GP143_HUMAN
ID GP143_HUMAN Reviewed; 404 AA.
AC P51810; Q6NTI7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=G-protein coupled receptor 143;
DE AltName: Full=Ocular albinism type 1 protein;
GN Name=GPR143; Synonyms=OA1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=7647783; DOI=10.1038/ng0595-13;
RA Bassi M.T., Schiaffino M.V., Renieri A., de Nigris F., Galli L.,
RA Bruttini M., Gebbia M.A.B., Bergen A.A.B., Lewis R., Ballabio A.;
RT "Cloning of the gene for ocular albinism type 1 from the distal short arm
RT of the X chromosome.";
RL Nat. Genet. 10:13-19(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 REVIEW ON OA1 VARIANTS.
RX PubMed=10094567;
RX DOI=10.1002/(sici)1098-1004(1999)13:2<99::aid-humu2>3.0.co;2-c;
RA Oetting W.S., King R.A.;
RT "Molecular basis of albinism: mutations and polymorphisms of pigmentation
RT genes associated with albinism.";
RL Hum. Mutat. 13:99-115(1999).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Melanocyte;
RX PubMed=10471510; DOI=10.1038/12715;
RA Schiaffino M.V., d'Addio M., Alloni A., Baschirotto C., Valetti C.,
RA Cortese K., Puri C., Bassi M.T., Colla C., De Luca M., Tacchetti C.,
RA Ballabio A.;
RT "Ocular albinism: evidence for a defect in an intracellular signal
RT transduction system.";
RL Nat. Genet. 23:108-112(1999).
RN [7]
RP GLYCOSYLATION, AND CHARACTERIZATION OF VARIANTS OA1 CYS-5; ASP-35; ASN-78;
RP ASP-84; SER-116; GLU-118; ARG-133; ASP-173; ASN-261; THR-290 DEL AND
RP GLY-292.
RX PubMed=11115845; DOI=10.1093/hmg/9.20.3011;
RA d'Addio M., Pizzigoni A., Bassi M.T., Baschirotto C., Valetti C.,
RA Incerti B., Clementi M., De Luca M., Ballabio A., Schiaffino M.V.;
RT "Defective intracellular transport and processing of OA1 is a major cause
RT of ocular albinism type 1.";
RL Hum. Mol. Genet. 9:3011-3018(2000).
RN [8]
RP REVIEW ON OA1 VARIANTS.
RX PubMed=11793467; DOI=10.1002/humu.10034;
RA Oetting W.S.;
RT "New insights into ocular albinism type 1 (OA1): mutations and
RT polymorphisms of the OA1 gene.";
RL Hum. Mutat. 19:85-92(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [10]
RP SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS OA1 VAL-229; LYS-232;
RP LYS-235 AND VAL-244, AND MUTAGENESIS OF 224-LEU-LEU-225 AND
RP 329-LEU-LEU-330.
RX PubMed=16621890; DOI=10.1242/jcs.02930;
RA Piccirillo R., Palmisano I., Innamorati G., Bagnato P., Altimare D.,
RA Schiaffino M.V.;
RT "An unconventional dileucine-based motif and a novel cytosolic motif are
RT required for the lysosomal and melanosomal targeting of OA1.";
RL J. Cell Sci. 119:2003-2014(2006).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
RP FUNCTION, INTERACTION WITH ARRB1 AND ARRB1, PHOSPHORYLATION,
RP CHARACTERIZATION OF VARIANT OA1 GLY-116, AND SUBCELLULAR LOCATION.
RX PubMed=16524428; DOI=10.1111/j.1600-0749.2006.00292.x;
RA Innamorati G., Piccirillo R., Bagnato P., Palmisano I., Schiaffino M.V.;
RT "The melanosomal/lysosomal protein OA1 has properties of a G protein-
RT coupled receptor.";
RL Pigment Cell Res. 19:125-135(2006).
RN [13]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT OA1 LYS-232.
