed=2215617; DOI=10.1056/nejm199011083231903;
Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E.,
Sandberg M.A., Berson E.L.;
"Mutations within the rhodopsin gene in patients with autosomal dominant
retinitis pigmentosa.";
N. Engl. J. Med. 323:1302-1307(1990).
[14]
VARIANT RP4 ILE-255 DEL.
PubMed=1985460;
Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C.,
Bhattacharya S.S.;
"A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant
retinitis pigmentosa.";
Am. J. Hum. Genet. 48:26-30(1991).
[15]
VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
PubMed=1897520;
Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.;
"Identification of novel rhodopsin mutations associated with retinitis
pigmentosa by GC-clamped denaturing gradient gel electrophoresis.";
Am. J. Hum. Genet. 49:699-706(1991).
[16]
VARIANT RP4 ARG-347.
PubMed=1840561; DOI=10.1016/0888-7543(91)90159-c;
Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E.,
Schinzel A.;
"Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis
pigmentosa.";
Genomics 11:468-470(1991).
[17]
VARIANTS RP4.
PubMed=1862076; DOI=10.1073/pnas.88.15.6481;
Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., Jacobson S.G.,
Heckenlively J.R., Nowakowski R., Fishman G., Gouras P., Nathans J.;
"Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991).
[18]
VARIANTS RP4.
PubMed=1833777; DOI=10.1073/pnas.88.20.9370;
Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.;
"Mutation spectrum of the rhodopsin gene among patients with autosomal
dominant retinitis pigmentosa.";
Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991).
[19]
VARIANT RP4 ARG-207.
PubMed=1302614; DOI=10.1093/hmg/1.9.769;
Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M.,
Sharpe E., Humphries P.;
"Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin
gene in the original 3q linked family.";
Hum. Mol. Genet. 1:769-771(1992).
[20]
VARIANTS RP4 MET-17 AND LEU-347.
PubMed=1391967; DOI=10.1007/bf01899733;
Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., Sakuma T.,
Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., Kanai A.;
"Point mutations of rhodopsin gene found in Japanese families with
autosomal dominant retinitis pigmentosa (ADRP).";
Jpn. J. Hum. Genet. 37:125-132(1992).
[21]
VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND VARIANTS
ALA-51; ILE-104 AND MET-209.
PubMed=8317502;
Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C.,
Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R.,
Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.;
"Identification of novel rhodopsin mutations responsible for retinitis
pigmentosa: implications for the structure and function of rhodopsin.";
Am. J. Hum. Genet. 53:80-89(1993).
[22]
VARIANT RP4 SER-15.
PubMed=8353500; DOI=10.1093/hmg/2.6.813;
Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P.,
Duvigneau C., Gal A.;
"Autosomal dominant 'sector' retinitis pigmentosa due to a point mutation
predicting an Asn-15-Ser substitution of rhodopsin.";
Hum. Mol. Genet. 2:813-814(1993).
[23]
VARIANT CSNBAD1 GLU-292.
PubMed=8358437; DOI=10.1038/ng0793-280;
Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.;
"Heterozygous missense mutation in the rhodopsin gene as a cause of
congenital stationary night blindness.";
Nat. Genet. 4:280-283(1993).
[24]
VARIANTS RP4.
PubMed=8088850; DOI=10.1006/geno.1994.1301;
Vaithinathan R., Berson E.L., Dryja T.P.;
"Further screening of the rhodopsin gene in patients with autosomal
dominant retinitis pigmentosa.";
Genomics 21:461-463(1994).
[25]
VARIANT RP4 THR-44.
PubMed=8076945; DOI=10.1007/bf00208284;
Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C.,
Carballo M.;
"Identification of a novel rhodopsin mutation (Met-44-Thr) in a simplex
case of retinitis pigmentosa.";
Hum. Genet. 94:283-286(1994).
[26]
VARIANTS RP4 PHE-110; PRO-131 AND VAL-164.
PubMed=7981701; DOI=10.1093/hmg/3.7.1203;
Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S.,
Humphries P., Gal A.;
"Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with
autosomal dominant retinitis pigmentosa.";
Hum. Mol. Genet. 3:1203-1203(1994).
[27]
VARIANT RP4 GLN-171.
PubMed=7987326; DOI=10.1093/hmg/3.8.1421;
Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., Cabeza J.C.;
"Identification of a new mutation at codon 171 of rhodopsin gene causing
autosomal dominant retinitis pigmentosa.";
Hum. Mol. Genet. 3:1421-1421(1994).
[28]
VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
PubMed=7987331; DOI=10.1093/hmg/3.8.1433;
Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I.,
Philip N., Soubrane G., Coscas G., Munnich A.;
"Five novel missense mutations of the rhodopsin gene in autosomal dominant
retinitis pigmentosa.";
Hum. Mol. Genet. 3:1433-1434(1994).
[29]
VARIANTS RP4 ARG-40 AND LYS-216.
