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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.
12-SEP-2018, entry version 206.
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;
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;
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). 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 (By similarity). Interacts with GRK1
(PubMed:28524165). {ECO:0000250|UniProtKB:P02699,
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.
UniGene; Hs.247565; -.
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; -.
ProteinModelPortal; P08100; -.
SMR; P08100; -.
BioGrid; 111942; 11.
IntAct; P08100; 4.
STRING; 9606.ENSP00000296271; -.
DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DrugBank; DB03152; B-2-Octylglucoside.
DrugBank; DB01159; Halothane.
DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DrugBank; DB03381; Hexadecanal.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
DrugBank; DB01646; N-Acetylmethionine.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB04522; Phosphonoserine.
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; -.
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; -.
EuPathDB; HostDB:ENSG00000163914.4; -.
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; ENSGT00760000118977; -.
HOGENOM; HOG000253932; -.
HOVERGEN; HBG107442; -.
InParanoid; P08100; -.
KO; K04250; -.
OMA; LAAYMFM; -.
OrthoDB; EOG091G0BDA; -.
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; -.
PRO; PR:P08100; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163914; Expressed in 87 organ(s), highest expression level in retina.
CleanEx; HS_RHO; -.
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; TAS:ProtInc.
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:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
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;
Complete proteome; 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 Rhodopsin.
/FTId=PRO_0000197677.
TOPO_DOM 1 36 Extracellular.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 37 61 Helical; Name=1.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 62 73 Cytoplasmic.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 74 96 Helical; Name=2.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 97 110 Extracellular.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 111 133 Helical; Name=3.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 134 152 Cytoplasmic.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 153 173 Helical; Name=4.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 174 202 Extracellular.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 203 224 Helical; Name=5.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 225 252 Cytoplasmic.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 253 274 Helical; Name=6.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 275 284 Extracellular.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TRANSMEM 285 309 Helical; Name=7.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
TOPO_DOM 310 348 Cytoplasmic.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
REGION 330 348 Interaction with SAG.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
MOTIF 134 136 'Ionic lock' involved in activated form
stabilization.
{ECO:0000305|PubMed:26200343}.
METAL 201 201 Zinc. {ECO:0000250|UniProtKB:P02699}.
METAL 279 279 Zinc. {ECO:0000250|UniProtKB:P02699}.
SITE 113 113 Plays an important role in the
conformation switch to the active
conformation.
{ECO:0000269|PubMed:26200343}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 296 296 N6-(retinylidene)lysine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000269|PubMed:28753425}.
MOD_RES 336 336 Phosphothreonine.
{ECO:0000269|PubMed:28753425}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000269|PubMed:28753425}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 342 342 Phosphothreonine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P02699}.
LIPID 322 322 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P02699}.
LIPID 323 323 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P02699}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P02699}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:28753425}.
DISULFID 110 187 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28753425}.
VARIANT 4 4 T -> K (in RP4).
/FTId=VAR_004765.
VARIANT 15 15 N -> S (in RP4; dbSNP:rs104893786).
{ECO:0000269|PubMed:8353500}.
/FTId=VAR_004766.
VARIANT 17 17 T -> M (in RP4; dbSNP:rs104893769).
{ECO:0000269|PubMed:1391967,
ECO:0000269|PubMed:1897520}.
/FTId=VAR_004767.
VARIANT 23 23 P -> H (in RP4; most common variant;
impairs protein folding; leads to
interaction with EDEM1 followed by
degradation by the ERAD system;
dbSNP:rs104893768).
{ECO:0000269|PubMed:12566452,
ECO:0000269|PubMed:1897520,
ECO:0000269|PubMed:19934218,
ECO:0000269|PubMed:2137202,
ECO:0000269|PubMed:2215617}.
/FTId=VAR_004768.
VARIANT 23 23 P -> L (in RP4).
/FTId=VAR_004769.
VARIANT 28 28 Q -> H (in RP4).
/FTId=VAR_004770.
VARIANT 40 40 L -> R (in RP4).
{ECO:0000269|PubMed:8081400}.