RX PubMed=18697795; DOI=10.1093/hmg/ddn241;
RA Palmisano I., Bagnato P., Palmigiano A., Innamorati G., Rotondo G.,
RA Altimare D., Venturi C., Sviderskaya E.V., Piccirillo R., Coppola M.,
RA Marigo V., Incerti B., Ballabio A., Surace E.M., Tacchetti C.,
RA Bennett D.C., Schiaffino M.V.;
RT "The ocular albinism type 1 protein, an intracellular G protein-coupled
RT receptor, regulates melanosome transport in pigment cells.";
RL Hum. Mol. Genet. 17:3487-3501(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18828673; DOI=10.1371/journal.pbio.0060236;
RA Lopez V.M., Decatur C.L., Stamer W.D., Lynch R.M., McKay B.S.;
RT "L-DOPA is an endogenous ligand for OA1.";
RL PLoS Biol. 6:E236-E236(2008).
RN [15]
RP FUNCTION, AND INTERACTION WITH MLANA.
RX PubMed=19717472; DOI=10.1093/hmg/ddp415;
RA Giordano F., Bonetti C., Surace E.M., Marigo V., Raposo G.;
RT "The ocular albinism type 1 (OA1) G-protein-coupled receptor functions with
RT MART-1 at early stages of melanogenesis to control melanosome identity and
RT composition.";
RL Hum. Mol. Genet. 18:4530-4545(2009).
RN [16]
RP VARIANTS OA1 ASP-35; ASP-84; ASP-173; THR-290 DEL AND GLY-292.
RX PubMed=8634705; DOI=10.1093/hmg/4.12.2319;
RA Schiaffino M.V., Bassi M.T., Balli L., Renieri A., Bruttini M.,
RA de Nigris F., Bergen A.A.B., Charles S.J., Yates J.R.W., Meindl A.,
RA Lewis R.A., King R.A., Ballabio A.;
RT "Analysis of the OA1 gene reveals mutations in only one-third of patients
RT with X-linked ocular albinism.";
RL Hum. Mol. Genet. 4:2319-2325(1995).
RN [17]
RP VARIANTS OA1 ARG-84; ARG-116; GLU-118; ARG-133; VAL-138; ASN-152; LYS-232
RP AND LYS-235.
RX PubMed=9529334; DOI=10.1086/301776;
RA Schnur R.E., Gao M., Wick P.A., Keller M., Benke P.J., Edwards M.J.,
RA Grix A.W., Hockey A., Jung J.H., Kidd K.K., Kistenmacher M., Levin A.V.,
RA Lewis R.A., Musarella M.A., Nowakowski R.W., Orlow S.J., Pagon R.S.,
RA Pillers D.-A.M., Punnett H.H., Quinn G.E., Tezcan K., Wagstaff J.,
RA Weleber R.G.;
RT "OA1 mutations and deletions in X-linked ocular albinism.";
RL Am. J. Hum. Genet. 62:800-809(1998).
RN [18]
RP VARIANTS OA1 ASP-35; ARG-39; VAL-78; ARG-133 AND LYS-233.
RX PubMed=9887374; DOI=10.1038/sj.ejhg.5200226;
RA Rosenberg T., Schwartz M.;
RT "X-linked ocular albinism: prevalence and mutations -- a national study.";
RL Eur. J. Hum. Genet. 6:570-577(1998).
RN [19]
RP VARIANTS OA1 CYS-5; ASN-78; SER-116; GLU-118; ARG-124; VAL-229; VAL-244;
RP ASN-261; GLY-271 AND CYS-292.
RX PubMed=11214907; DOI=10.1007/s004390000440;
RA Bassi M.T., Bergen A.A., Bitoun P., Charles S.J., Clementi M., Gosselin R.,
RA Hurst J., Lewis R.A., Lorenz B., Meitinger T., Messiaen L., Ramesar R.S.,
RA Ballabio A., Schiaffino M.V.;
RT "Diverse prevalence of large deletions within the OA1 gene in ocular
RT albinism type 1 patients from Europe and North America.";
RL Hum. Genet. 108:51-54(2001).