PubMed=8081400; DOI=10.1002/humu.1380030417;
Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., Bhattacharya S.;
"Two new rhodopsin transversion mutations (L40R; M216K) in families with
autosomal dominant retinitis pigmentosa.";
Hum. Mutat. 3:409-410(1994).
[30]
VARIANT RP4 LEU-345.
PubMed=8045708;
Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.;
"Autosomal dominant retinitis pigmentosa in a large family: a clinical and
molecular genetic study.";
Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994).
[31]
CHARACTERIZATION OF VARIANT CSNBAD1 ASP-90, AND FUNCTION.
PubMed=8107847; DOI=10.1038/367639a0;
Rao V.R., Cohen G.B., Oprian D.D.;
"Rhodopsin mutation G90D and a molecular mechanism for congenital night
blindness.";
Nature 367:639-642(1994).
[32]
VARIANT ARRP LYS-150.
PubMed=7987385; DOI=10.1038/ng0994-10;
Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R., Orth U.,
Oehlmann R., Gal A.;
"Missense rhodopsin mutation in a family with recessive RP.";
Nat. Genet. 8:10-11(1994).
[33]
VARIANT RP4 ALA-347.
PubMed=7633434; DOI=10.1093/hmg/4.4.775;
Macke J.P., Hennessey J.C., Nathans J.;
"Rhodopsin mutation proline347-to-alanine in a family with autosomal
dominant retinitis pigmentosa indicates an important role for proline at
position 347.";
Hum. Mol. Genet. 4:775-776(1995).
[34]
VARIANT CSNBAD1 ASP-90, AND FUNCTION.
PubMed=7846071; DOI=10.1073/pnas.92.3.880;
Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K.,
Alpern M.;
"Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp
mutation.";
Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995).
[35]
VARIANT RP4 TRP-135.
PubMed=8554077; DOI=10.1016/s0002-9394(14)70530-6;
Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., Munnich A.,
Kaplan J.;
"Retinitis punctata albescens associated with the Arg135Trp mutation in the
rhodopsin gene.";
Am. J. Ophthalmol. 121:19-25(1996).
[36]
VARIANT RP4 ARG-109.
PubMed=9452035; DOI=10.1002/humu.1380110114;
Goliath R., Bardien S., September A., Martin R., Ramesar R., Greenberg J.;
"Rhodopsin mutation G109R in a family with autosomal dominant retinitis
pigmentosa.";
Hum. Mutat. Suppl. 1:S40-S41(1998).
[37]
VARIANT CSNBAD1 ILE-94.
PubMed=9888392;
DOI=10.1002/(sici)1098-1004(1999)13:1<75::aid-humu9>3.0.co;2-4;
Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N.,
Findlay J.B.C., Humphries P., Kenna P.F.;
"A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal
dominant congenital stationary night blindness.";
Hum. Mutat. 13:75-81(1999).
[38]
CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12566452; DOI=10.1074/jbc.m300087200;
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K.,
Kaushal S.;
"Pharmacological chaperone-mediated in vivo folding and stabilization of
the P23H-opsin mutant associated with autosomal dominant retinitis
pigmentosa.";
J. Biol. Chem. 278:14442-14450(2003).
[39]
CHARACTERIZATION OF VARIANT RP4 HIS-23, AND SUBCELLULAR LOCATION.
PubMed=19934218; DOI=10.1242/jcs.055228;
Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.;
"A dual role for EDEM1 in the processing of rod opsin.";
J. Cell Sci. 122:4465-4472(2009).
[40]
VARIANT RP4 LYS-150.
PubMed=19960070;
Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., Sadeque A.,
Bokhari H., Collin R.W., Orth U., van Genderen M.M., den Hollander A.I.,
Cremers F.P., Qamar R.;
"A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani
families with autosomal recessive retinitis pigmentosa.";
Mol. Vis. 15:2526-2534(2009).
[41]
VARIANTS RP4 TRP-135; SER-180 AND ASN-214.
PubMed=22334370; DOI=10.1002/humu.22045;
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E.,
den Hollander A.I., Hoischen A., Hoyng C., Klevering B.J.,
van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.;
"Next-generation genetic testing for retinitis pigmentosa.";
Hum. Mutat. 33:963-972(2012).
[42]
VARIANT ILE-104.
PubMed=28837730; DOI=10.1167/iovs.16-20941;
Wang B., Liu Y., Chen S., Wu Y., Lin S., Duan Y., Zheng K., Zhang L.,
Gu X., Hong W., Shao H., Zeng X., Sun B., Duan S.;
"A novel potentially causative variant of NDUFAF7 revealed by mutation
screening in a chinese family with pathologic myopia.";
Invest. Ophthalmol. Vis. Sci. 58:4182-4192(2017).
