GP83A_DANRE
ID GP83A_DANRE Reviewed; 368 AA.
AC A5PLE7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=G-protein coupled receptor 183-A;
GN Name=gpr183a; Synonyms=gpr183; ORFNames=zgc:165579;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: G-protein coupled receptor expressed in lymphocytes that acts
CC as a chemotactic receptor for B-cells, T-cells, splenic dendritic
CC cells, monocytes/macrophages and astrocytes (By similarity). Receptor
CC for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and
CC other related oxysterols (By similarity). Mediates cell positioning and
CC movement of a number of cells by binding the 7-alpha,25-OHC ligand that
CC forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC
CC mediates the correct localization of B-cells during humoral immune
CC responses (By similarity). {ECO:0000250|UniProtKB:P32249,
CC ECO:0000250|UniProtKB:Q3U6B2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32249};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC142876; AAI42877.1; -; mRNA.
DR RefSeq; NP_001092711.1; NM_001099241.1.
DR AlphaFoldDB; A5PLE7; -.
DR SMR; A5PLE7; -.
DR STRING; 7955.ENSDARP00000010296; -.
DR PaxDb; A5PLE7; -.
DR PRIDE; A5PLE7; -.
DR GeneID; 556770; -.
DR KEGG; dre:556770; -.
DR CTD; 556770; -.
DR ZFIN; ZDB-GENE-070615-28; gpr183a.
DR eggNOG; ENOG502QWD9; Eukaryota.
DR InParanoid; A5PLE7; -.
DR OrthoDB; 760173at2759; -.
DR PhylomeDB; A5PLE7; -.
DR Reactome; R-DRE-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR PRO; PR:A5PLE7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008142; F:oxysterol binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:ZFIN.
DR GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0036145; P:dendritic cell homeostasis; ISS:UniProtKB.
DR GO; GO:0098508; P:endothelial to hematopoietic transition; IMP:ZFIN.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:2000458; P:regulation of astrocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0010818; P:T cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0061470; P:T follicular helper cell differentiation; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunity; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..368
FT /note="G-protein coupled receptor 183-A"
FT /id="PRO_0000383156"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 368 AA; 41705 MW; 64541B5E54225D94 CRC64;
METTSANFTQ NDSNVCTNLY NHRGWAQYFL PAMYSLICIV GLLGNVLALH VIWPNLKKIN
STTLYSANLV VSDILFSLAL PLRVVYYARG FDWPMGEGLC KAVALLFYIN MYAGVNFMTC
LSVDRFIAVV LPLRFSRFRK VQKVRYICGV VWVVVLMQTL PLLSMPMTNI EQSGHITCME
YPNFEKIDNL PVMLIGAVVL GFGIPVITIL VCYTALCLKL RHLAKSNKLT EKSGRSSKAI
GVICTVILVF VVCYSPYHVD LLQYMIKKLR YDPDCSELHK FQISLHITVC FMNLNSCLDP
FIYFFACKGY KKKVLKLLKK QVSMSFSSVV RTSPEGSSKD VFGNDKIQMN SRSFQKERSS
VLLNSLEQ
