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P51810 (GP143_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein coupled receptor 143
Alternative name(s):
Ocular albinism type 1 protein
Gene names
Name:GPR143
Synonyms:OA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCell membrane
Golgi apparatus
Lysosome
Membrane
   DiseaseAlbinism
Disease mutation
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-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_componentGolgi apparatus

Inferred from direct assay Ref.15. Source: UniProtKB

apical plasma membrane

Inferred from direct assay Ref.14. Source: UniProtKB

integral component of 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_functionL-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

MLANAQ166551EBI-2509708,EBI-2509726

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404G-protein coupled receptor 143
PRO_0000195086

Regions

Topological domain1 – 2828Extracellular Potential
Transmembrane29 – 4921Helical; Name=1; Potential
Topological domain50 – 7829Cytoplasmic Potential
Transmembrane79 – 9921Helical; Name=2; Potential
Topological domain100 – 12425Extracellular Potential
Transmembrane125 – 14521Helical; Name=3; Potential
Topological domain146 – 1494Cytoplasmic Potential
Transmembrane150 – 17021Helical; Name=4; Potential
Topological domain171 – 19121Extracellular Potential
Transmembrane192 – 21221Helical; Name=5; Potential
Topological domain213 – 24836Cytoplasmic Potential
Transmembrane249 – 26921Helical; Name=6; Potential
Topological domain270 – 29223Extracellular Potential
Transmembrane293 – 31321Helical; Name=7; Potential
Topological domain314 – 40491Cytoplasmic Potential
Region221 – 23818Necessary for its G protein-activation ability and normal distribution of melanosomes
Motif222 – 23110lysosomal/melanosomal membrane localization signal
Motif329 – 3302lysosomal/melanosomal membrane localization signal

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Potential

Natural variations

Natural variant51R → 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 variant351G → 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 variant391L → R in OA1. Ref.18
VAR_018131
Natural variant781D → 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 variant781D → V in OA1. Ref.18
VAR_018133
Natural variant801Missing in OA1. Ref.24
VAR_063264
Natural variant811G → V in OA1. Ref.20
VAR_063265
Natural variant841G → 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 variant841G → R in OA1. Ref.17
VAR_005509
Natural variant891S → F in NYS6. Ref.22
VAR_063266
Natural variant1161C → G in OA1. Ref.12 Ref.23
VAR_063267
Natural variant1161C → R in OA1. Ref.17
VAR_005510
Natural variant1161C → 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 variant1161C → W in OA1. Ref.20
VAR_063268
Natural variant1181G → 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 variant1241Q → R in OA1. Ref.19
VAR_018135
Natural variant1321W → R in OA1. Ref.21
VAR_063269
Natural variant1331W → 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 variant1341L → P in OA1. Ref.20
VAR_063270
Natural variant1381A → V in OA1. Ref.17
VAR_005514
Natural variant1521S → N in OA1. Ref.17
VAR_005515
Natural variant1661T → N in OA1. Ref.20
VAR_063271
Natural variant1731A → 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 variant1851E → K in OA1. Ref.21
VAR_063272
Natural variant1861R → P in OA1. Ref.21
VAR_063273
Natural variant1861R → W in OA1. Ref.21
VAR_063274
Natural variant2291G → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.19
VAR_018136
Natural variant2321T → 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 variant2331E → K in OA1. Ref.18
VAR_018137
Natural variant2351E → K in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.17
VAR_005518
Natural variant2441I → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. Ref.10 Ref.19
VAR_018138
Natural variant2611I → 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 variant2711E → G in OA1. Ref.19
VAR_018140
Natural variant2901Missing 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 variant2921W → C in OA1. Ref.19
VAR_018141
Natural variant2921W → 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

Mutagenesis223 – 2242LL → 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
Mutagenesis329 – 3302WE → 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 LengthMass (Da)Tools
P51810 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 20DEB20E80CC0E1D

FASTA40443,878
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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].
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].
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. expand/collapse author list , 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.
RefSeqNP_000264.2. NM_000273.2.
UniGeneHs.74124.

3D structure databases

ProteinModelPortalP51810.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110989. 2 interactions.
DIPDIP-53284N.
IntActP51810. 1 interaction.
STRING9606.ENSP00000370316.

Chemistry

GuidetoPHARMACOLOGY203.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP51810.

Polymorphism databases

DMDM3219999.

Proteomic databases

PaxDbP51810.
PRIDEP51810.

Protocols and materials databases

DNASU4935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380929; ENSP00000370316; ENSG00000101850.
ENST00000467482; ENSP00000417161; ENSG00000101850.
GeneID4935.
KEGGhsa:4935.
UCSCuc004cst.2. human.

Organism-specific databases

CTD4935.
GeneCardsGC0XM009654.
HGNCHGNC:20145. GPR143.
HPAHPA003648.
MIM300500. phenotype.
300808. gene.
300814. phenotype.
neXtProtNX_P51810.
Orphanet651. Idiopathic infantile nystagmus.
54. X-linked recessive ocular albinism.
PharmGKBPA31872.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39873.
HOGENOMHOG000112769.
HOVERGENHBG051784.
InParanoidP51810.
KOK08470.
OrthoDBEOG7HXCQZ.
TreeFamTF324849.

Gene expression databases

ArrayExpressP51810.
BgeeP51810.
CleanExHS_GPR143.
GenevestigatorP51810.

Family and domain databases

InterProIPR001414. Ocular_alb1.
[Graphical view]
PfamPF02101. Ocular_alb. 1 hit.
[Graphical view]
PRINTSPR00965. OCULARALBNSM.
ProtoNetSearch...

Other

ChiTaRSGPR143. human.
GeneWikiGPR143.
GenomeRNAi4935.
NextBio19011.
PROP51810.
SOURCESearch...

Entry information

Entry nameGP143_HUMAN
AccessionPrimary (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: March 19, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries