P51810 (GP143_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
G-protein coupled receptor 143

Alternative name(s):
Ocular albinism type 1 protein

Gene names

Name:	GPR143
Synonyms:	OA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca2+ influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand-dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Plays also a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport. Ref.6 Ref.12 Ref.13 Ref.14 Ref.15
Subunit structure	Interacts with heterotrimeric G(i) proteins. Interacts with ARRB1 and ARRB2. Interacts with MLANA. Ref.6 Ref.12 Ref.15
Subcellular location	Golgi apparatus. Melanosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note: Distributed throughout the endo-melanosomal system but most of endogenous protein is localized in unpigmented stage II melanosomes. Its expression on the apical cell membrane is sensitive to tyrosine. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Tissue specificity	Expressed at high levels in the retina, including the retinal pigment epithelium (RPE), and in melanocytes. Weak expression is observed in brain and adrenal gland. Ref.1 Ref.14
Domain	The cytoplasmic domain 3 and the C-terminus tail domain contain the lysosomal sorting signals and are necessary and sufficient for intracellular retention and delivery to lysosomal and melanosomal, respectively in melanocytic and non-melanocytic cells.
Post-translational modification	Glycosylated. Ref.7 Phosphorylated. Ref.12
Involvement in disease	Albinism ocular 1 (OA1) [MIM:300500]: Form of albinism affecting only the eye. Pigment of the hair and skin is normal or only slightly diluted. Eyes may be severely affected with photophobia and reduced visual acuity. Nystagmus or strabismus are often associated. The irides and fundus are depigmented. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Nystagmus congenital X-linked 6 (NYS6) [MIM:300814]: A condition defined as conjugated, spontaneous and involuntary ocular oscillations that appear at birth or during the first three months of life. Other associated features may include mildly decreased visual acuity, strabismus, astigmatism, and occasionally head nodding. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22
Sequence similarities	Belongs to the G-protein coupled receptor OA family.
Sequence caution	The sequence AAH68977.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA88742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence EAW98773.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell membrane Golgi apparatus Lysosome Membrane
Disease	Albinism Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium-mediated signaling using intracellular calcium source Inferred from direct assay Ref.14. Source: UniProtKB eye pigment biosynthetic process Traceable author statement Ref.1. Source: ProtInc melanosome organization Inferred from mutant phenotype Ref.15. Source: UniProtKB melanosome transport Inferred from direct assay Ref.15. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from direct assay Ref.12. Source: UniProtKB regulation of calcium-mediated signaling Inferred from direct assay Ref.14. Source: UniProtKB visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from direct assay Ref.15. Source: UniProtKB apical plasma membrane Inferred from direct assay Ref.14. Source: UniProtKB integral to membrane Traceable author statement Ref.1. Source: ProtInc lysosomal membrane Inferred from direct assay Ref.10. Source: UniProtKB melanosome membrane Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	L-DOPA binding Inferred from direct assay Ref.14. Source: UniProtKB L-DOPA receptor activity Inferred from direct assay Ref.14. Source: UniProtKB dopamine binding Inferred from direct assay Ref.14. Source: UniProtKB tyrosine binding Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLANA	Q16655	1	EBI-2509708,EBI-2509726

