GPR55_HUMAN
ID GPR55_HUMAN Reviewed; 319 AA.
AC Q9Y2T6; Q8N580;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=G-protein coupled receptor 55;
GN Name=GPR55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9931487; DOI=10.1016/s0169-328x(98)00277-0;
RA Sawzdargo M., Nguyen T., Lee D.K., Lynch K.R., Cheng R., Heng H.H.Q.,
RA George S.R., O'Dowd B.F.;
RT "Identification and cloning of three novel human G protein-coupled receptor
RT genes GPR52, PsiGPR53 and GPR55: GPR55 is extensively expressed in human
RT brain.";
RL Brain Res. Mol. Brain Res. 64:193-198(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [4]
RP LIGAND-BINDING.
RX PubMed=17765871; DOI=10.1016/j.bbrc.2007.08.078;
RA Oka S., Nakajima K., Yamashita A., Kishimoto S., Sugiura T.;
RT "Identification of GPR55 as a lysophosphatidylinositol receptor.";
RL Biochem. Biophys. Res. Commun. 362:928-934(2007).
RN [5]
RP SUBCELLULAR LOCATION, CHARACTERIZATION, AND LIGAND-BINDING.
RX PubMed=18757503; DOI=10.1096/fj.08-108670;
RA Henstridge C.M., Balenga N.A., Ford L.A., Ross R.A., Waldhoer M.,
RA Irving A.J.;
RT "The GPR55 ligand L-alpha-lysophosphatidylinositol promotes RhoA-dependent
RT Ca2+ signaling and NFAT activation.";
RL FASEB J. 23:183-193(2009).
RN [6]
RP LIGAND-BINDING.
RX PubMed=19723626; DOI=10.1074/jbc.m109.050187;
RA Kapur A., Zhao P., Sharir H., Bai Y., Caron M.G., Barak L.S., Abood M.E.;
RT "Atypical responsiveness of the orphan receptor GPR55 to cannabinoid
RT ligands.";
RL J. Biol. Chem. 284:29817-29827(2009).
RN [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19805329; DOI=10.1073/pnas.0902743106;
RA Whyte L.S., Ryberg E., Sims N.A., Ridge S.A., Mackie K., Greasley P.J.,
RA Ross R.A., Rogers M.J.;
RT "The putative cannabinoid receptor GPR55 affects osteoclast function in
RT vitro and bone mass in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16511-16516(2009).
CC -!- FUNCTION: May be involved in hyperalgesia associated with inflammatory
CC and neuropathic pain (By similarity). Receptor for L-alpha-
CC lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from
CC intracellular stores via the heterotrimeric G protein GNA13 and RHOA.
CC Putative cannabinoid receptor. May play a role in bone physiology by
CC regulating osteoclast number and function. {ECO:0000250,
CC ECO:0000269|PubMed:19805329}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18757503};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18757503}.
CC -!- TISSUE SPECIFICITY: Expressed in the caudate nucleus and putamen, but
CC not detected in the hippocampus, thalamus, pons cerebellum, frontal
CC cortex of the brain or in the liver. Expressed in osteoclasts and
CC osteoblasts. {ECO:0000269|PubMed:19805329, ECO:0000269|PubMed:9931487}.
CC -!- MISCELLANEOUS: The classification of this protein as a cannabinoid
CC receptor remains a contentious issue due to conflicting pharmacological
CC results.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22410.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF096786; AAD22410.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR541776; CAG46575.1; -; mRNA.
DR EMBL; BC032694; AAH32694.1; -; mRNA.
DR CCDS; CCDS2480.1; -.
DR RefSeq; NP_005674.2; NM_005683.3.
DR RefSeq; XP_005247009.1; XM_005246952.3.
DR RefSeq; XP_011510477.1; XM_011512175.2.
DR RefSeq; XP_011510478.1; XM_011512176.2.
DR AlphaFoldDB; Q9Y2T6; -.
DR SMR; Q9Y2T6; -.
DR BioGRID; 114705; 88.
DR IntAct; Q9Y2T6; 2.
DR STRING; 9606.ENSP00000375894; -.
DR BindingDB; Q9Y2T6; -.
DR ChEMBL; CHEMBL1075322; -.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB06155; Rimonabant.
DR DrugBank; DB11755; Tetrahydrocannabivarin.