RN [20]
RP VARIANTS OA1 VAL-81; TRP-116; PRO-134 AND ASN-166.
RX PubMed=16646960; DOI=10.1186/1471-2350-7-41;
RA Mayeur H., Roche O., Vetu C., Jaliffa C., Marchant D., Dollfus H.,
RA Bonneau D., Munier F.L., Schorderet D.F., Levin A.V., Heon E.,
RA Sutherland J., Lacombe D., Said E., Mezer E., Kaplan J., Dufier J.L.,
RA Marsac C., Menasche M., Abitbol M.;
RT "Eight previously unidentified mutations found in the OA1 ocular albinism
RT gene.";
RL BMC Med. Genet. 7:41-41(2006).
RN [21]
RP VARIANTS OA1 ARG-132; LYS-185; TRP-186 AND PRO-186.
RX PubMed=17822861; DOI=10.1016/j.gene.2007.07.020;
RA Roma C., Ferrante P., Guardiola O., Ballabio A., Zollo M.;
RT "New mutations identified in the ocular albinism type 1 gene.";
RL Gene 402:20-27(2007).
RN [22]
RP VARIANT NYS6 PHE-89.
RX PubMed=17516023; DOI=10.1007/s10038-007-0152-3;
RA Liu J.Y., Ren X., Yang X., Guo T., Yao Q., Li L., Dai X., Zhang M.,
RA Wang L., Liu M., Wang Q.K.;
RT "Identification of a novel GPR143 mutation in a large Chinese family with
RT congenital nystagmus as the most prominent and consistent manifestation.";
RL J. Hum. Genet. 52:565-570(2007).
RN [23]
RP VARIANT OA1 GLY-116.
RX PubMed=17960122;
RA Iannaccone A., Gallaher K.T., Buchholz J., Jennings B.J., Neitz M.,
RA Sidjanin D.J.;
RT "Identification of two novel mutations in families with X-linked ocular
RT albinism.";
RL Mol. Vis. 13:1856-1861(2007).
RN [24]
RP VARIANTS OA1 LEU-80 DEL AND GLU-118.
RX PubMed=18978956;
RA Fang S., Guo X., Jia X., Xiao X., Li S., Zhang Q.;
RT "Novel GPR143 mutations and clinical characteristics in six Chinese
RT families with X-linked ocular albinism.";
RL Mol. Vis. 14:1974-1982(2008).
CC -!- FUNCTION: Receptor for tyrosine, L-DOPA and dopamine. After binding to
CC L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases
CC secretion of the neurotrophic factor SERPINF1 and relocalizes beta
CC arrestin at the plasma membrane; this ligand-dependent signaling occurs
CC through a G(q)-mediated pathway in melanocytic cells. Its activity is
CC mediated by G proteins which activate the phosphoinositide signaling
CC pathway. Also plays a role as an intracellular G protein-coupled
CC receptor involved in melanosome biogenesis, organization and transport.
CC {ECO:0000269|PubMed:10471510, ECO:0000269|PubMed:16524428,
CC ECO:0000269|PubMed:18697795, ECO:0000269|PubMed:18828673,
CC ECO:0000269|PubMed:19717472}.
CC -!- SUBUNIT: Interacts with heterotrimeric G(i) proteins. Interacts with
CC ARRB1 and ARRB2. Interacts with MLANA. {ECO:0000269|PubMed:10471510,
CC ECO:0000269|PubMed:16524428, ECO:0000269|PubMed:19717472}.
CC -!- INTERACTION:
CC P51810; P14679: TYR; NbExp=4; IntAct=EBI-2509708, EBI-25397340;
CC -!- SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:10471510,
CC ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:16524428,
CC ECO:0000269|PubMed:16621890, ECO:0000269|PubMed:17081065}; Multi-pass
CC membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:16524428, ECO:0000269|PubMed:16621890}; Multi-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:18828673}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Distributed throughout the endo-melanosomal system
CC but most of endogenous protein is localized in unpigmented stage II
CC melanosomes. Its expression on the apical cell membrane is sensitive to
CC tyrosine (PubMed:18828673). {ECO:0000269|PubMed:18828673}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the retina, including
CC the retinal pigment epithelium (RPE), and in melanocytes. Weak
CC expression is observed in brain and adrenal gland.
CC {ECO:0000269|PubMed:18828673, ECO:0000269|PubMed:7647783}.
CC -!- DOMAIN: The cytoplasmic domain 3 and the C-terminus tail domain contain
CC the lysosomal sorting signals and are necessary and sufficient for
CC intracellular retention and delivery to lysosomal and melanosomal,
CC respectively in melanocytic and non-melanocytic cells.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11115845}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16524428}.
CC -!- DISEASE: Albinism ocular 1 (OA1) [MIM:300500]: Form of albinism
CC affecting only the eye. Pigment of the hair and skin is normal or only
CC slightly diluted. Eyes may be severely affected with photophobia and
CC reduced visual acuity. Nystagmus or strabismus are often associated.
CC The irides and fundus are depigmented. {ECO:0000269|PubMed:11115845,
CC ECO:0000269|PubMed:11214907, ECO:0000269|PubMed:16524428,
CC ECO:0000269|PubMed:16621890, ECO:0000269|PubMed:16646960,
CC ECO:0000269|PubMed:17822861, ECO:0000269|PubMed:17960122,
CC ECO:0000269|PubMed:18697795, ECO:0000269|PubMed:18978956,
CC ECO:0000269|PubMed:8634705, ECO:0000269|PubMed:9529334,
CC ECO:0000269|PubMed:9887374}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Nystagmus congenital X-linked 6 (NYS6) [MIM:300814]: A
CC condition defined as conjugated, spontaneous and involuntary ocular
CC oscillations that appear at birth or during the first three months of
CC life. Other associated features may include mildly decreased visual
CC acuity, strabismus, astigmatism, and occasionally head nodding.
CC {ECO:0000269|PubMed:17516023}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor OA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68977.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA88742.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW98773.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the OA1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/oa1mut.htm";
CC -!- WEB RESOURCE: Name=Albinism database (ADB); Note=GPR143 mutations;
CC URL="http://www.ifpcs.org/albinism/oa1mut.html";
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DR EMBL; Z48804; CAA88742.1; ALT_INIT; mRNA.
DR EMBL; AC003036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98773.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC068977; AAH68977.1; ALT_INIT; mRNA.
DR CCDS; CCDS14134.2; -.
DR RefSeq; NP_000264.2; NM_000273.2.
DR AlphaFoldDB; P51810; -.
DR SMR; P51810; -.
DR BioGRID; 110989; 2.
DR DIP; DIP-53284N; -.
DR IntAct; P51810; 4.
DR STRING; 9606.ENSP00000417161; -.
DR ChEMBL; CHEMBL4523867; -.
DR TCDB; 9.A.14.20.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P51810; 1 site.
DR iPTMnet; P51810; -.
DR PhosphoSitePlus; P51810; -.
DR BioMuta; GPR143; -.
DR DMDM; 3219999; -.
DR EPD; P51810; -.
DR MassIVE; P51810; -.
DR PaxDb; P51810; -.
DR PeptideAtlas; P51810; -.
DR PRIDE; P51810; -.
DR ProteomicsDB; 56406; -.
DR Antibodypedia; 8143; 166 antibodies from 28 providers.
DR DNASU; 4935; -.
DR Ensembl; ENST00000467482.6; ENSP00000417161.1; ENSG00000101850.13.
DR GeneID; 4935; -.
DR KEGG; hsa:4935; -.
DR MANE-Select; ENST00000467482.6; ENSP00000417161.1; NM_000273.3; NP_000264.2.
DR UCSC; uc004cst.3; human.
DR CTD; 4935; -.
DR DisGeNET; 4935; -.
DR GeneCards; GPR143; -.
DR HGNC; HGNC:20145; GPR143.
DR HPA; ENSG00000101850; Tissue enhanced (brain, choroid plexus).
DR MalaCards; GPR143; -.
DR MIM; 300500; phenotype.
DR MIM; 300808; gene.
DR MIM; 300814; phenotype.
DR neXtProt; NX_P51810; -.
DR OpenTargets; ENSG00000101850; -.
DR Orphanet; 651; NON RARE IN EUROPE: Idiopathic infantile nystagmus.
DR Orphanet; 54; X-linked recessive ocular albinism.
DR PharmGKB; PA31872; -.
DR VEuPathDB; HostDB:ENSG00000101850; -.
DR eggNOG; ENOG502QQII; Eukaryota.
DR GeneTree; ENSGT00390000016722; -.
DR HOGENOM; CLU_053538_1_1_1; -.
DR InParanoid; P51810; -.
DR OMA; DIWPAAF; -.
DR OrthoDB; 1476889at2759; -.
DR PhylomeDB; P51810; -.
DR TreeFam; TF324849; -.
DR PathwayCommons; P51810; -.
DR Reactome; R-HSA-375280; Amine ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P51810; -.
DR BioGRID-ORCS; 4935; 7 hits in 693 CRISPR screens.
DR ChiTaRS; GPR143; human.
DR GeneWiki; GPR143; -.
DR GenomeRNAi; 4935; -.
DR Pharos; P51810; Tbio.
DR PRO; PR:P51810; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51810; protein.
DR Bgee; ENSG00000101850; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; P51810; baseline and differential.
DR Genevisible; P51810; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035240; F:dopamine binding; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0072544; F:L-DOPA binding; IDA:UniProtKB.
DR GO; GO:0035643; F:L-DOPA receptor activity; IDA:UniProtKB.
DR GO; GO:0072545; F:tyrosine binding; IDA:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:UniProtKB.
DR GO; GO:0006726; P:eye pigment biosynthetic process; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0032400; P:melanosome localization; IDA:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:1903056; P:regulation of melanosome organization; IEA:Ensembl.
DR GO; GO:1902908; P:regulation of melanosome transport; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR InterPro; IPR001414; GPR143.
DR PANTHER; PTHR15177; PTHR15177; 1.
DR Pfam; PF02101; Ocular_alb; 1.
DR PRINTS; PR00965; OCULARALBNSM.
PE 1: Evidence at protein level;
KW Albinism; Cell membrane; Disease variant; G-protein coupled receptor;
KW Glycoprotein; Lysosome; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..404
FT /note="G-protein coupled receptor 143"
FT /id="PRO_0000195086"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 221..238
FT /note="Necessary for its G protein-activation ability and
FT normal distribution of melanosomes"
FT REGION 338..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..231
FT /note="lysosomal/melanosomal membrane localization signal"
FT MOTIF 329..330
FT /note="lysosomal/melanosomal membrane localization signal"
FT COMPBIAS 355..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="R -> C (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum; lacks G
FT protein-activation abilities; dbSNP:rs62635289)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:11214907"
FT /id="VAR_018130"
FT VARIANT 35
