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P51810

- GP143_HUMAN

UniProt

P51810 - GP143_HUMAN

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Protein
G-protein coupled receptor 143
Gene
GPR143, OA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB
  2. L-DOPA binding Source: UniProtKB
  3. L-DOPA receptor activity Source: UniProtKB
  4. dopamine binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. tyrosine binding Source: UniProtKB

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: UniProtKB
  2. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  3. eye pigment biosynthetic process Source: ProtInc
  4. melanosome localization Source: UniProtKB
  5. melanosome organization Source: UniProtKB
  6. melanosome transport Source: UniProtKB
  7. neuropeptide signaling pathway Source: GOC
  8. phosphatidylinositol-mediated signaling Source: UniProtKB
  9. regulation of calcium-mediated signaling Source: UniProtKB
  10. signal transduction Source: ProtInc
  11. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein coupled receptor 143
Alternative name(s):
Ocular albinism type 1 protein
Gene namesi
Name:GPR143
Synonyms:OA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:20145. GPR143.

Subcellular locationi

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.7 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828Extracellular Reviewed prediction
Add
BLAST
Transmembranei29 – 4921Helical; Name=1; Reviewed prediction
Add
BLAST
Topological domaini50 – 7829Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei79 – 9921Helical; Name=2; Reviewed prediction
Add
BLAST
Topological domaini100 – 12425Extracellular Reviewed prediction
Add
BLAST
Transmembranei125 – 14521Helical; Name=3; Reviewed prediction
Add
BLAST
Topological domaini146 – 1494Cytoplasmic Reviewed prediction
Transmembranei150 – 17021Helical; Name=4; Reviewed prediction
Add
BLAST
Topological domaini171 – 19121Extracellular Reviewed prediction
Add
BLAST
Transmembranei192 – 21221Helical; Name=5; Reviewed prediction
Add
BLAST
Topological domaini213 – 24836Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei249 – 26921Helical; Name=6; Reviewed prediction
Add
BLAST
Topological domaini270 – 29223Extracellular Reviewed prediction
Add
BLAST
Transmembranei293 – 31321Helical; Name=7; Reviewed prediction
Add
BLAST
Topological domaini314 – 40491Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. apical plasma membrane Source: UniProtKB
  3. cytoplasm Source: ProtInc
  4. integral component of membrane Source: ProtInc
  5. lysosomal membrane Source: UniProtKB
  6. melanosome Source: UniProtKB
  7. melanosome membrane Source: UniProtKB
  8. membrane Source: ProtInc
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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.12 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → C in OA1; results in altered glycosylation pattern and subcellular localization consistent with proteiin retention in the endoplasmic reticulum; lacks G protein-activation abilities. 2 Publications
VAR_018130
Natural varianti35 – 351G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 3 Publications
VAR_005507
Natural varianti39 – 391L → R in OA1. 1 Publication
VAR_018131
Natural varianti78 – 781D → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018132
Natural varianti78 – 781D → V in OA1. 1 Publication
VAR_018133
Natural varianti80 – 801Missing in OA1. 1 Publication
VAR_063264
Natural varianti81 – 811G → V in OA1. 1 Publication
VAR_063265
Natural varianti84 – 841G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005508
Natural varianti84 – 841G → R in OA1. 1 Publication
VAR_005509
Natural varianti116 – 1161C → G in OA1. 2 Publications
VAR_063267
Natural varianti116 – 1161C → R in OA1. 1 Publication
VAR_005510
Natural varianti116 – 1161C → S in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018134
Natural varianti116 – 1161C → W in OA1. 1 Publication
VAR_063268
Natural varianti118 – 1181G → E in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 4 Publications
VAR_005511
Natural varianti124 – 1241Q → R in OA1. 1 Publication
VAR_018135
Natural varianti132 – 1321W → R in OA1. 1 Publication
VAR_063269
Natural varianti133 – 1331W → R in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 3 Publications
VAR_005513
Natural varianti134 – 1341L → P in OA1. 1 Publication
VAR_063270
Natural varianti138 – 1381A → V in OA1. 1 Publication
VAR_005514
Natural varianti152 – 1521S → N in OA1. 1 Publication
VAR_005515
Natural varianti166 – 1661T → N in OA1. 1 Publication
VAR_063271
Natural varianti173 – 1731A → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005516
Natural varianti185 – 1851E → K in OA1. 1 Publication
VAR_063272
Natural varianti186 – 1861R → P in OA1. 1 Publication
VAR_063273
Natural varianti186 – 1861R → W in OA1. 1 Publication
VAR_063274
Natural varianti229 – 2291G → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_018136
Natural varianti232 – 2321T → K in OA1; abnormal distribution of melanosomes; Not delivered at the cell surface of melanocytic and non-melanocytic cells. 3 Publications
VAR_005517
Natural varianti233 – 2331E → K in OA1. 1 Publication
VAR_018137
Natural varianti235 – 2351E → K in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_005518
Natural varianti244 – 2441I → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_018138
Natural varianti261 – 2611I → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018139
Natural varianti271 – 2711E → G in OA1. 1 Publication
VAR_018140
Natural varianti290 – 2901Missing in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005519
Natural varianti292 – 2921W → C in OA1. 1 Publication
VAR_018141
Natural varianti292 – 2921W → G in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005520
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891S → F in NYS6. 1 Publication
VAR_063266