/FTId=VAR_004771.
VARIANT 44 44 M -> T (in RP4; dbSNP:rs774336493).
{ECO:0000269|PubMed:8076945}.
/FTId=VAR_004772.
VARIANT 45 45 F -> L (in RP4; dbSNP:rs104893770).
/FTId=VAR_004773.
VARIANT 46 46 L -> R (in RP4).
/FTId=VAR_004774.
VARIANT 51 51 G -> A (in dbSNP:rs149079952).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004775.
VARIANT 51 51 G -> R (in RP4; dbSNP:rs104893792).
/FTId=VAR_004776.
VARIANT 51 51 G -> V (in RP4).
/FTId=VAR_004777.
VARIANT 53 53 P -> R (in RP4; dbSNP:rs28933395).
/FTId=VAR_004778.
VARIANT 58 58 T -> R (in RP4; dbSNP:rs28933394).
{ECO:0000269|PubMed:1897520,
ECO:0000269|PubMed:2215617}.
/FTId=VAR_004779.
VARIANT 68 71 Missing (in RP4).
/FTId=VAR_004780.
VARIANT 87 87 V -> D (in RP4; dbSNP:rs104893771).
/FTId=VAR_004781.
VARIANT 89 89 G -> D (in RP4; dbSNP:rs104893772).
/FTId=VAR_004782.
VARIANT 90 90 G -> D (in CSNBAD1; constitutive activity
in the absence of bound retinal;
dbSNP:rs104893790).
{ECO:0000269|PubMed:7846071,
ECO:0000269|PubMed:8107847}.
/FTId=VAR_004783.
VARIANT 94 94 T -> I (in CSNBAD1; dbSNP:rs104893796).
{ECO:0000269|PubMed:9888392}.
/FTId=VAR_004784.
VARIANT 104 104 V -> I (found in patients with pathologic
myopia; unknown pathological
significance; dbSNP:rs144317206).
{ECO:0000269|PubMed:28837730,
ECO:0000269|PubMed:8317502}.
/FTId=VAR_004785.
VARIANT 106 106 G -> R (in RP4; dbSNP:rs104893773).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004786.
VARIANT 106 106 G -> W (in RP4; dbSNP:rs104893773).
/FTId=VAR_004787.
VARIANT 109 109 G -> R (in RP4).
{ECO:0000269|PubMed:9452035}.
/FTId=VAR_004788.
VARIANT 110 110 C -> F (in RP4).
{ECO:0000269|PubMed:7981701}.
/FTId=VAR_004789.
VARIANT 110 110 C -> Y (in RP4; dbSNP:rs104893787).
/FTId=VAR_004790.
VARIANT 114 114 G -> D (in RP4; dbSNP:rs104893788).
/FTId=VAR_004791.
VARIANT 125 125 L -> R (in RP4).
/FTId=VAR_004792.
VARIANT 127 127 S -> F (in RP4).
{ECO:0000269|PubMed:7987331}.
/FTId=VAR_004793.
VARIANT 131 131 L -> P (in RP4).
{ECO:0000269|PubMed:7981701,
ECO:0000269|PubMed:7987331}.
/FTId=VAR_004794.
VARIANT 135 135 R -> G (in RP4).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004795.
VARIANT 135 135 R -> L (in RP4; dbSNP:rs104893774).
/FTId=VAR_004796.
VARIANT 135 135 R -> W (in RP4; dbSNP:rs104893775).
{ECO:0000269|PubMed:22334370,
ECO:0000269|PubMed:8554077}.
/FTId=VAR_004797.
VARIANT 140 140 C -> S (in RP4).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004798.
VARIANT 150 150 E -> K (in RP4; autosomal recessive;
dbSNP:rs104893791).
{ECO:0000269|PubMed:19960070,
ECO:0000269|PubMed:7987385}.
/FTId=VAR_004799.
VARIANT 164 164 A -> E (in RP4; dbSNP:rs104893793).
/FTId=VAR_004800.
VARIANT 164 164 A -> V (in RP4; dbSNP:rs104893793).