-!- FUNCTION: Photoreceptor required for image-forming vision at low light
intensity (PubMed:8107847, PubMed:7846071). Required for photoreceptor
cell viability after birth (PubMed:2215617, PubMed:12566452). Light-
induced isomerization of the chromophore 11-cis-retinal to all-trans-
retinal triggers a conformational change that activates signaling via
G-proteins (PubMed:8107847, PubMed:28524165, PubMed:26200343,
PubMed:28753425). Subsequent receptor phosphorylation mediates
displacement of the bound G-protein alpha subunit by the arrestin SAG
and terminates signaling (PubMed:28524165, PubMed:26200343).
{ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:2215617,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425,
ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847,
ECO:0000305|PubMed:28524165}.
-!- SUBUNIT: Homodimer (By similarity). May form a complex composed of RHO,
GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the
interaction between GRK1 and RHO (By similarity). Interacts with GRK1
(PubMed:28524165). Interacts (phosphorylated form) with SAG
(PubMed:28524165, PubMed:26200343, PubMed:28753425). Interacts with
GNAT1 (PubMed:26200343). Interacts with GNAT3. SAG and G-proteins
compete for a common binding site (PubMed:26200343). Interacts with
PRCD; the interaction promotes PRCD stability (By similarity).
{ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P15409,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28524165,
ECO:0000269|PubMed:28753425}.
-!- INTERACTION:
O95405:ZFYVE9; NbExp=2; IntAct=EBI-1394177, EBI-296817;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12566452,
ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25664179,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}; Multi-pass
membrane protein {ECO:0000269|PubMed:19934218,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. Cell
projection, cilium, photoreceptor outer segment
{ECO:0000269|PubMed:25664179}. Note=Synthesized in the inner segment
(IS) of rod photoreceptor cells before vectorial transport to disk
membranes in the rod outer segment (OS) photosensory cilia.
{ECO:0000269|PubMed:25664179}.
-!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediate vision
in dim light.
-!- PTM: Phosphorylated on some or all of the serine and threonine residues
present in the C-terminal region (By similarity). After activation by
light, phosphorylated by GRK1 (in vitro) (PubMed:28524165).
{ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:28524165}.
-!- PTM: Contains one covalently linked retinal chromophore. Upon light
absorption, the covalently bound 11-cis-retinal is converted to all-
trans-retinal. After hydrolysis of the Schiff base and release of the
covalently bound all-trans-retinal, active rhodopsin is regenerated by
binding of a fresh molecule of 11-cis-retinal(PubMed:12566452).
{ECO:0000269|PubMed:12566452}.
-!- DISEASE: Retinitis pigmentosa 4 (RP4) [MIM:613731]: A retinal dystrophy
belonging to the group of pigmentary retinopathies. Retinitis
pigmentosa is characterized by retinal pigment deposits visible on
fundus examination and primary loss of rod photoreceptor cells followed
by secondary loss of cone photoreceptors. Patients typically have night
vision blindness and loss of midperipheral visual field. As their
condition progresses, they lose their far peripheral visual field and
eventually central vision as well. {ECO:0000269|PubMed:12566452,
ECO:0000269|PubMed:1302614, ECO:0000269|PubMed:1391967,
ECO:0000269|PubMed:1833777, ECO:0000269|PubMed:1840561,
ECO:0000269|PubMed:1862076, ECO:0000269|PubMed:1897520,
ECO:0000269|PubMed:1985460, ECO:0000269|PubMed:19934218,
ECO:0000269|PubMed:19960070, ECO:0000269|PubMed:2137202,
ECO:0000269|PubMed:2215617, ECO:0000269|PubMed:22334370,
ECO:0000269|PubMed:2239971, ECO:0000269|PubMed:7633434,
ECO:0000269|PubMed:7981701, ECO:0000269|PubMed:7987326,
ECO:0000269|PubMed:7987331, ECO:0000269|PubMed:8045708,
ECO:0000269|PubMed:8076945, ECO:0000269|PubMed:8081400,
ECO:0000269|PubMed:8088850, ECO:0000269|PubMed:8317502,
ECO:0000269|PubMed:8353500, ECO:0000269|PubMed:8554077,
ECO:0000269|PubMed:9452035}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Night blindness, congenital stationary, autosomal dominant 1
(CSNBAD1) [MIM:610445]: A non-progressive retinal disorder
characterized by impaired night vision, often associated with nystagmus
and myopia. {ECO:0000269|PubMed:7846071, ECO:0000269|PubMed:8107847,
ECO:0000269|PubMed:8358437, ECO:0000269|PubMed:9888392}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=Mutations of the RHO gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/rhomut.htm";
-!- WEB RESOURCE: Name=Wikipedia; Note=Rhodopsin entry;
URL="https://en.wikipedia.org/wiki/Rhodopsin";
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EMBL; U49742; AAC31763.1; -; Genomic_DNA.
EMBL; AB065668; BAC05894.1; -; Genomic_DNA.
EMBL; BX537381; CAD97623.1; -; mRNA.
EMBL; BC112104; AAI12105.1; -; mRNA.
EMBL; BC112106; AAI12107.1; -; mRNA.
EMBL; U16824; AAA97436.1; -; Genomic_DNA.