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi223 – 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. 1 Publication
Mutagenesisi329 – 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. 1 Publication

Keywords - Diseasei

Albinism, Disease mutation

Organism-specific databases

MIMi300500. phenotype.
300814. phenotype.
Orphaneti651. Idiopathic infantile nystagmus.
54. X-linked recessive ocular albinism.
PharmGKBiPA31872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404G-protein coupled receptor 143
PRO_0000195086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Glycosylated.1 Publication
Phosphorylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP51810.
PRIDEiP51810.

PTM databases

PhosphoSiteiP51810.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiP51810.
BgeeiP51810.
CleanExiHS_GPR143.
GenevestigatoriP51810.

Organism-specific databases

HPAiHPA003648.

Interactioni

Subunit structurei

Interacts with heterotrimeric G(i) proteins. Interacts with ARRB1 and ARRB2. Interacts with MLANA.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MLANAQ166551EBI-2509708,EBI-2509726

Protein-protein interaction databases

BioGridi110989. 2 interactions.
DIPiDIP-53284N.
IntActiP51810. 1 interaction.
STRINGi9606.ENSP00000370316.

Structurei

3D structure databases

ProteinModelPortaliP51810.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 23818Necessary for its G protein-activation ability and normal distribution of melanosomes
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 23110lysosomal/melanosomal membrane localization signal
Motifi329 – 3302lysosomal/melanosomal membrane localization signal

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG39873.
HOGENOMiHOG000112769.
HOVERGENiHBG051784.
InParanoidiP51810.
KOiK08470.
OrthoDBiEOG7HXCQZ.
PhylomeDBiP51810.
TreeFamiTF324849.

Family and domain databases

InterProiIPR001414. Ocular_alb1.
[Graphical view]
PfamiPF02101. Ocular_alb. 1 hit.
[Graphical view]
PRINTSiPR00965. OCULARALBNSM.

Sequencei

Sequence statusi: Complete.

P51810-1 [UniParc]FASTAAdd to Basket

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MASPRLGTFC CPTRDAATQL VLSFQPRAFH ALCLGSGGLR LALGLLQLLP    50
GRRPAGPGSP ATSPPASVRI LRAAAACDLL GCLGMVIRST VWLGFPNFVD 100
SVSDMNHTEI WPAAFCVGSA MWIQLLYSAC FWWLFCYAVD AYLVIRRSAG 150
LSTILLYHIM AWGLATLLCV EGAAMLYYPS VSRCERGLDH AIPHYVTMYL 200
PLLLVLVANP ILFQKTVTAV ASLLKGRQGI YTENERRMGA VIKIRFFKIM 250
LVLIICWLSN IINESLLFYL EMQTDINGGS LKPVRTAAKT TWFIMGILNP 300
AQGFLLSLAF YGWTGCSLGF QSPRKEIQWE SLTTSAAEGA HPSPLMPHEN 350
PASGKVSQVG GQTSDEALSM LSEGSDASTI EIHTASESCN KNEGDPALPT 400
HGDL 404
Length:404
Mass (Da):43,878
Last modified:July 15, 1998 - v2
Checksum:i20DEB20E80CC0E1D
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → C in OA1; results in altered glycosylation pattern and subcellular localization consistent with proteiin retention in the endoplasmic reticulum; lacks G protein-activation abilities. 2 Publications
VAR_018130
Natural varianti35 – 351G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 3 Publications
VAR_005507
Natural varianti39 – 391L → R in OA1. 1 Publication
VAR_018131
Natural varianti78 – 781D → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018132
Natural varianti78 – 781D → V in OA1. 1 Publication
VAR_018133
Natural varianti80 – 801Missing in OA1. 1 Publication
VAR_063264
Natural varianti81 – 811G → V in OA1. 1 Publication
VAR_063265
Natural varianti84 – 841G → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005508
Natural varianti84 – 841G → R in OA1. 1 Publication
VAR_005509
Natural varianti89 – 891S → F in NYS6. 1 Publication
VAR_063266
Natural varianti116 – 1161C → G in OA1. 2 Publications
VAR_063267
Natural varianti116 – 1161C → R in OA1. 1 Publication
VAR_005510
Natural varianti116 – 1161C → S in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018134
Natural varianti116 – 1161C → W in OA1. 1 Publication
VAR_063268
Natural varianti118 – 1181G → E in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 4 Publications
VAR_005511
Natural varianti124 – 1241Q → R in OA1. 1 Publication
VAR_018135
Natural varianti132 – 1321W → R in OA1. 1 Publication
VAR_063269
Natural varianti133 – 1331W → R in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 3 Publications
VAR_005513
Natural varianti134 – 1341L → P in OA1. 1 Publication
VAR_063270
Natural varianti138 – 1381A → V in OA1. 1 Publication
VAR_005514
Natural varianti152 – 1521S → N in OA1. 1 Publication
VAR_005515
Natural varianti166 – 1661T → N in OA1. 1 Publication
VAR_063271
Natural varianti173 – 1731A → D in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005516
Natural varianti185 – 1851E → K in OA1. 1 Publication
VAR_063272
Natural varianti186 – 1861R → P in OA1. 1 Publication
VAR_063273
Natural varianti186 – 1861R → W in OA1. 1 Publication
VAR_063274
Natural varianti229 – 2291G → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_018136
Natural varianti232 – 2321T → K in OA1; abnormal distribution of melanosomes; Not delivered at the cell surface of melanocytic and non-melanocytic cells. 3 Publications
VAR_005517
Natural varianti233 – 2331E → K in OA1. 1 Publication
VAR_018137
Natural varianti235 – 2351E → K in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_005518
Natural varianti244 – 2441I → V in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells. 2 Publications
VAR_018138
Natural varianti261 – 2611I → N in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_018139
Natural varianti271 – 2711E → G in OA1. 1 Publication
VAR_018140
Natural varianti290 – 2901Missing in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005519
Natural varianti292 – 2921W → C in OA1. 1 Publication
VAR_018141
Natural varianti292 – 2921W → G in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum. 2 Publications
VAR_005520