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 404	404	G-protein coupled receptor 143		PRO_0000195086
Regions
	Topological domain	1 – 28	28	Extracellular Potential
	Transmembrane	29 – 49	21	Helical; Name=1; Potential
	Topological domain	50 – 78	29	Cytoplasmic Potential
	Transmembrane	79 – 99	21	Helical; Name=2; Potential
	Topological domain	100 – 124	25	Extracellular Potential
	Transmembrane	125 – 145	21	Helical; Name=3; Potential
	Topological domain	146 – 149	4	Cytoplasmic Potential
	Transmembrane	150 – 170	21	Helical; Name=4; Potential
	Topological domain	171 – 191	21	Extracellular Potential
	Transmembrane	192 – 212	21	Helical; Name=5; Potential
	Topological domain	213 – 248	36	Cytoplasmic Potential
	Transmembrane	249 – 269	21	Helical; Name=6; Potential
	Topological domain	270 – 292	23	Extracellular Potential
	Transmembrane	293 – 313	21	Helical; Name=7; Potential
	Topological domain	314 – 404	91	Cytoplasmic Potential
	Region	221 – 238	18	Necessary for its G protein-activation ability and normal distribution of melanosomes
	Motif	222 – 231	10	lysosomal/melanosomal membrane localization signal
	Motif	329 – 330	2	lysosomal/melanosomal membrane localization signal
Amino acid modifications
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	5	1	R → C in OA1; results in altered glycosylation pattern and subcellular localization consistent with proteiin retention in the endoplasmic reticulum; lacks G protein-activation abilities. Ref.7 Ref.19		VAR_018130
	Natural variant	35	1	G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.16 Ref.18		VAR_005507
	Natural variant	39	1	L → R in OA1. Ref.18		VAR_018131
	Natural variant	78	1	D → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.19		VAR_018132
	Natural variant	78	1	D → V in OA1. Ref.18		VAR_018133
	Natural variant	80	1	Missing in OA1. Ref.24		VAR_063264
	Natural variant	81	1	G → V in OA1. Ref.20		VAR_063265
	Natural variant	84	1	G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.16		VAR_005508
	Natural variant	84	1	G → R in OA1. Ref.17		VAR_005509
	Natural variant	89	1	S → F in NYS6. Ref.22		VAR_063266
	Natural variant	116	1	C → G in OA1. Ref.12 Ref.23		VAR_063267
	Natural variant	116	1	C → R in OA1. Ref.17		VAR_005510
	Natural variant	116	1	C → S in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.19		VAR_018134
	Natural variant	116	1	C → W in OA1. Ref.20		VAR_063268
	Natural variant	118	1	G → E in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.17 Ref.19 Ref.24		VAR_005511
	Natural variant	124	1	Q → R in OA1. Ref.19		VAR_018135
	Natural variant	132	1	W → R in OA1. Ref.21		VAR_063269
	Natural variant	133	1	W → R in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.17 Ref.18		VAR_005513
	Natural variant	134	1	L → P in OA1. Ref.20		VAR_063270
	Natural variant	138	1	A → V in OA1. Ref.17		VAR_005514
	Natural variant	152	1	S → N in OA1. Ref.17		VAR_005515
	Natural variant	166	1	T → N in OA1. Ref.20		VAR_063271
	Natural variant	173	1	A → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.16		VAR_005516
	Natural variant	185	1	E → K in OA1. Ref.21		VAR_063272
	Natural variant	186	1	R → P in OA1. Ref.21		VAR_063273
	Natural variant	186	1	R → W in OA1. Ref.21		VAR_063274
	Natural variant	229	1	G → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.19		VAR_018136
	Natural variant	232	1	T → K in OA1; abnormal distribution of melanosomes; Not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.13 Ref.17		VAR_005517
	Natural variant	233	1	E → K in OA1. Ref.18		VAR_018137
	Natural variant	235	1	E → K in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.17		VAR_005518
	Natural variant	244	1	I → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.19		VAR_018138
	Natural variant	261	1	I → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.19		VAR_018139
	Natural variant	271	1	E → G in OA1. Ref.19		VAR_018140
	Natural variant	290	1	Missing in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.16		VAR_005519
	Natural variant	292	1	W → C in OA1. Ref.19		VAR_018141
	Natural variant	292	1	W → G in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. Ref.7 Ref.16		VAR_005520
Experimental info
	Mutagenesis	223 – 224	2	LL → AA: Delivered to both at the cell surface and in vesicles of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells; when associated with 329-A-A-330. Ref.10
	Mutagenesis	329 – 330	2	WE → AA: Mostly delivered at the cell surface of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells; when associated with 224-A-A-225. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P51810 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 20DEB20E80CC0E1D	FASTA	404	43,878
	10 20 30 40 50 60 MASPRLGTFC CPTRDAATQL VLSFQPRAFH ALCLGSGGLR LALGLLQLLP GRRPAGPGSP 70 80 90 100 110 120 ATSPPASVRI LRAAAACDLL GCLGMVIRST VWLGFPNFVD SVSDMNHTEI WPAAFCVGSA 130 140 150 160 170 180 MWIQLLYSAC FWWLFCYAVD AYLVIRRSAG LSTILLYHIM AWGLATLLCV EGAAMLYYPS 190 200 210 220 230 240 VSRCERGLDH AIPHYVTMYL PLLLVLVANP ILFQKTVTAV ASLLKGRQGI YTENERRMGA 250 260 270 280 290 300 VIKIRFFKIM LVLIICWLSN IINESLLFYL EMQTDINGGS LKPVRTAAKT TWFIMGILNP 310 320 330 340 350 360 AQGFLLSLAF YGWTGCSLGF QSPRKEIQWE SLTTSAAEGA HPSPLMPHEN PASGKVSQVG 370 380 390 400 GQTSDEALSM LSEGSDASTI EIHTASESCN KNEGDPALPT HGDL

