GP183_SALSA
ID GP183_SALSA Reviewed; 366 AA.
AC B5X337;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=G-protein coupled receptor 183;
GN Name=gpr183;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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; BT045456; ACI33718.1; -; mRNA.
DR RefSeq; NP_001133697.1; NM_001140225.1.
DR AlphaFoldDB; B5X337; -.
DR SMR; B5X337; -.
DR STRING; 8030.ENSSSAP00000036679; -.
DR GeneID; 100195196; -.
DR KEGG; sasa:100195196; -.
DR CTD; 556770; -.
DR OMA; PLFYCIV; -.
DR OrthoDB; 760173at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
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:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0036145; P:dendritic cell homeostasis; ISS:UniProtKB.
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: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..366
FT /note="G-protein coupled receptor 183"
FT /id="PRO_0000383158"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..317
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 366 AA; 41336 MW; DC3D4199B7C80CFB CRC64;
MQVMRTFNQP PTSSHPTPTL NDSDTCITLY NHRGYARVLM PLFYCIVFFV GLLGNALAFH
IIRPNVKKIN STTLYSANLV ISDILFTLSL PLRIIYYALG FHWPLGETLC KIVGLIFYIN
TYAGVNFMTC LSVDRFIAVV LPLRFARFRK VSNVRYICVG VWLLVLMQTL PLLSMPMTNE
EPDGFITCME YPNFEPVPNI SYILIGAVFL GYGVPVVTIL VCYSILCCKL RLAAKANQLT
DKSGRSQKAI GVICCVSLVF VVCFSPYHID LLQYMIRKLI YTPDCAELTA FQISLHFTVC
LMNLNSCLDP FIYFFACKGY KTKVLKILKR QVSVSFSSAA RTLPEGLSRD ISDGNKIHLN
STRHKE