EMBL; S81166; AAB35906.1; -; Genomic_DNA.
CCDS; CCDS3063.1; -.
PIR; A41200; OOHU.
RefSeq; NP_000530.1; NM_000539.3.
PDB; 4ZWJ; X-ray; 3.30 A; A/B/C/D=1-348.
PDB; 5DGY; X-ray; 7.70 A; A/B/C/D=1-348.
PDB; 5W0P; X-ray; 3.01 A; A/B/C/D=1-348.
PDB; 6CMO; EM; 4.50 A; R=3-323.
PDBsum; 4ZWJ; -.
PDBsum; 5DGY; -.
PDBsum; 5W0P; -.
PDBsum; 6CMO; -.
SMR; P08100; -.
BioGrid; 111942; 11.
IntAct; P08100; 4.
STRING; 9606.ENSP00000296271; -.
DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DrugBank; DB01728; 3-[Aminoethylphosphoryl]-[1,2-Di-Palmitoyl]-Sn-Glycerol.
DrugBank; DB03152; B-2-Octylglucoside.
DrugBank; DB02451; B-nonylglucoside.
DrugBank; DB04522; Dexfosfoserine.
DrugBank; DB01159; Halothane.
DrugBank; DB04079; Heptane-1,2,3-Triol.
DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DrugBank; DB03381; Hexadecanal.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
DrugBank; DB01646; N-Acetylmethionine.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB02482; Phosphonothreonine.
TCDB; 9.A.14.1.2; the g-protein-coupled receptor (gpcr) family.
GlyConnect; 525; -.
iPTMnet; P08100; -.
PhosphoSitePlus; P08100; -.
SwissPalm; P08100; -.
UniCarbKB; P08100; -.
BioMuta; RHO; -.
DMDM; 129207; -.
MassIVE; P08100; -.
PaxDb; P08100; -.
PeptideAtlas; P08100; -.
PRIDE; P08100; -.
ProteomicsDB; 52066; -.
DNASU; 6010; -.
Ensembl; ENST00000296271; ENSP00000296271; ENSG00000163914.
GeneID; 6010; -.
KEGG; hsa:6010; -.
UCSC; uc003emt.4; human.
CTD; 6010; -.
DisGeNET; 6010; -.
GeneCards; RHO; -.
GeneReviews; RHO; -.
HGNC; HGNC:10012; RHO.
HPA; CAB022486; -.
HPA; CAB034887; -.
HPA; CAB034888; -.
HPA; HPA013440; -.
MalaCards; RHO; -.
MIM; 180380; gene.
MIM; 610445; phenotype.
MIM; 613731; phenotype.
neXtProt; NX_P08100; -.
OpenTargets; ENSG00000163914; -.
Orphanet; 215; Congenital stationary night blindness.
Orphanet; 791; Retinitis pigmentosa.
Orphanet; 52427; Retinitis punctata albescens.
PharmGKB; PA34390; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00960000186618; -.
HOGENOM; CLU_009579_3_0_1; -.
InParanoid; P08100; -.
KO; K04250; -.
OMA; LYVTIQH; -.
OrthoDB; 541116at2759; -.
PhylomeDB; P08100; -.
TreeFam; TF324998; -.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-419771; Opsins.
Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
SignaLink; P08100; -.
SIGNOR; P08100; -.
ChiTaRS; RHO; human.
GeneWiki; Rhodopsin; -.
GenomeRNAi; 6010; -.
Pharos; P08100; Tbio.
PRO; PR:P08100; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P08100; protein.
Bgee; ENSG00000163914; Expressed in retina and 86 other tissues.
Genevisible; P08100; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0097381; C:photoreceptor disc membrane; IDA:UniProtKB.
GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
GO; GO:0007602; P:phototransduction; IBA:GO_Central.
GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR001760; Opsin.
InterPro; IPR027430; Retinal_BS.
InterPro; IPR000732; Rhodopsin.
InterPro; IPR019477; Rhodopsin_N.
Pfam; PF00001; 7tm_1; 1.
Pfam; PF10413; Rhodopsin_N; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00238; OPSIN.
PRINTS; PR00579; RHODOPSIN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE; PS00238; OPSIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell projection; Chromophore;
Congenital stationary night blindness; Disease mutation; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein;
Polymorphism; Receptor; Reference proteome; Retinal protein;
Retinitis pigmentosa; Sensory transduction; Transducer; Transmembrane;
Transmembrane helix; Vision; Zinc.