References

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[1]	"Cloning of the gene for ocular albinism type 1 from the distal short arm of the X chromosome." Bassi M.T., Schiaffino M.V., Renieri A., de Nigris F., Galli L., Bruttini M., Gebbia M.A.B., Bergen A.A.B., Lewis R., Ballabio A. Nat. Genet. 10:13-19(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Retina.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	"Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism." Oetting W.S., King R.A. Hum. Mutat. 13:99-115(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON OA1 VARIANTS.
[6]	"Ocular albinism: evidence for a defect in an intracellular signal transduction system." Schiaffino M.V., d'Addio M., Alloni A., Baschirotto C., Valetti C., Cortese K., Puri C., Bassi M.T., Colla C., De Luca M., Tacchetti C., Ballabio A. Nat. Genet. 23:108-112(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION. Tissue: Melanocyte.
[7]	"Defective intracellular transport and processing of OA1 is a major cause of ocular albinism type 1." d'Addio M., Pizzigoni A., Bassi M.T., Baschirotto C., Valetti C., Incerti B., Clementi M., De Luca M., Ballabio A., Schiaffino M.V. Hum. Mol. Genet. 9:3011-3018(2000) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, CHARACTERIZATION OF VARIANTS OA1 CYS-5; ASP-35; ASN-78; ASP-84; SER-116; GLU-118; ARG-133; ASP-173; ASN-261; THR-290 DEL AND GLY-292.
[8]	"New insights into ocular albinism type 1 (OA1): mutations and polymorphisms of the OA1 gene." Oetting W.S. Hum. Mutat. 19:85-92(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON OA1 VARIANTS.
[9]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"An unconventional dileucine-based motif and a novel cytosolic motif are required for the lysosomal and melanosomal targeting of OA1." Piccirillo R., Palmisano I., Innamorati G., Bagnato P., Altimare D., Schiaffino M.V. J. Cell Sci. 119:2003-2014(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS OA1 VAL-229; LYS-232; LYS-235 AND VAL-244, MUTAGENESIS OF 224-LEU-LEU-225 AND 329-LEU-LEU-330.
[11]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"The melanosomal/lysosomal protein OA1 has properties of a G protein-coupled receptor." Innamorati G., Piccirillo R., Bagnato P., Palmisano I., Schiaffino M.V. Pigment Cell Res. 19:125-135(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARRB1 AND ARRB1, PHOSPHORYLATION, CHARACTERIZATION OF VARIANT OA1 GLY-116, SUBCELLULAR LOCATION.
[13]	"The ocular albinism type 1 protein, an intracellular G protein-coupled receptor, regulates melanosome transport in pigment cells." Palmisano I., Bagnato P., Palmigiano A., Innamorati G., Rotondo G., Altimare D., Venturi C., Sviderskaya E.V., Piccirillo R., Coppola M., Marigo V., Incerti B., Ballabio A., Surace E.M., Tacchetti C., Bennett D.C., Schiaffino M.V. Hum. Mol. Genet. 17:3487-3501(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF VARIANT OA1 LYS-232, SUBCELLULAR LOCATION.
[14]	"L-DOPA is an endogenous ligand for OA1." Lopez V.M., Decatur C.L., Stamer W.D., Lynch R.M., McKay B.S. PLoS Biol. 6:E236-E236(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]	"The ocular albinism type 1 (OA1) G-protein-coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and composition." Giordano F., Bonetti C., Surace E.M., Marigo V., Raposo G. Hum. Mol. Genet. 18:4530-4545(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MLANA.
[16]	"Analysis of the OA1 gene reveals mutations in only one-third of patients with X-linked ocular albinism." Schiaffino M.V., Bassi M.T., Balli L., Renieri A., Bruttini M., de Nigris F., Bergen A.A.B., Charles S.J., Yates J.R.W., Meindl A., Lewis R.A., King R.A., Ballabio A. Hum. Mol. Genet. 4:2319-2325(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 ASP-35; ASP-84; ASP-173; THR-290 DEL AND GLY-292.
[17]	"OA1 mutations and deletions in X-linked ocular albinism." Schnur R.E., Gao M., Wick P.A., Keller M., Benke P.J., Edwards M.J., Grix A.W., Hockey A., Jung J.H., Kidd K.K., Kistenmacher M., Levin A.V., Lewis R.A., Musarella M.A., Nowakowski R.W., Orlow S.J., Pagon R.S., Pillers D.-A.M. , Punnett H.H., Quinn G.E., Tezcan K., Wagstaff J., Weleber R.G. Am. J. Hum. Genet. 62:800-809(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 ARG-84; ARG-116; GLU-118; ARG-133; VAL-138; ASN-152; LYS-232 AND LYS-235.
[18]	"X-linked ocular albinism: prevalence and mutations -- a national study." Rosenberg T., Schwartz M. Eur. J. Hum. Genet. 6:570-577(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 ASP-35; ARG-39; VAL-78; ARG-133 AND LYS-233.
[19]	"Diverse prevalence of large deletions within the OA1 gene in ocular albinism type 1 patients from Europe and North America." Bassi M.T., Bergen A.A., Bitoun P., Charles S.J., Clementi M., Gosselin R., Hurst J., Lewis R.A., Lorenz B., Meitinger T., Messiaen L., Ramesar R.S., Ballabio A., Schiaffino M.V. Hum. Genet. 108:51-54(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 CYS-5; ASN-78; SER-116; GLU-118; ARG-124; VAL-229; VAL-244; ASN-261; GLY-271 AND CYS-292.
[20]	"Eight previously unidentified mutations found in the OA1 ocular albinism gene." Mayeur H., Roche O., Vetu C., Jaliffa C., Marchant D., Dollfus H., Bonneau D., Munier F.L., Schorderet D.F., Levin A.V., Heon E., Sutherland J., Lacombe D., Said E., Mezer E., Kaplan J., Dufier J.L., Marsac C., Menasche M., Abitbol M. BMC Med. Genet. 7:41-41(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 VAL-81; TRP-116; PRO-134 AND ASN-166.
[21]	"New mutations identified in the ocular albinism type 1 gene." Roma C., Ferrante P., Guardiola O., Ballabio A., Zollo M. Gene 402:20-27(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 ARG-132; LYS-185; TRP-186 AND PRO-186.
[22]	"Identification of a novel GPR143 mutation in a large Chinese family with congenital nystagmus as the most prominent and consistent manifestation." Liu J.Y., Ren X., Yang X., Guo T., Yao Q., Li L., Dai X., Zhang M., Wang L., Liu M., Wang Q.K. J. Hum. Genet. 52:565-570(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT NYS6 PHE-89.
[23]	"Identification of two novel mutations in families with X-linked ocular albinism." Iannaccone A., Gallaher K.T., Buchholz J., Jennings B.J., Neitz M., Sidjanin D.J. Mol. Vis. 13:1856-1861(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OA1 GLY-116.
[24]	"Novel GPR143 mutations and clinical characteristics in six Chinese families with X-linked ocular albinism." Fang S., Guo X., Jia X., Xiao X., Li S., Zhang Q. Mol. Vis. 14:1974-1982(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OA1 LEU-80 DEL AND GLU-118.
+	Additional computationally mapped references.

