GP183_BOVIN
ID GP183_BOVIN Reviewed; 360 AA.
AC Q1RMI1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=G-protein coupled receptor 183;
GN Name=GPR183;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) 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; BC114884; AAI14885.1; -; mRNA.
DR RefSeq; NP_001039937.1; NM_001046472.2.
DR RefSeq; XP_005214015.1; XM_005213958.3.
DR RefSeq; XP_005214016.1; XM_005213959.3.
DR AlphaFoldDB; Q1RMI1; -.
DR SMR; Q1RMI1; -.
DR STRING; 9913.ENSBTAP00000007471; -.
DR PaxDb; Q1RMI1; -.
DR PRIDE; Q1RMI1; -.
DR Ensembl; ENSBTAT00000007471; ENSBTAP00000007471; ENSBTAG00000032084.
DR GeneID; 540287; -.
DR KEGG; bta:540287; -.
DR CTD; 1880; -.
DR VEuPathDB; HostDB:ENSBTAG00000032084; -.
DR VGNC; VGNC:29577; GPR183.
DR eggNOG; ENOG502QWD9; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q1RMI1; -.
DR OMA; HYTVFLM; -.
DR OrthoDB; 760173at2759; -.
DR TreeFam; TF350009; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000032084; Expressed in milk and 91 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: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; ISS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0002313; P:mature B cell differentiation involved in immune response; ISS:UniProtKB.
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 2: Evidence at transcript level;
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..360
FT /note="G-protein coupled receptor 183"
FT /id="PRO_0000383155"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 125..133
FT /note="Interaction with G proteins"
FT /evidence="ECO:0000250"
FT REGION 339..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 111
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 115
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 259
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U6B2"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 360 AA; 41179 MW; FBBDE30013127BAE CRC64;
MDIKMDNFTT PSAASLESDC DLYAHHHTAR ILMPLHYSIV FIIGLVGNLL ALIVIIQNRK
KINSTTLYST NLVISDILFT TALPTRIAYY ALGFDWRIGD ALCRITALVF YINTYAGVNF
MTCLSIDRFF AVVHPLRYNK IKRIEHAKCI CIFVWILVFG QTLPLLINPM SKQEAERTTC
MEYPNFEETK SLPWILLGAC FIGYVLPLVI ILICYSQICC KLFKTAKQNP LTEKSGVNKK
ALNTIIFIIV VFVVCFTPYH VAIIQHMIKK LRLPGLLECS QRHSFQISLH FTVCLMNFNC
CMDPFIYFFA CKGYKRKVMK MLKRQVSVSI SSAVRSAPEE NSREMTETQM MIHSKSLNGK