CHAIN 1..348
/note="Rhodopsin"
/id="PRO_0000197677"
TOPO_DOM 1..36
/note="Extracellular"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 37..61
/note="Helical; Name=1"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 62..73
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 74..96
/note="Helical; Name=2"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 97..110
/note="Extracellular"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 111..133
/note="Helical; Name=3"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 134..152
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 153..173
/note="Helical; Name=4"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 174..202
/note="Extracellular"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 203..224
/note="Helical; Name=5"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 225..252
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 253..274
/note="Helical; Name=6"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 275..284
/note="Extracellular"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TRANSMEM 285..309
/note="Helical; Name=7"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
TOPO_DOM 310..348
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
REGION 330..348
/note="Interaction with SAG"
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425"
MOTIF 134..136
/note="'Ionic lock' involved in activated form
stabilization"
/evidence="ECO:0000305|PubMed:26200343"
METAL 201
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P02699"
METAL 279
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P02699"
SITE 113
/note="Plays an important role in the conformation switch
to the active conformation"
/evidence="ECO:0000269|PubMed:26200343"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000250|UniProtKB:P02699"
MOD_RES 296
/note="N6-(retinylidene)lysine"
/evidence="ECO:0000250|UniProtKB:P02699"
MOD_RES 334
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:28753425"
MOD_RES 336
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:28753425"
MOD_RES 338
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:28753425"
MOD_RES 340
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P02699"
MOD_RES 342
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P02699"
MOD_RES 343
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P02699"
LIPID 322
/note="S-palmitoyl cysteine"
/evidence="ECO:0000250|UniProtKB:P02699"
LIPID 323
/note="S-palmitoyl cysteine"
/evidence="ECO:0000250|UniProtKB:P02699"
CARBOHYD 2
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000250|UniProtKB:P02699"
CARBOHYD 15
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:28753425"
DISULFID 110..187
/evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425"
VARIANT 4
/note="T -> K (in RP4)"
/id="VAR_004765"
VARIANT 15
/note="N -> S (in RP4; dbSNP:rs104893786)"
/evidence="ECO:0000269|PubMed:8353500"
/id="VAR_004766"
VARIANT 17
/note="T -> M (in RP4; dbSNP:rs104893769)"
/evidence="ECO:0000269|PubMed:1391967,
ECO:0000269|PubMed:1897520"
/id="VAR_004767"
VARIANT 23
/note="P -> H (in RP4; most common variant; impairs protein
folding; leads to interaction with EDEM1 followed by
degradation by the ERAD system; dbSNP:rs104893768)"
/evidence="ECO:0000269|PubMed:12566452,
ECO:0000269|PubMed:1897520, ECO:0000269|PubMed:19934218,
ECO:0000269|PubMed:2137202, ECO:0000269|PubMed:2215617"
/id="VAR_004768"
VARIANT 23
/note="P -> L (in RP4)"
/id="VAR_004769"
VARIANT 28
/note="Q -> H (in RP4)"
/id="VAR_004770"
VARIANT 40
/note="L -> R (in RP4)"
/evidence="ECO:0000269|PubMed:8081400"
/id="VAR_004771"
VARIANT 44
/note="M -> T (in RP4; dbSNP:rs774336493)"
/evidence="ECO:0000269|PubMed:8076945"
/id="VAR_004772"
VARIANT 45
/note="F -> L (in RP4; dbSNP:rs104893770)"
/id="VAR_004773"
VARIANT 46
/note="L -> R (in RP4)"
/id="VAR_004774"
VARIANT 51