FT /note="G -> D (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635018)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:8634705, ECO:0000269|PubMed:9887374"
FT /id="VAR_005507"
FT VARIANT 39
FT /note="L -> R (in OA1; dbSNP:rs62635019)"
FT /evidence="ECO:0000269|PubMed:9887374"
FT /id="VAR_018131"
FT VARIANT 78
FT /note="D -> N (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635024)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:11214907"
FT /id="VAR_018132"
FT VARIANT 78
FT /note="D -> V (in OA1; dbSNP:rs62635025)"
FT /evidence="ECO:0000269|PubMed:9887374"
FT /id="VAR_018133"
FT VARIANT 80
FT /note="Missing (in OA1)"
FT /evidence="ECO:0000269|PubMed:18978956"
FT /id="VAR_063264"
FT VARIANT 81
FT /note="G -> V (in OA1)"
FT /evidence="ECO:0000269|PubMed:16646960"
FT /id="VAR_063265"
FT VARIANT 84
FT /note="G -> D (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635027)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:8634705"
FT /id="VAR_005508"
FT VARIANT 84
FT /note="G -> R (in OA1; dbSNP:rs62635026)"
FT /evidence="ECO:0000269|PubMed:9529334"
FT /id="VAR_005509"
FT VARIANT 89
FT /note="S -> F (in NYS6; dbSNP:rs137852298)"
FT /evidence="ECO:0000269|PubMed:17516023"
FT /id="VAR_063266"
FT VARIANT 116
FT /note="C -> G (in OA1)"
FT /evidence="ECO:0000269|PubMed:16524428,
FT ECO:0000269|PubMed:17960122"
FT /id="VAR_063267"
FT VARIANT 116
FT /note="C -> R (in OA1; dbSNP:rs62635030)"
FT /evidence="ECO:0000269|PubMed:9529334"
FT /id="VAR_005510"
FT VARIANT 116
FT /note="C -> S (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635029)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:11214907"
FT /id="VAR_018134"
FT VARIANT 116
FT /note="C -> W (in OA1)"
FT /evidence="ECO:0000269|PubMed:16646960"
FT /id="VAR_063268"
FT VARIANT 118
FT /note="G -> E (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635031)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:11214907, ECO:0000269|PubMed:18978956,
FT ECO:0000269|PubMed:9529334"
FT /id="VAR_005511"
FT VARIANT 124
FT /note="Q -> R (in OA1; dbSNP:rs62635032)"
FT /evidence="ECO:0000269|PubMed:11214907"
FT /id="VAR_018135"
FT VARIANT 132
FT /note="W -> R (in OA1)"
FT /evidence="ECO:0000269|PubMed:17822861"
FT /id="VAR_063269"
FT VARIANT 133
FT /note="W -> R (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs137852296)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:9529334, ECO:0000269|PubMed:9887374"
FT /id="VAR_005513"
FT VARIANT 134
FT /note="L -> P (in OA1)"
FT /evidence="ECO:0000269|PubMed:16646960"
FT /id="VAR_063270"
FT VARIANT 138
FT /note="A -> V (in OA1; dbSNP:rs62635762)"
FT /evidence="ECO:0000269|PubMed:9529334"
FT /id="VAR_005514"
FT VARIANT 152
FT /note="S -> N (in OA1; dbSNP:rs58933950)"
FT /evidence="ECO:0000269|PubMed:9529334"
FT /id="VAR_005515"
FT VARIANT 166
FT /note="T -> N (in OA1)"
FT /evidence="ECO:0000269|PubMed:16646960"
FT /id="VAR_063271"
FT VARIANT 173
FT /note="A -> D (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635035)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:8634705"
FT /id="VAR_005516"
FT VARIANT 185
FT /note="E -> K (in OA1)"
FT /evidence="ECO:0000269|PubMed:17822861"
FT /id="VAR_063272"
FT VARIANT 186
FT /note="R -> P (in OA1)"
