GPR55_MOUSE
ID GPR55_MOUSE Reviewed; 327 AA.
AC Q3UJF0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=G-protein coupled receptor 55;
GN Name=Gpr55; Synonyms=Gm218;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18502582; DOI=10.1016/j.pain.2008.04.006;
RA Staton P.C., Hatcher J.P., Walker D.J., Morrison A.D., Shapland E.M.,
RA Hughes J.P., Chong E., Mander P.K., Green P.J., Billinton A.,
RA Fulleylove M., Lancaster H.C., Smith J.C., Bailey L.T., Wise A.,
RA Brown A.J., Richardson J.C., Chessell I.P.;
RT "The putative cannabinoid receptor GPR55 plays a role in mechanical
RT hyperalgesia associated with inflammatory and neuropathic pain.";
RL Pain 139:225-236(2008).
CC -!- FUNCTION: Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI
CC induces Ca(2+) release from intracellular stores via the heterotrimeric
CC G protein GNA13 and RHOA (By similarity). Putative cannabinoid receptor
CC (By similarity). May play a role in bone physiology by regulating
CC osteoclast number and function (By similarity). May be involved in
CC hyperalgesia associated with inflammatory and neuropathic pain.
CC {ECO:0000250, ECO:0000269|PubMed:18502582}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are resistant to mechanical
CC hyperalgesia and have increased levels of anti-inflammatory cytokines.
CC {ECO:0000269|PubMed:18502582}.
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}.
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DR EMBL; AK146484; BAE27205.1; -; mRNA.
DR EMBL; AC102506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15115.1; -.
DR RefSeq; NP_001028462.2; NM_001033290.2.
DR RefSeq; XP_006529526.1; XM_006529463.3.
DR RefSeq; XP_017175826.1; XM_017320337.1.
DR AlphaFoldDB; Q3UJF0; -.
DR SMR; Q3UJF0; -.
DR STRING; 10090.ENSMUSP00000084196; -.
DR GlyGen; Q3UJF0; 2 sites.
DR iPTMnet; Q3UJF0; -.
DR PhosphoSitePlus; Q3UJF0; -.
DR PaxDb; Q3UJF0; -.
DR PRIDE; Q3UJF0; -.
DR ProteomicsDB; 271275; -.
DR Antibodypedia; 20197; 181 antibodies from 26 providers.
DR Ensembl; ENSMUST00000086975; ENSMUSP00000084196; ENSMUSG00000049608.
DR GeneID; 227326; -.
DR KEGG; mmu:227326; -.
DR UCSC; uc007buq.1; mouse.
DR CTD; 9290; -.
DR MGI; MGI:2685064; Gpr55.
DR VEuPathDB; HostDB:ENSMUSG00000049608; -.
DR eggNOG; ENOG502QWNM; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q3UJF0; -.
DR OMA; TCFHNMS; -.
DR OrthoDB; 981789at2759; -.
DR PhylomeDB; Q3UJF0; -.
DR TreeFam; TF335700; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 227326; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q3UJF0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UJF0; protein.
DR Bgee; ENSMUSG00000049608; Expressed in jejunum and 25 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004949; F:cannabinoid receptor activity; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO: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:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS: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 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..327
FT /note="G-protein coupled receptor 55"
FT /id="PRO_0000233978"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 226..231
FT /note="WVQKRA -> LGTKREP (in Ref. 1; BAE27205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 38090 MW; 4B33F94E3CCAEA1C CRC64;
MSQPERDNCS FDSVDKLTRT LQLAVHIPTF LLGLVLNLLA IRGFSAFLKK RKLDYIATSI
YMINLAVFDL LLVLSLPFKM VLPQVESPLP SFCTLVECLY FISMYGSVFT ICFISLDRFL
AIQYPILASH LRSPRKTFGI CCIIWMLVWI GSIPIYTFHR EVERYKCFHN MSDVTWSASV
FFPLEIFGFL LPMGIMGFCS YRSIHILLRR PDSTEDWVQQ RDTKGWVQKR ACIWTIATNL
VIFVVSFLPV HLGFFLQYLV RNRFILDCRM KQGISLFLQL SLCFSNINCC LDVFCYYFVI
KEFRMRIKAH RPSTIKLVNQ DTMVSRG
