GP183_RAT
ID GP183_RAT Reviewed; 357 AA.
AC D4A7K7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=G-protein coupled receptor 183;
DE AltName: Full=Epstein-Barr virus-induced G-protein coupled receptor 2;
DE Short=EBI2;
DE Short=EBV-induced G-protein coupled receptor 2;
GN Name=Gpr183; Synonyms=Ebi2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) 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). Guides B-cell movement along the B-cell
CC zone-T-cell zone boundary and later to interfollicular and outer
CC follicular regions (By similarity). Its specific expression during B-
CC cell maturation helps position B-cells appropriately for mounting T-
CC dependent antibody responses (By similarity). Collaborates with CXCR5
CC to mediate B-cell migration; probably by forming a heterodimer with
CC CXCR5 that affects the interaction between of CXCL13 and CXCR5 (By
CC similarity). Also acts as a chemotactic receptor for some T-cells upon
CC binding to 7-alpha,25-OHC ligand (By similarity). Promotes follicular
CC helper T (Tfh) cells differentiation by positioning activated T-cells
CC at the follicle-T-zone interface, promoting contact of newly activated
CC CD4 T-cells with activated dendritic cells and exposing them to Tfh-
CC cell-promoting inducible costimulator (ICOS) ligand (By similarity).
CC Expression in splenic dendritic cells is required for their
CC homeostasis, localization and ability to induce B- and T-cell
CC responses: GPR183 acts as a chemotactic receptor in dendritic cells
CC that mediates the accumulation of CD4(+) dendritic cells in bridging
CC channels (By similarity). Regulates migration of astrocytes and is
CC involved in communication between astrocytes and macrophages (By
CC similarity). Promotes osteoclast precursor migration to bone surfaces
CC (By similarity). Signals constitutively through G(i)-alpha, but not
CC G(s)-alpha or G(q)-alpha (By similarity). Signals constitutively also
CC via MAPK1/3 (ERK1/2) (By similarity). {ECO:0000250|UniProtKB:P32249,
CC ECO:0000250|UniProtKB:Q3U6B2}.
CC -!- SUBUNIT: Homodimer and heterodimer. Heterodimerizes with CXCR5; leading
CC to modulate the interaction between of CXCL13 and CXCR5.
CC {ECO:0000250|UniProtKB:P32249}.
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; AABR03095075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473951; EDM02572.1; -; Genomic_DNA.
DR RefSeq; NP_001102856.1; NM_001109386.1.
DR AlphaFoldDB; D4A7K7; -.
DR SMR; D4A7K7; -.
DR STRING; 10116.ENSRNOP00000035137; -.
DR BindingDB; D4A7K7; -.
DR ChEMBL; CHEMBL4802001; -.
DR GlyGen; D4A7K7; 1 site.
DR iPTMnet; D4A7K7; -.
DR PhosphoSitePlus; D4A7K7; -.
DR PaxDb; D4A7K7; -.
DR Ensembl; ENSRNOT00000034560; ENSRNOP00000035137; ENSRNOG00000025094.
DR Ensembl; ENSRNOT00000098097; ENSRNOP00000097517; ENSRNOG00000025094.
DR GeneID; 679975; -.
DR KEGG; rno:679975; -.
DR CTD; 1880; -.
DR RGD; 1598095; Gpr183.
DR eggNOG; ENOG502QWD9; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; D4A7K7; -.
DR OMA; HYTVFLM; -.
DR OrthoDB; 760173at2759; -.
DR PhylomeDB; D4A7K7; -.
DR TreeFam; TF350009; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:D4A7K7; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000025094; Expressed in spleen and 17 other tissues.
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:0002312; P:B cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
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:0006959; P:humoral immune response; ISO:RGD.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0002313; P:mature B cell differentiation involved in immune response; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; 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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Adaptive immunity; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunity; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="G-protein coupled receptor 183"
FT /id="PRO_0000418884"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 122..130
FT /note="Interaction with G proteins"
FT /evidence="ECO:0000250"
FT REGION 336..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 108
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 112
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 256
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U6B2"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U6B2"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 357 AA; 40227 MW; F14C3483B1825553 CRC64;
MANNFTTPLA ASHGNNCDLY AHHSTARILM PLHYSLVFII GLVGNLLALV VIVQNRKKIN
STTLYSMNLV ISDILFTTAL PTRIVYYALG FDWRIGDALC RITALLFYIN TYAGVNFMTC
LSIDRFFAVV HPLRYNKIKR IEYAKGICVF VWILVFAQTL PLLLKPMSKQ EADKTTCMEY
PNFEGTASLP WILLGACLLG YVLPLAIILL CYSQICCKLF RTAKQNPLTE KSGVNKKALN
TIILIIGVFV LCFTPYHVAI MQHMVKTLYA PGALGCGVRH SFQISLHFTV CLMNFNCCMD
PFIYFFACKG YKRKVMKMLK RQVSVSISSA VRSAPEENSR EMTESQMMIH SKASNGR
