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Database: UniProt
Entry: Q8K1Z6
LinkDB: Q8K1Z6
Original site: Q8K1Z6 
ID   GPR18_MOUSE             Reviewed;         331 AA.
AC   Q8K1Z6; Q3T9N3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   15-MAR-2017, entry version 120.
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:AAH34872.1, ECO:0000312|MGI:MGI:107859};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:BAE42987.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD {ECO:0000312|EMBL:BAE42987.1};
RC   TISSUE=Spleen {ECO:0000312|EMBL:BAE42987.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000312|EMBL:AAH34872.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH34872.1};
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH34872.1};
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23461720; DOI=10.1111/bph.12136;
RA   Caldwell M.D., Hu S.S., Viswanathan S., Bradshaw H., Kelly M.E.,
RA   Straiker A.;
RT   "A GPR18-based signalling system regulates IOP in murine eye.";
RL   Br. J. Pharmacol. 169:834-843(2013).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23104136; DOI=10.1124/mol.112.081182;
RA   Lu V.B., Puhl H.L. III, Ikeda S.R.;
RT   "N-Arachidonyl glycine does not activate G protein-coupled receptor 18
RT   signaling via canonical pathways.";
RL   Mol. Pharmacol. 83:267-282(2013).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25348153; DOI=10.1084/jem.20140646;
RA   Wang X., Sumida H., Cyster J.G.;
RT   "GPR18 is required for a normal CD8alphaalpha intestinal
RT   intraepithelial lymphocyte compartment.";
RL   J. Exp. Med. 211:2351-2359(2014).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=26197390; DOI=10.1371/journal.pone.0133854;
RA   Becker A.M., Callahan D.J., Richner J.M., Choi J., DiPersio J.F.,
RA   Diamond M.S., Bhattacharya D.;
RT   "GPR18 controls reconstitution of mouse small intestine
RT   intraepithelial lymphocytes following bone marrow transplantation.";
RL   PLoS ONE 10:E0133854-E0133854(2015).
RN   [8]
RP   FUNCTION.
RX   PubMed=27893106; DOI=10.1167/iovs.16-19437;
RA   Miller S., Leishman E., Oehler O., Daily L., Murataeva N.,
RA   Wager-Miller J., Bradshaw H., Straiker A.;
RT   "Evidence for a GPR18 role in diurnal regulation of intraocular
RT   pressure.";
RL   Invest. Ophthalmol. Vis. Sci. 57:6419-6426(2016).
CC   -!- FUNCTION: Receptor for endocannabinoid N-arachidonyl glycine
CC       (NAGly) (By similarity). However, conflicting results about the
CC       role of NAGly as an agonist are reported (PubMed:23104136). Can
CC       also be activated by plant-derived and synthetic cannabinoid
CC       agonists (By similarity). The activity of this receptor is
CC       mediated by G proteins which inhibit adenylyl cyclase (By
CC       similarity). May contribute to regulation of the immune system (By
CC       similarity). Is required for normal homeostasis of CD8+ subsets of
CC       intraepithelial lymphocytes (IELs) (CD8alphaalpha and CD8alphabeta
CC       IELs) in small intstine by supporting preferential migration of
CC       CD8alphaalpha T-cells to intraepithelial compartment over lamina
CC       propria compartment, and by mediating their reconstitution into
CC       small intestine after bone marrow transplant (PubMed:25348153,
CC       PubMed:26197390). Plays a role in hypotensive responses, mediating
CC       reduction in intraocular and blood pressure (PubMed:23461720,
CC       PubMed:27893106). Mediates NAGly-induced process of reorganization
CC       of actin filaments and induction of acrosomal exocytosis (By
CC       similarity). {ECO:0000250|UniProtKB:Q14330,
CC       ECO:0000269|PubMed:23104136, ECO:0000269|PubMed:23461720,
CC       ECO:0000269|PubMed:25348153, ECO:0000269|PubMed:26197390,
CC       ECO:0000269|PubMed:27893106}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23104136};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle
CC       membrane {ECO:0000250|UniProtKB:Q14330}.
CC   -!- TISSUE SPECIFICITY: Expressed in the eye including cornea, retina,
CC       iris and ciliary epithelium (at protein level) (PubMed:23461720).
CC       Expressed in spleen, liver and lymphocytes with highest expression
CC       levels in intestinal intraepithelial lymphocytes (PubMed:25348153,
CC       PubMed:26197390). {ECO:0000269|PubMed:23461720,
CC       ECO:0000269|PubMed:25348153, ECO:0000269|PubMed:26197390}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:26197390).
