GP143_MOUSE
ID GP143_MOUSE Reviewed; 405 AA.
AC P70259; O89031;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=G-protein coupled receptor 143;
DE AltName: Full=MOA1;
DE AltName: Full=Ocular albinism type 1 protein homolog;
GN Name=Gpr143; Synonyms=Oa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Retina;
RX PubMed=8889556; DOI=10.1101/gr.6.9.880;
RA Bassi M.T., Incerti B., Easty D.J., Sviderskaya E.V., Ballabio A.;
RT "Cloning of the murine homolog of the ocular albinism type 1 (OA1) gene:
RT sequence, genomic structure, and expression analysis in pigment cells.";
RL Genome Res. 6:880-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8921399; DOI=10.1006/geno.1996.0545;
RA Newton J.M., Orlow S.J., Barsh G.S.;
RT "Isolation and characterization of a mouse homolog of the X-linked ocular
RT albinism (OA1) gene.";
RL Genomics 37:219-225(1996).
RN [3]
RP FUNCTION.
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).
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:18697795}.
CC -!- SUBUNIT: Interacts with heterotrimeric G(i) proteins. Interacts with
CC ARRB1 and ARRB2. Interacts with MLANA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P51810}; Multi-
CC pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P51810}; 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. {ECO:0000250|UniProtKB:P51810}.
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. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor OA family.
CC {ECO:0000305}.
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DR EMBL; X98352; CAA66996.1; -; Genomic_DNA.
DR EMBL; U63918; AAC52890.1; -; mRNA.
DR CCDS; CCDS30476.1; -.
DR RefSeq; NP_035081.3; NM_010951.3.
DR AlphaFoldDB; P70259; -.
DR SMR; P70259; -.
DR STRING; 10090.ENSMUSP00000026383; -.
DR GlyGen; P70259; 2 sites.
DR iPTMnet; P70259; -.
DR PhosphoSitePlus; P70259; -.
DR PaxDb; P70259; -.
DR PRIDE; P70259; -.
DR ProteomicsDB; 267747; -.
DR Antibodypedia; 8143; 166 antibodies from 28 providers.
DR DNASU; 18241; -.
DR Ensembl; ENSMUST00000026383; ENSMUSP00000026383; ENSMUSG00000025333.
DR GeneID; 18241; -.
DR KEGG; mmu:18241; -.
DR UCSC; uc009uqo.1; mouse.
DR CTD; 4935; -.
DR MGI; MGI:107193; Gpr143.
DR VEuPathDB; HostDB:ENSMUSG00000025333; -.
DR eggNOG; ENOG502QQII; Eukaryota.
DR GeneTree; ENSGT00390000016722; -.
DR HOGENOM; CLU_053538_1_1_1; -.
DR InParanoid; P70259; -.
DR OMA; DIWPAAF; -.
DR OrthoDB; 1476889at2759; -.
DR PhylomeDB; P70259; -.
DR TreeFam; TF324849; -.
DR Reactome; R-MMU-375280; Amine ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 18241; 2 hits in 74 CRISPR screens.
DR PRO; PR:P70259; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70259; protein.
DR Bgee; ENSMUSG00000025333; Expressed in iris and 23 other tissues.
DR ExpressionAtlas; P70259; baseline and differential.
DR Genevisible; P70259; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0035240; F:dopamine binding; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0072544; F:L-DOPA binding; ISS:UniProtKB.
DR GO; GO:0035643; F:L-DOPA receptor activity; ISS:UniProtKB.
DR GO; GO:0072545; F:tyrosine binding; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032400; P:melanosome localization; ISO:MGI.
DR GO; GO:0032438; P:melanosome organization; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:1903056; P:regulation of melanosome organization; IMP:UniProtKB.
DR GO; GO:1902908; P:regulation of melanosome transport; IMP:UniProtKB.
DR InterPro; IPR001414; GPR143.
DR PANTHER; PTHR15177; PTHR15177; 1.
DR Pfam; PF02101; Ocular_alb; 1.
DR PRINTS; PR00965; OCULARALBNSM.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lysosome;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..405
FT /note="G-protein coupled receptor 143"
FT /id="PRO_0000195087"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..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..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..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..405
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 /evidence="ECO:0000250"
FT MOTIF 222..231
FT /note="lysosomal/melanosomal membrane localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 329..330
FT /note="lysosomal/melanosomal membrane localization signal"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 175
FT /note="M -> S (in Ref. 2; AAC52890)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="F -> L (in Ref. 2; AAC52890)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Q -> L (in Ref. 2; AAC52890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44564 MW; 716405A6512ED312 CRC64;
MASPRLGIFC CPTWDAATQL VLSFQPRVFH ALCLGSGTLR LVLGLLQLLS GRRSVGHRAP
ATSPAASVHI LRAATACDLL GCLGIVIRST VWIAYPEFIE NISNVNATDI WPATFCVGSA
MWIQLLYSAC FWWLFCYAVD VYLVIRRSAG RSTILLYHIM AWGLAVLLCV EGAVMLYYPS
VSRCERGLDH AIPHYVTTYL PLLLVLVANP ILFHKTVTSV ASLLKGRKGV YTENERLMGA
VIKTRFFKIM LVLIACWLSN IINESLLFYL EMQPDIHGGS LKRIQNAART TWFIMGILNP
AQGLLLSLAF YGWTGCSLDV HPPKMVIQWE TMTASAAEGT YQTPVRSCVP HQNPRKVVCV
GGHTSDEVLS ILSEDSDAST VEIHTATGSC NIKEVDSISQ AQGEL