/note="G -> A (in dbSNP:rs149079952)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004775"
VARIANT 51
/note="G -> R (in RP4; dbSNP:rs104893792)"
/id="VAR_004776"
VARIANT 51
/note="G -> V (in RP4)"
/id="VAR_004777"
VARIANT 53
/note="P -> R (in RP4; dbSNP:rs28933395)"
/id="VAR_004778"
VARIANT 58
/note="T -> R (in RP4; dbSNP:rs28933394)"
/evidence="ECO:0000269|PubMed:1897520,
ECO:0000269|PubMed:2215617"
/id="VAR_004779"
VARIANT 68..71
/note="Missing (in RP4)"
/id="VAR_004780"
VARIANT 87
/note="V -> D (in RP4; dbSNP:rs104893771)"
/id="VAR_004781"
VARIANT 89
/note="G -> D (in RP4; dbSNP:rs104893772)"
/id="VAR_004782"
VARIANT 90
/note="G -> D (in CSNBAD1; constitutive activity in the
absence of bound retinal; dbSNP:rs104893790)"
/evidence="ECO:0000269|PubMed:7846071,
ECO:0000269|PubMed:8107847"
/id="VAR_004783"
VARIANT 94
/note="T -> I (in CSNBAD1; dbSNP:rs104893796)"
/evidence="ECO:0000269|PubMed:9888392"
/id="VAR_004784"
VARIANT 104
/note="V -> I (found in patients with pathologic myopia;
unknown pathological significance; dbSNP:rs144317206)"
/evidence="ECO:0000269|PubMed:28837730,
ECO:0000269|PubMed:8317502"
/id="VAR_004785"
VARIANT 106
/note="G -> R (in RP4; dbSNP:rs104893773)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004786"
VARIANT 106
/note="G -> W (in RP4; dbSNP:rs104893773)"
/id="VAR_004787"
VARIANT 109
/note="G -> R (in RP4; dbSNP:rs1415160298)"
/evidence="ECO:0000269|PubMed:9452035"
/id="VAR_004788"
VARIANT 110
/note="C -> F (in RP4)"
/evidence="ECO:0000269|PubMed:7981701"
/id="VAR_004789"
VARIANT 110
/note="C -> Y (in RP4; dbSNP:rs104893787)"
/id="VAR_004790"
VARIANT 114
/note="G -> D (in RP4; dbSNP:rs104893788)"
/id="VAR_004791"
VARIANT 125
/note="L -> R (in RP4)"
/id="VAR_004792"
VARIANT 127
/note="S -> F (in RP4)"
/evidence="ECO:0000269|PubMed:7987331"
/id="VAR_004793"
VARIANT 131
/note="L -> P (in RP4; dbSNP:rs1553781140)"
/evidence="ECO:0000269|PubMed:7981701,
ECO:0000269|PubMed:7987331"
/id="VAR_004794"
VARIANT 135
/note="R -> G (in RP4)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004795"
VARIANT 135
/note="R -> L (in RP4; dbSNP:rs104893774)"
/id="VAR_004796"
VARIANT 135
/note="R -> W (in RP4; dbSNP:rs104893775)"
/evidence="ECO:0000269|PubMed:22334370,
ECO:0000269|PubMed:8554077"
/id="VAR_004797"
VARIANT 140
/note="C -> S (in RP4)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004798"
VARIANT 150
/note="E -> K (in RP4; autosomal recessive;
dbSNP:rs104893791)"
/evidence="ECO:0000269|PubMed:19960070,
ECO:0000269|PubMed:7987385"
/id="VAR_004799"
VARIANT 164
/note="A -> E (in RP4; dbSNP:rs104893793)"
/id="VAR_004800"
VARIANT 164
/note="A -> V (in RP4; dbSNP:rs104893793)"
/evidence="ECO:0000269|PubMed:7981701"
/id="VAR_004801"
VARIANT 167
/note="C -> R (in RP4)"
/id="VAR_004802"
VARIANT 171
/note="P -> L (in RP4)"
/id="VAR_004803"
VARIANT 171
/note="P -> Q (in RP4)"
/evidence="ECO:0000269|PubMed:7987326"
/id="VAR_004804"
VARIANT 171
/note="P -> S (in RP4; dbSNP:rs104893794)"
/id="VAR_004805"
VARIANT 178
/note="Y -> C (in RP4; dbSNP:rs104893776)"
/id="VAR_004806"
VARIANT 178
/note="Y -> N (in RP4)"
/evidence="ECO:0000269|PubMed:7987331"
/id="VAR_004807"
VARIANT 180
/note="P -> S (in RP4)"
/evidence="ECO:0000269|PubMed:22334370"
/id="VAR_068359"
VARIANT 181
/note="E -> K (in RP4; dbSNP:rs775557680)"
/id="VAR_004808"
VARIANT 182
/note="G -> S (in RP4; dbSNP:rs104893780)"
/evidence="ECO:0000269|PubMed:1897520"
/id="VAR_004809"
VARIANT 186
/note="S -> P (in RP4)"
/id="VAR_004810"
VARIANT 188
/note="G -> E (in RP4; dbSNP:rs1424131846)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004811"
VARIANT 188
/note="G -> R (in RP4; dbSNP:rs527236100)"
/id="VAR_004812"
VARIANT 190
/note="D -> G (in RP4; dbSNP:rs104893777)"
/id="VAR_004814"
VARIANT 190
/note="D -> N (in RP4; dbSNP:rs104893779)"
/id="VAR_004813"
VARIANT 190
/note="D -> Y (in RP4; dbSNP:rs104893779)"
/id="VAR_004815"
VARIANT 207
