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GPR18_BOVIN
ID   GPR18_BOVIN             Reviewed;         332 AA.
AC   Q3T0E9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=N-arachidonyl glycine receptor;
DE            Short=NAGly receptor;
DE   AltName: Full=G-protein coupled receptor 18;
GN   Name=GPR18;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for endocannabinoid N-arachidonyl glycine (NAGly).
CC       However, conflicting results about the role of NAGly as an agonist are
CC       reported. Can also be activated by plant-derived and synthetic
CC       cannabinoid agonists. The activity of this receptor is mediated by G
CC       proteins which inhibit adenylyl cyclase. May contribute to regulation
CC       of the immune system. Is required for normal homeostasis of CD8+
CC       subsets of intraepithelial lymphocytes (IELs) (CD8alphaalpha and
CC       CD8alphabeta IELs) in small intstine by supporting preferential
CC       migration of CD8 alphaalpha T-cells to intraepithelial compartment over
CC       lamina propria compartment, and by mediating their reconstitution into
CC       small intestine after bone marrow transplant. Plays a role in
CC       hypotensive responses, mediating reduction in intraocular and blood
CC       pressure. Mediates NAGly-induced process of reorganization of actin
CC       filaments and induction of acrosomal exocytosis.
CC       {ECO:0000250|UniProtKB:Q14330, ECO:0000250|UniProtKB:Q8K1Z6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14330};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q14330}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; BC102421; AAI02422.1; -; mRNA.
DR   RefSeq; NP_001029861.1; NM_001034689.2.
DR   AlphaFoldDB; Q3T0E9; -.
DR   SMR; Q3T0E9; -.
DR   STRING; 9913.ENSBTAP00000007469; -.
DR   PaxDb; Q3T0E9; -.
DR   PRIDE; Q3T0E9; -.
DR   Ensembl; ENSBTAT00000007469; ENSBTAP00000007469; ENSBTAG00000002240.
DR   GeneID; 540038; -.
DR   KEGG; bta:540038; -.
DR   CTD; 2841; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002240; -.
DR   VGNC; VGNC:29574; GPR18.
DR   eggNOG; ENOG502QT1V; Eukaryota.
DR   GeneTree; ENSGT01050000244980; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q3T0E9; -.
DR   OMA; CYLVIIY; -.
DR   OrthoDB; 1122184at2759; -.
DR   TreeFam; TF330775; -.
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; ENSBTAG00000002240; Expressed in semen and 80 other tissues.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0002300; P:CD8-positive, alpha-beta intraepithelial T cell differentiation; IEA:Ensembl.
DR   GO; GO:0002305; P:CD8-positive, gamma-delta intraepithelial T cell differentiation; IEA:Ensembl.
DR   GO; GO:0002689; P:negative regulation of leukocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR028335; GPR18.
DR   PANTHER; PTHR24232:SF1; PTHR24232:SF1; 1.
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   Cell membrane; Cytoplasmic vesicle; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..332
FT                   /note="N-arachidonyl glycine receptor"
FT                   /id="PRO_0000245013"
FT   TOPO_DOM        1..26
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1Z6"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   332 AA;  37949 MW;  C536851A24AE803B CRC64;
     MTTPHSQAQP GLPIDPHPDE YKVAALVFYS CIFIIGLFVN VTALWVFSCT TKKRTTVTVY
     MMNVALLDLV FIMSLPFRML YYAKGEWPFG EYFCRILGAL TVFYPSIALW LLAFISADRY
     MAIVQPKYAK ELKNTCKAVM ACVGVWIMTL TTTIPLLLLY EDPDTASSTP PTCLKISDII
     YLKAINALNF TRLIFFFLIP LFIMIGCYLV IIHSLLHGKT SKLKPKVKEK SIRIIITLMV
     QVLVCFMPFH ICFAFLMLGG DENSYNPWGA FTTFLMNLST CLDVILYYIV SKQFQARVIS
     VMLYRNYLRS VRRKSFRSGS LRSLSNINSE ML
 
 
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