FT /evidence="ECO:0000269|PubMed:17822861"
FT /id="VAR_063273"
FT VARIANT 186
FT /note="R -> W (in OA1; dbSNP:rs199899645)"
FT /evidence="ECO:0000269|PubMed:17822861"
FT /id="VAR_063274"
FT VARIANT 229
FT /note="G -> V (in OA1; not delivered at the cell surface of
FT melanocytic and non-melanocytic cells; dbSNP:rs62635037)"
FT /evidence="ECO:0000269|PubMed:11214907,
FT ECO:0000269|PubMed:16621890"
FT /id="VAR_018136"
FT VARIANT 232
FT /note="T -> K (in OA1; abnormal distribution of
FT melanosomes; Not delivered at the cell surface of
FT melanocytic and non-melanocytic cells; dbSNP:rs137852297)"
FT /evidence="ECO:0000269|PubMed:16621890,
FT ECO:0000269|PubMed:18697795, ECO:0000269|PubMed:9529334"
FT /id="VAR_005517"
FT VARIANT 233
FT /note="E -> K (in OA1; dbSNP:rs62635038)"
FT /evidence="ECO:0000269|PubMed:9887374"
FT /id="VAR_018137"
FT VARIANT 235
FT /note="E -> K (in OA1; not delivered at the cell surface of
FT melanocytic and non-melanocytic cells)"
FT /evidence="ECO:0000269|PubMed:16621890,
FT ECO:0000269|PubMed:9529334"
FT /id="VAR_005518"
FT VARIANT 244
FT /note="I -> V (in OA1; not delivered at the cell surface of
FT melanocytic and non-melanocytic cells; dbSNP:rs62635040)"
FT /evidence="ECO:0000269|PubMed:11214907,
FT ECO:0000269|PubMed:16621890"
FT /id="VAR_018138"
FT VARIANT 261
FT /note="I -> N (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:11214907"
FT /id="VAR_018139"
FT VARIANT 271
FT /note="E -> G (in OA1; dbSNP:rs62635043)"
FT /evidence="ECO:0000269|PubMed:11214907"
FT /id="VAR_018140"
FT VARIANT 290
FT /note="Missing (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635044)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:8634705"
FT /id="VAR_005519"
FT VARIANT 292
FT /note="W -> C (in OA1; dbSNP:rs62635046)"
FT /evidence="ECO:0000269|PubMed:11214907"
FT /id="VAR_018141"
FT VARIANT 292
FT /note="W -> G (in OA1; results in altered glycosylation
FT pattern and subcellular localization consistent with
FT protein retention in the endoplasmic reticulum;
FT dbSNP:rs62635045)"
FT /evidence="ECO:0000269|PubMed:11115845,
FT ECO:0000269|PubMed:8634705"
FT /id="VAR_005520"
FT MUTAGEN 223..224
FT /note="LL->AA: Delivered to both at the cell surface and in
FT vesicles of melanocytic and non-melanocytic cells. Strongly
FT delivered at the cell surface of melanocytic and non-
FT melanocytic cells; when associated with 329-A-A-330."
FT MUTAGEN 329..330
FT /note="WE->AA: Mostly delivered at the cell surface of
FT melanocytic and non-melanocytic cells. Strongly delivered
FT at the cell surface of melanocytic and non-melanocytic
FT cells; when associated with 224-A-A-225."
FT /evidence="ECO:0000269|PubMed:16621890"
SQ SEQUENCE 404 AA; 43878 MW; 20DEB20E80CC0E1D CRC64;
MASPRLGTFC CPTRDAATQL VLSFQPRAFH ALCLGSGGLR LALGLLQLLP GRRPAGPGSP
ATSPPASVRI LRAAAACDLL GCLGMVIRST VWLGFPNFVD SVSDMNHTEI WPAAFCVGSA
MWIQLLYSAC FWWLFCYAVD AYLVIRRSAG LSTILLYHIM AWGLATLLCV EGAAMLYYPS
VSRCERGLDH AIPHYVTMYL PLLLVLVANP ILFQKTVTAV ASLLKGRQGI YTENERRMGA
VIKIRFFKIM LVLIICWLSN IINESLLFYL EMQTDINGGS LKPVRTAAKT TWFIMGILNP
AQGFLLSLAF YGWTGCSLGF QSPRKEIQWE SLTTSAAEGA HPSPLMPHEN PASGKVSQVG
GQTSDEALSM LSEGSDASTI EIHTASESCN KNEGDPALPT HGDL