/note="M -> R (in RP4; dbSNP:rs104893782)"
/evidence="ECO:0000269|PubMed:1302614"
/id="VAR_004816"
VARIANT 209
/note="V -> M (found in a patient with retinitis
pigmentosa; unknown pathological significance;
dbSNP:rs567288669)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004817"
VARIANT 211
/note="H -> P (in RP4; dbSNP:rs28933993)"
/id="VAR_004818"
VARIANT 211
/note="H -> R (in RP4)"
/evidence="ECO:0000269|PubMed:8317502"
/id="VAR_004819"
VARIANT 214
/note="I -> N (in RP4)"
/evidence="ECO:0000269|PubMed:22334370"
/id="VAR_068360"
VARIANT 216
/note="M -> K (in RP4)"
/evidence="ECO:0000269|PubMed:8081400"
/id="VAR_004820"
VARIANT 220
/note="F -> C (in RP4; dbSNP:rs766161322)"
/id="VAR_004821"
VARIANT 222
/note="C -> R (in RP4)"
/id="VAR_004822"
VARIANT 255
/note="Missing (in RP4)"
/evidence="ECO:0000269|PubMed:1985460"
/id="VAR_004823"
VARIANT 264
/note="Missing (in RP4)"
/id="VAR_004824"
VARIANT 267
/note="P -> L (in RP4; dbSNP:rs104893781)"
/evidence="ECO:0000269|PubMed:1897520"
/id="VAR_004825"
VARIANT 267
/note="P -> R (in RP4)"
/evidence="ECO:0000269|PubMed:7987331"
/id="VAR_004826"
VARIANT 292
/note="A -> E (in CSNBAD1; dbSNP:rs104893789)"
/evidence="ECO:0000269|PubMed:8358437"
/id="VAR_004827"
VARIANT 296
/note="K -> E (in RP4; dbSNP:rs29001653)"
/id="VAR_004828"
VARIANT 297
/note="S -> R (in RP4)"
/evidence="ECO:0000269|PubMed:7987331"
/id="VAR_004829"
VARIANT 342
/note="T -> M (in RP4; dbSNP:rs183318466)"
/id="VAR_004830"
VARIANT 345
/note="V -> L (in RP4; dbSNP:rs104893795)"
/evidence="ECO:0000269|PubMed:8045708"
/id="VAR_004831"
VARIANT 345
/note="V -> M (in RP4; dbSNP:rs104893795)"
/id="VAR_004832"
VARIANT 347
/note="P -> A (in RP4)"
/evidence="ECO:0000269|PubMed:7633434"
/id="VAR_004833"
VARIANT 347
/note="P -> L (in RP4; common variant; dbSNP:rs29001566)"
/evidence="ECO:0000269|PubMed:1391967,
ECO:0000269|PubMed:2215617"
/id="VAR_004834"
VARIANT 347
/note="P -> Q (in RP4; dbSNP:rs29001566)"
/id="VAR_004835"
VARIANT 347
/note="P -> R (in RP4; dbSNP:rs29001566)"
/evidence="ECO:0000269|PubMed:1840561"
/id="VAR_004836"
VARIANT 347
/note="P -> S (in RP4; dbSNP:rs29001637)"
/evidence="ECO:0000269|PubMed:2215617"
/id="VAR_004837"
MUTAGEN 113
/note="E->Q: Induces a conformation change that promotes
interaction with GRK1 and SAG; when associated with Y-257."
/evidence="ECO:0000269|PubMed:26200343"
MUTAGEN 257
/note="M->Y: Induces a conformation change that promotes
interaction with GRK1 and SAG; when associated with Q-113."
/evidence="ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28524165"
MUTAGEN 336..340
/note="TVSKT->AVAKA: Loss of phosphorylation sites and
decreased interaction with SAG."
/evidence="ECO:0000269|PubMed:28753425"
MUTAGEN 336..338
/note="TVS->AVA: Loss of phosphorylation sites and
decreased interaction with SAG; when associated with A-
343."
/evidence="ECO:0000269|PubMed:28753425"
MUTAGEN 343
/note="S->A: Loss of phosphorylation sites and decreased
interaction with SAG; when associated with 336-A--A-338."
/evidence="ECO:0000269|PubMed:28753425"
STRAND 2..5
/evidence="ECO:0000244|PDB:5W0P"
STRAND 10..13
/evidence="ECO:0000244|PDB:5W0P"
STRAND 16..18
/evidence="ECO:0000244|PDB:5W0P"
TURN 23..25
/evidence="ECO:0000244|PDB:5W0P"
TURN 29..31
/evidence="ECO:0000244|PDB:4ZWJ"
HELIX 35..64
/evidence="ECO:0000244|PDB:5W0P"
HELIX 66..68
/evidence="ECO:0000244|PDB:5W0P"
TURN 71..73
/evidence="ECO:0000244|PDB:5W0P"
HELIX 74..88
/evidence="ECO:0000244|PDB:5W0P"
HELIX 90..100
/evidence="ECO:0000244|PDB:5W0P"
HELIX 106..140
/evidence="ECO:0000244|PDB:5W0P"
HELIX 143..147
/evidence="ECO:0000244|PDB:5W0P"
HELIX 150..168
/evidence="ECO:0000244|PDB:5W0P"
HELIX 170..173
/evidence="ECO:0000244|PDB:5W0P"
STRAND 174..176
/evidence="ECO:0000244|PDB:4ZWJ"
STRAND 178..181
/evidence="ECO:0000244|PDB:5W0P"
TURN 182..185
/evidence="ECO:0000244|PDB:5W0P"
STRAND 186..189
/evidence="ECO:0000244|PDB:5W0P"
