GPR18_MACFA
ID GPR18_MACFA Reviewed; 331 AA.
AC Q4R613;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=N-arachidonyl glycine receptor;
DE Short=NAGly receptor;
DE AltName: Full=G-protein coupled receptor 18;
GN Name=GPR18 {ECO:0000250|UniProtKB:Q14330}; ORFNames=QtsA-19357;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000312|EMBL:BAE01462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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 CD8alphaalpha 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; AB169378; BAE01462.1; -; mRNA.
DR RefSeq; NP_001270660.1; NM_001283731.1.
DR AlphaFoldDB; Q4R613; -.
DR SMR; Q4R613; -.
DR STRING; 9541.XP_005586213.1; -.
DR GeneID; 101926488; -.
DR CTD; 2841; -.
DR eggNOG; ENOG502QT1V; Eukaryota.
DR OrthoDB; 1122184at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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..331
FT /note="N-arachidonyl glycine receptor"
FT /id="PRO_0000278173"
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..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1Z6"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 331 AA; 38137 MW; 4BAF34F307BB72EB CRC64;
MITLNNQDQP VPFNNSYPDE YEIAALVFYS CIFIIGLFVN ITALWVFSCT TKKRTTVTIY
MMNVALVDLI FIMTLPFRMF YYAKDEWPFG EYFCQILGAL TVFYPSIALW LLAFISADRY
MAIVQPKYAK ELKNTCKAVL ACVGVWIMTL TTTIPLLLLH KDPDKDSTPA TCLKISDIVY
LKAVNVLNFT RLTFFFLIPL FIMIGCYLVI IHNLLHGRTS KLKPKVKEKS IRIIITLLVQ
VLVCFMPFHI CFAFLMLGTG ENSYSPWGAF TTFLMNLSTC LDVILYYIVS KQFQARVISV
MLYRNYLRGM RRKSFRSGSL RSLSNINSEM L