CC       However, reduced number of CD8alphaalpha gammadeltaT IELs has been
CC       reported (PubMed:25348153). {ECO:0000269|PubMed:25348153,
CC       ECO:0000269|PubMed:26197390}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
DR   EMBL; AK156039; BAE33557.1; -; mRNA.
DR   EMBL; AK156868; BAE33880.1; -; mRNA.
DR   EMBL; AK157029; BAE33938.1; -; mRNA.
DR   EMBL; AK172401; BAE42987.1; -; mRNA.
DR   EMBL; BC034872; AAH34872.1; -; mRNA.
DR   CCDS; CCDS27342.1; -.
DR   RefSeq; NP_877958.1; NM_182806.1.
DR   UniGene; Mm.37405; -.
DR   ProteinModelPortal; Q8K1Z6; -.
DR   STRING; 10090.ENSMUSP00000061410; -.
DR   iPTMnet; Q8K1Z6; -.
DR   PhosphoSitePlus; Q8K1Z6; -.
DR   PaxDb; Q8K1Z6; -.
DR   PRIDE; Q8K1Z6; -.
DR   Ensembl; ENSMUST00000055475; ENSMUSP00000061410; ENSMUSG00000050350.
DR   GeneID; 110168; -.
DR   KEGG; mmu:110168; -.
DR   UCSC; uc007vap.1; mouse.
DR   CTD; 2841; -.
DR   MGI; MGI:107859; Gpr18.
DR   eggNOG; ENOG410IFPC; Eukaryota.
DR   eggNOG; ENOG410YP7X; LUCA.
DR   GeneTree; ENSGT00730000110768; -.
DR   HOGENOM; HOG000112785; -.
DR   HOVERGEN; HBG105013; -.
DR   InParanoid; Q8K1Z6; -.
DR   KO; K08410; -.
DR   OMA; YAKGEWP; -.
DR   OrthoDB; EOG091G0BF1; -.
DR   PhylomeDB; Q8K1Z6; -.
DR   TreeFam; TF330775; -.
DR   Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   PRO; PR:Q8K1Z6; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000050350; -.
DR   CleanEx; MM_GPR18; -.
DR   Genevisible; Q8K1Z6; MM.
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; IDA:MGI.
DR   GO; GO:0002305; P:CD8-positive, gamma-delta intraepithelial T cell differentiation; IDA:MGI.
DR   GO; GO:0002689; P:negative regulation of leukocyte chemotaxis; IMP:MGI.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
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:SF70; PTHR24232:SF70; 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; Complete proteome; 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       N-arachidonyl glycine receptor.
FT                                /FTId=PRO_0000278174.
FT   TOPO_DOM      1     26       Extracellular. {ECO:0000255}.
FT   TRANSMEM     27     47       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     48     56       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     57     77       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM     78     95       Extracellular. {ECO:0000255}.
FT   TRANSMEM     96    116       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    117    138       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    139    159       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    160    191       Extracellular. {ECO:0000255}.
FT   TRANSMEM    192    212       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    213    236       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    237    257       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    258    268       Extracellular. {ECO:0000255}.
FT   TRANSMEM    269    289       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    290    331       Cytoplasmic. {ECO:0000255}.
FT   MOD_RES     322    322       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD     14     14       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    188    188       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     94    172       {ECO:0000255|PROSITE-ProRule:PRU00521}.
FT   CONFLICT     23     23       I -> V (in Ref. 1; BAE42987).
FT                                {ECO:0000305}.
SQ   SEQUENCE   331 AA;  37691 MW;  702FD55C911B4787 CRC64;
     MATLSNHNQL DLSNGSHPEE YKIAALVFYS CIFLIGLFVN VTALWVFSCT TKKRTTVTIY
     MMNVALLDLV FILSLPFRMF YYAKGEWPFG EYFCHILGAL VVFYPSLALW LLAFISADRY
     MAIVQPKYAK ELKNTGKAVL ACGGVWVMTL TTTVPLLLLY EDPDKASSPA TCLKISDITH
     LKAVNVLNFT RLIFFFLIPL FIMIGCYVVI IHSLLRGQTS KLKPKVKEKS IRIIMTLLLQ
     VLVCFVPFHI CFAVLMLQGQ ENSYSPWGAF TTFLMNLSTC LDVVLYYIVS KQFQARVISV
     MLYRNYLRSV RRKSVRSGSL RSLSNMNSEM L
//
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