STRAND 191..193
/evidence="ECO:0000244|PDB:5W0P"
TURN 196..199
/evidence="ECO:0000244|PDB:5W0P"
HELIX 200..209
/evidence="ECO:0000244|PDB:5W0P"
TURN 210..212
/evidence="ECO:0000244|PDB:5W0P"
HELIX 213..236
/evidence="ECO:0000244|PDB:5W0P"
HELIX 241..277
/evidence="ECO:0000244|PDB:5W0P"
HELIX 285..306
/evidence="ECO:0000244|PDB:5W0P"
TURN 307..309
/evidence="ECO:0000244|PDB:5W0P"
HELIX 311..321
/evidence="ECO:0000244|PDB:5W0P"
TURN 322..324
/evidence="ECO:0000244|PDB:4ZWJ"
TURN 331..333
/evidence="ECO:0000244|PDB:5W0P"
STRAND 339..341
/evidence="ECO:0000244|PDB:5W0P"
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


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BMMS-1233-MX Rhodopsin (Opsin) MTO
BMMS-1233-B1X Rhodopsin (Opsin) 0.1mL
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BMMS-1233-B1 Rhodopsin (Opsin) 0.5mL
BMMS-1233-B1X Rhodopsin (Opsin) 0.1mL
BMMS-1233-B Rhodopsin (Opsin) 1mL
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Q01127M Rhodopsin (opsin) host: Mouse 125ug
Q01127M Rhodopsin (opsin)Mouse Purified IgG1 125ug
MD-14-0505 Mouse Anti-Rhodopsin (opsin) Antibodies 125ug
Pathways :
WP1072: GPCRs, Class A Rhodopsin-like
WP455: GPCRs, Class A Rhodopsin-like
WP954: GPCRs, Class A Rhodopsin-like
WP189: GPCRs, Class A Rhodopsin-like
WP836: GPCRs, Class A Rhodopsin-like
WP1188: GPCRs, Class A Rhodopsin-like
WP473: GPCRs, Class A Rhodopsin-like

Related Genes :
[RHO OPN2] Rhodopsin (Opsin-2)
[Rh6 CG5192] Opsin Rh6 (Rhodopsin Rh6, long-wavelength)
[ninaE Rh1 GA18249] Opsin Rh1 (Outer R1-R6 photoreceptor cells opsin)
[rho zfo2] Rhodopsin
[ninaE Rh1 CG4550] Opsin Rh1 (Neither inactivation nor afterpotential E protein) (Outer R1-R6 photoreceptor cells opsin)
[RHO] Rhodopsin
[Rho] Rhodopsin
[RHO] Rhodopsin
[Rho] Rhodopsin
[RHO RHO1] Rhodopsin
[Opn4 Mop Mopn] Melanopsin (Opsin-4)
[Rh5 CG5279] Opsin Rh5
[RHO RH1] Rhodopsin
[Opn1sw Bcp] Short-wave-sensitive opsin 1 (S opsin) (Blue cone photoreceptor pigment) (Blue-sensitive opsin) (BOP) (Short wavelength-sensitive cone opsin)
[Rh3 RH92CD CG10888] Opsin Rh3 (Inner R7 photoreceptor cells opsin)
[opn1mw1 grops1 rh21] Green-sensitive opsin-1 (Green cone photoreceptor pigment 1) (Opsin RH2-1) (Opsin-1, medium-wave-sensitive 1)
[RHO OPS] Rhodopsin
[RHO] Rhodopsin
[opn1mw4 grops2 rh24] Green-sensitive opsin-4 (Green cone photoreceptor pigment 4) (Opsin RH2-4) (Opsin-1, medium-wave-sensitive 4)
[RHO] Rhodopsin
[Opn1sw Bcp] Short-wave-sensitive opsin 1 (S opsin) (Blue cone photoreceptor pigment) (Blue-sensitive opsin) (BOP) (Short wavelength-sensitive cone opsin)
[PRA1] Green-sensitive opsin (Green cone photoreceptor pigment)
[Opn5 Gpr136 Pgr12] Opsin-5 (G-protein coupled receptor 136) (G-protein coupled receptor PGR12) (Neuropsin)
[nop-1 NCU10055] Opsin-1 (NR)
[] Pinopsin (Pineal gland-specific opsin) (P-opsin) (Pineal opsin)
[Opn1mw Gcp] Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (M opsin) (Medium wavelength-sensitive cone opsin)
[Opn1mw Gcp] Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (Medium wavelength-sensitive cone opsin)
[OPN1MW GCP] Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (GOP)
[OPN1SW BCP] Short-wave-sensitive opsin 1 (Blue cone photoreceptor pigment) (Blue-sensitive opsin) (BOP)
[OPN5 GPR136 PGR12 TMEM13] Opsin-5 (G-protein coupled receptor 136) (G-protein coupled receptor PGR12) (Neuropsin) (Transmembrane protein 13)

Bibliography :
[28782536] Immunolesion of melanopsin neurons causes gonadal regression in Pekin drakes (Anas platyrhynchos domesticus).
[28418107] A new path in defining light parameters for hair growth: Discovery and modulation of photoreceptors in human hair follicle.
[619987] Effect of alterations in the amphipathic microenvironment on the conformational stability of bovine opsin. 2. Rate of loss of opsin regenerability.
[453] Photoreceptor processes: some problems and perspectives.