{ECO:0000269|PubMed:7981701}.
/FTId=VAR_004801.
VARIANT 167 167 C -> R (in RP4).
/FTId=VAR_004802.
VARIANT 171 171 P -> L (in RP4).
/FTId=VAR_004803.
VARIANT 171 171 P -> Q (in RP4).
{ECO:0000269|PubMed:7987326}.
/FTId=VAR_004804.
VARIANT 171 171 P -> S (in RP4; dbSNP:rs104893794).
/FTId=VAR_004805.
VARIANT 178 178 Y -> C (in RP4; dbSNP:rs104893776).
/FTId=VAR_004806.
VARIANT 178 178 Y -> N (in RP4).
{ECO:0000269|PubMed:7987331}.
/FTId=VAR_004807.
VARIANT 180 180 P -> S (in RP4).
{ECO:0000269|PubMed:22334370}.
/FTId=VAR_068359.
VARIANT 181 181 E -> K (in RP4; dbSNP:rs775557680).
/FTId=VAR_004808.
VARIANT 182 182 G -> S (in RP4; dbSNP:rs104893780).
{ECO:0000269|PubMed:1897520}.
/FTId=VAR_004809.
VARIANT 186 186 S -> P (in RP4).
/FTId=VAR_004810.
VARIANT 188 188 G -> E (in RP4).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004811.
VARIANT 188 188 G -> R (in RP4; dbSNP:rs527236100).
/FTId=VAR_004812.
VARIANT 190 190 D -> G (in RP4; dbSNP:rs104893777).
/FTId=VAR_004814.
VARIANT 190 190 D -> N (in RP4; dbSNP:rs104893779).
/FTId=VAR_004813.
VARIANT 190 190 D -> Y (in RP4; dbSNP:rs104893779).
/FTId=VAR_004815.
VARIANT 207 207 M -> R (in RP4; dbSNP:rs104893782).
{ECO:0000269|PubMed:1302614}.
/FTId=VAR_004816.
VARIANT 209 209 V -> M (found in a patient with retinitis
pigmentosa; unknown pathological
significance; dbSNP:rs567288669).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004817.
VARIANT 211 211 H -> P (in RP4; dbSNP:rs28933993).
/FTId=VAR_004818.
VARIANT 211 211 H -> R (in RP4).
{ECO:0000269|PubMed:8317502}.
/FTId=VAR_004819.
VARIANT 214 214 I -> N (in RP4).
{ECO:0000269|PubMed:22334370}.
/FTId=VAR_068360.
VARIANT 216 216 M -> K (in RP4).
{ECO:0000269|PubMed:8081400}.
/FTId=VAR_004820.
VARIANT 220 220 F -> C (in RP4; dbSNP:rs766161322).
/FTId=VAR_004821.
VARIANT 222 222 C -> R (in RP4).
/FTId=VAR_004822.
VARIANT 255 255 Missing (in RP4).
{ECO:0000269|PubMed:1985460}.
/FTId=VAR_004823.
VARIANT 264 264 Missing (in RP4).
/FTId=VAR_004824.
VARIANT 267 267 P -> L (in RP4; dbSNP:rs104893781).
{ECO:0000269|PubMed:1897520}.
/FTId=VAR_004825.
VARIANT 267 267 P -> R (in RP4).
{ECO:0000269|PubMed:7987331}.
/FTId=VAR_004826.
VARIANT 292 292 A -> E (in CSNBAD1; dbSNP:rs104893789).
{ECO:0000269|PubMed:8358437}.
/FTId=VAR_004827.
VARIANT 296 296 K -> E (in RP4; dbSNP:rs29001653).
/FTId=VAR_004828.
VARIANT 297 297 S -> R (in RP4).
{ECO:0000269|PubMed:7987331}.
/FTId=VAR_004829.
VARIANT 342 342 T -> M (in RP4; dbSNP:rs183318466).
/FTId=VAR_004830.
VARIANT 345 345 V -> L (in RP4; dbSNP:rs104893795).
{ECO:0000269|PubMed:8045708}.
/FTId=VAR_004831.