Web resources

Mutations of the OA1 gene

Retina International's Scientific Newsletter

Albinism database (ADB)

GPR143 mutations

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48804 mRNA. Translation: CAA88742.1. Different initiation. AC003036 Genomic DNA. No translation available. AC090481 Genomic DNA. No translation available. CH471074 Genomic DNA. Translation: EAW98773.1. Different initiation. BC068977 mRNA. Translation: AAH68977.1. Different initiation.
IPI	IPI00218565.
RefSeq	NP_000264.2. NM_000273.2.
UniGene	Hs.74124.
3D structure databases
ProteinModelPortal	P51810.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-53284N.
IntAct	P51810. 1 interaction.
STRING	9606.ENSP00000370316.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P51810.
Polymorphism databases
DMDM	3219999.
Proteomic databases
PaxDb	P51810.
PRIDE	P51810.
Protocols and materials databases
DNASU	4935.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380929; ENSP00000370316; ENSG00000101850. ENST00000467482; ENSP00000417161; ENSG00000101850.
GeneID	4935.
KEGG	hsa:4935.
UCSC	uc004cst.2. human.
Organism-specific databases
CTD	4935.
GeneCards	GC0XM009654.
HGNC	HGNC:20145. GPR143.
HPA	HPA003648.
MIM	300500. phenotype. 300808. gene. 300814. phenotype.
neXtProt	NX_P51810.
Orphanet	651. Congenital idiopathic nystagmus. 54. X-linked recessive ocular albinism.
PharmGKB	PA31872.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39873.
HOGENOM	HOG000112769.
HOVERGEN	HBG051784.
InParanoid	P51810.
KO	K08470.
OrthoDB	EOG42RD7J.
Gene expression databases
ArrayExpress	P51810.
Bgee	P51810.
CleanEx	HS_GPR143.
Genevestigator	P51810.
GermOnline	ENSG00000101850. Homo sapiens.
Family and domain databases
InterPro	IPR001414. Ocular_alb1. [Graphical view]
Pfam	PF02101. Ocular_alb. 1 hit. [Graphical view]
PRINTS	PR00965. OCULARALBNSM.
ProtoNet	Search...
Other
ChiTaRS	GPR143. human.
GenomeRNAi	4935.
NextBio	19011.
SOURCE	Search...

Entry information

Entry name

GP143_HUMAN

Accession

Primary (citable) accession number: P51810
Secondary accession number(s): Q6NTI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.