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14134.2.
RefSeqiNP_000264.2. NM_000273.2.
UniGeneiHs.74124.

Genome annotation databases

EnsembliENST00000380929; ENSP00000370316; ENSG00000101850.
ENST00000467482; ENSP00000417161; ENSG00000101850.
GeneIDi4935.
KEGGihsa:4935.
UCSCiuc004cst.2. human.

Polymorphism databases

DMDMi3219999.

Cross-referencesi

Web resourcesi

Mutations of the OA1 gene

Retina International's Scientific Newsletter

Albinism database (ADB)

GPR143 mutations

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS14134.2.
RefSeqi NP_000264.2. NM_000273.2.
UniGenei Hs.74124.

3D structure databases

ProteinModelPortali P51810.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110989. 2 interactions.
DIPi DIP-53284N.
IntActi P51810. 1 interaction.
STRINGi 9606.ENSP00000370316.

Chemistry

GuidetoPHARMACOLOGYi 203.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P51810.

Polymorphism databases

DMDMi 3219999.

Proteomic databases

PaxDbi P51810.
PRIDEi P51810.

Protocols and materials databases

DNASUi 4935.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380929 ; ENSP00000370316 ; ENSG00000101850 .
ENST00000467482 ; ENSP00000417161 ; ENSG00000101850 .
GeneIDi 4935.
KEGGi hsa:4935.
UCSCi uc004cst.2. human.

Organism-specific databases

CTDi 4935.
GeneCardsi GC0XM009654.
GeneReviewsi GPR143.
HGNCi HGNC:20145. GPR143.
HPAi HPA003648.
MIMi 300500. phenotype.
300808. gene.
300814. phenotype.
neXtProti NX_P51810.
Orphaneti 651. Idiopathic infantile nystagmus.
54. X-linked recessive ocular albinism.
PharmGKBi PA31872.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39873.
HOGENOMi HOG000112769.
HOVERGENi HBG051784.
InParanoidi P51810.
KOi K08470.
OrthoDBi EOG7HXCQZ.
PhylomeDBi P51810.
TreeFami TF324849.

Miscellaneous databases

ChiTaRSi GPR143. human.
GeneWikii GPR143.
GenomeRNAii 4935.
NextBioi 19011.
PROi P51810.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51810.
Bgeei P51810.
CleanExi HS_GPR143.
Genevestigatori P51810.

Family and domain databases

InterProi IPR001414. Ocular_alb1.
[Graphical view ]
Pfami PF02101. Ocular_alb. 1 hit.
[Graphical view ]
PRINTSi PR00965. OCULARALBNSM.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiGP143_HUMAN
AccessioniPrimary (citable) accession number: P51810
Secondary accession number(s): Q6NTI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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