VARIANT 345 345 V -> M (in RP4; dbSNP:rs104893795).
/FTId=VAR_004832.
VARIANT 347 347 P -> A (in RP4).
{ECO:0000269|PubMed:7633434}.
/FTId=VAR_004833.
VARIANT 347 347 P -> L (in RP4; common variant;
dbSNP:rs29001566).
{ECO:0000269|PubMed:1391967,
ECO:0000269|PubMed:2215617}.
/FTId=VAR_004834.
VARIANT 347 347 P -> Q (in RP4; dbSNP:rs29001566).
/FTId=VAR_004835.
VARIANT 347 347 P -> R (in RP4; dbSNP:rs29001566).
{ECO:0000269|PubMed:1840561}.
/FTId=VAR_004836.
VARIANT 347 347 P -> S (in RP4; dbSNP:rs29001637).
{ECO:0000269|PubMed:2215617}.
/FTId=VAR_004837.
MUTAGEN 113 113 E->Q: Induces a conformation change that
promotes interaction with GRK1 and SAG;
when associated with Y-257.
{ECO:0000269|PubMed:26200343}.
MUTAGEN 257 257 M->Y: Induces a conformation change that
promotes interaction with GRK1 and SAG;
when associated with Q-113.
{ECO:0000269|PubMed:26200343,
ECO:0000269|PubMed:28524165}.
MUTAGEN 336 340 TVSKT->AVAKA: Loss of phosphorylation
sites and decreased interaction with SAG.
{ECO:0000269|PubMed:28753425}.
MUTAGEN 336 338 TVS->AVA: Loss of phosphorylation sites
and decreased interaction with SAG; when
associated with A-343.
{ECO:0000269|PubMed:28753425}.
MUTAGEN 343 343 S->A: Loss of phosphorylation sites and
decreased interaction with SAG; when
associated with 336-A--A-338.
{ECO:0000269|PubMed:28753425}.
STRAND 2 5 {ECO:0000244|PDB:5W0P}.
STRAND 10 13 {ECO:0000244|PDB:5W0P}.
STRAND 16 18 {ECO:0000244|PDB:5W0P}.
TURN 23 25 {ECO:0000244|PDB:5W0P}.
TURN 29 31 {ECO:0000244|PDB:4ZWJ}.
HELIX 35 64 {ECO:0000244|PDB:5W0P}.
HELIX 66 68 {ECO:0000244|PDB:5W0P}.
TURN 71 73 {ECO:0000244|PDB:5W0P}.
HELIX 74 88 {ECO:0000244|PDB:5W0P}.
HELIX 90 100 {ECO:0000244|PDB:5W0P}.
HELIX 106 140 {ECO:0000244|PDB:5W0P}.
HELIX 143 147 {ECO:0000244|PDB:5W0P}.
HELIX 150 168 {ECO:0000244|PDB:5W0P}.
HELIX 170 173 {ECO:0000244|PDB:5W0P}.
STRAND 174 176 {ECO:0000244|PDB:4ZWJ}.
STRAND 178 181 {ECO:0000244|PDB:5W0P}.
TURN 182 185 {ECO:0000244|PDB:5W0P}.
STRAND 186 189 {ECO:0000244|PDB:5W0P}.
STRAND 191 193 {ECO:0000244|PDB:5W0P}.
TURN 196 199 {ECO:0000244|PDB:5W0P}.
HELIX 200 209 {ECO:0000244|PDB:5W0P}.
TURN 210 212 {ECO:0000244|PDB:5W0P}.
HELIX 213 236 {ECO:0000244|PDB:5W0P}.
HELIX 241 277 {ECO:0000244|PDB:5W0P}.
HELIX 285 306 {ECO:0000244|PDB:5W0P}.
TURN 307 309 {ECO:0000244|PDB:5W0P}.
HELIX 311 321 {ECO:0000244|PDB:5W0P}.
TURN 322 324 {ECO:0000244|PDB:4ZWJ}.
TURN 331 333 {ECO:0000244|PDB:5W0P}.
STRAND 339 341 {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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