GPR18_RAT
ID GPR18_RAT Reviewed; 331 AA.
AC A1A5S3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=N-arachidonyl glycine receptor;
DE Short=NAGly receptor;
DE AltName: Full=G-protein coupled receptor 18;
GN Name=Gpr18 {ECO:0000312|EMBL:AAI28783.1};
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] {ECO:0000312|EMBL:AAI28783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI28783.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24431468; DOI=10.1124/jpet.113.209213;
RA Penumarti A., Abdel-Rahman A.A.;
RT "The novel endocannabinoid receptor GPR18 is expressed in the rostral
RT ventrolateral medulla and exerts tonic restraining influence on blood
RT pressure.";
RL J. Pharmacol. Exp. Ther. 349:29-38(2014).
CC -!- FUNCTION: Receptor for endocannabinoid N-arachidonyl glycine (NAGly)
CC (PubMed:24431468). However, conflicting results about the role of NAGly
CC as an agonist are reported (By similarity). Can also be activated by
CC plant-derived and synthetic cannabinoid agonists (PubMed:24431468). The
CC activity of this receptor is mediated by G proteins which inhibit
CC adenylyl cyclase (By similarity). May contribute to regulation of the
CC immune system (By similarity). Is required for normal homeostasis of
CC CD8+ 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 (By similarity). Plays a
CC role in hypotensive responses, mediating reduction in intraocular and
CC blood pressure (PubMed:24431468). Mediates NAGly-induced process of
CC reorganization of actin filaments and induction of acrosomal exocytosis
CC (By similarity). {ECO:0000250|UniProtKB:Q14330,
CC ECO:0000250|UniProtKB:Q8K1Z6, ECO:0000269|PubMed:24431468}.
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 -!- TISSUE SPECIFICITY: Expressed in testis, spleen and brain (at protein
CC level). {ECO:0000269|PubMed:24431468}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC128782; AAI28783.1; -; mRNA.
DR RefSeq; NP_001073178.1; NM_001079710.1.
DR AlphaFoldDB; A1A5S3; -.
DR SMR; A1A5S3; -.
DR STRING; 10116.ENSRNOP00000016848; -.
DR GlyGen; A1A5S3; 2 sites.
DR iPTMnet; A1A5S3; -.
DR PhosphoSitePlus; A1A5S3; -.
DR PaxDb; A1A5S3; -.
DR Ensembl; ENSRNOT00000016848; ENSRNOP00000016848; ENSRNOG00000012628.
DR GeneID; 679957; -.
DR KEGG; rno:679957; -.
DR CTD; 2841; -.
DR RGD; 1304889; Gpr18.
DR eggNOG; ENOG502QT1V; Eukaryota.
DR GeneTree; ENSGT01050000244980; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; A1A5S3; -.
DR OMA; CYLVIIY; -.
DR OrthoDB; 1122184at2759; -.
DR PhylomeDB; A1A5S3; -.
DR TreeFam; TF330775; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:A1A5S3; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000012628; Expressed in spleen and 11 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; ISO:RGD.
DR GO; GO:0002305; P:CD8-positive, gamma-delta intraepithelial T cell differentiation; ISO:RGD.
DR GO; GO:0002689; P:negative regulation of leukocyte chemotaxis; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
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 1: Evidence at protein 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_0000278175"
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..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..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; 37556 MW; F33341AA4FCC67C2 CRC64;
MAIPSNRDQL ALSNGSHPEE YKIAALVFYS CIFLIGLLVN VTALWVFSCT TKKRTTVTIY
MMNVALLDLV FILSLPFRMF YYAKGEWPFG DYFCHILGAL VVFYPSLALW LLALISADRY
MAIVQPKYAK ELKNTGKAVL ACVGVWIMTL TTTVPLLLLD EDPDKASSPA TCLKISDIIH
LKAVNVLNFT RLIFFFLIPL FIMIGCYVVI IHSLLRGQTS KLKPKVKEKS IRIIVTLLLQ
VLACFVPFHI CFALLMLQGE ENSYSPWGAF TTFLMNLSTC LDVVLYYIVS KQFQARVISV
MLYRNYLRSV RRKSVRSGSL RSLSNMNSEM L