DR DrugCentral; Q9Y2T6; -.
DR GuidetoPHARMACOLOGY; 109; -.
DR GlyGen; Q9Y2T6; 2 sites.
DR PhosphoSitePlus; Q9Y2T6; -.
DR BioMuta; GPR55; -.
DR DMDM; 71159390; -.
DR PaxDb; Q9Y2T6; -.
DR PeptideAtlas; Q9Y2T6; -.
DR PRIDE; Q9Y2T6; -.
DR ProteomicsDB; 85898; -.
DR Antibodypedia; 20197; 181 antibodies from 26 providers.
DR DNASU; 9290; -.
DR Ensembl; ENST00000392039.2; ENSP00000375893.2; ENSG00000135898.10.
DR Ensembl; ENST00000392040.5; ENSP00000375894.1; ENSG00000135898.10.
DR Ensembl; ENST00000444078.5; ENSP00000410267.1; ENSG00000135898.10.
DR Ensembl; ENST00000622008.4; ENSP00000482381.1; ENSG00000135898.10.
DR Ensembl; ENST00000650999.1; ENSP00000498258.1; ENSG00000135898.10.
DR GeneID; 9290; -.
DR KEGG; hsa:9290; -.
DR MANE-Select; ENST00000650999.1; ENSP00000498258.1; NM_005683.4; NP_005674.2.
DR UCSC; uc002vrf.4; human.
DR CTD; 9290; -.
DR DisGeNET; 9290; -.
DR GeneCards; GPR55; -.
DR HGNC; HGNC:4511; GPR55.
DR HPA; ENSG00000135898; Tissue enhanced (brain, lymphoid tissue, testis).
DR MIM; 604107; gene.
DR neXtProt; NX_Q9Y2T6; -.
DR OpenTargets; ENSG00000135898; -.
DR PharmGKB; PA28900; -.
DR VEuPathDB; HostDB:ENSG00000135898; -.
DR eggNOG; ENOG502QWNM; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR InParanoid; Q9Y2T6; -.
DR OMA; TCFHNMS; -.
DR OrthoDB; 981789at2759; -.
DR PhylomeDB; Q9Y2T6; -.
DR TreeFam; TF335700; -.
DR PathwayCommons; Q9Y2T6; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q9Y2T6; -.
DR SIGNOR; Q9Y2T6; -.
DR BioGRID-ORCS; 9290; 8 hits in 1058 CRISPR screens.
DR ChiTaRS; GPR55; human.
DR GeneWiki; GPR55; -.
DR GenomeRNAi; 9290; -.
DR Pharos; Q9Y2T6; Tclin.
DR PRO; PR:Q9Y2T6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2T6; protein.
DR Bgee; ENSG00000135898; Expressed in monocyte and 86 other tissues.
DR ExpressionAtlas; Q9Y2T6; baseline and differential.
DR Genevisible; Q9Y2T6; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0004949; F:cannabinoid receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0045453; P:bone resorption; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR028334; GPR55.
DR PANTHER; PTHR24232:SF56; PTHR24232:SF56; 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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..319
FT /note="G-protein coupled receptor 55"
FT /id="PRO_0000069577"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 195
FT /note="G -> V (in dbSNP:rs3749073)"
FT /id="VAR_024257"
FT VARIANT 215
FT /note="T -> N (in dbSNP:rs34229723)"
FT /id="VAR_049395"
SQ SEQUENCE 319 AA; 36637 MW; D6E5C6CA8426E7D5 CRC64;
MSQQNTSGDC LFDGVNELMK TLQFAVHIPT FVLGLLLNLL AIHGFSTFLK NRWPDYAATS
IYMINLAVFD LLLVLSLPFK MVLSQVQSPF PSLCTLVECL YFVSMYGSVF TICFISMDRF
LAIRYPLLVS HLRSPRKIFG ICCTIWVLVW TGSIPIYSFH GKVEKYMCFH NMSDDTWSAK
VFFPLEVFGF LLPMGIMGFC CSRSIHILLG RRDHTQDWVQ QKACIYSIAA SLAVFVVSFL
PVHLGFFLQF LVRNSFIVEC RAKQSISFFL QLSMCFSNVN CCLDVFCYYF VIKEFRMNIR
AHRPSRVQLV LQDTTISRG
