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Q3UJF0 (GPR55_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein coupled receptor 55
Gene names
Name:Gpr55
Synonyms:Gm218
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI induces Ca2+ release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA By similarity. Putative cannabinoid receptor By similarity. May play a role in bone physiology by regulating osteoclast number and function By similarity. May be involved in hyperalgesia associated with inflammatory and neuropathic pain. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Disruption phenotype

Mutant mice are resistant to mechanical hyperalgesia and have increased levels of anti-inflammatory cytokines. Ref.3

Miscellaneous

The classification of this protein as a cannabinoid receptor remains a contentious issue due to conflicting pharmacological results.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327G-protein coupled receptor 55
PRO_0000233978

Regions

Topological domain1 – 2020Extracellular Potential
Transmembrane21 – 4121Helical; Name=1; Potential
Topological domain42 – 5716Cytoplasmic Potential
Transmembrane58 – 7821Helical; Name=2; Potential
Topological domain79 – 9315Extracellular Potential
Transmembrane94 – 11421Helical; Name=3; Potential
Topological domain115 – 13622Cytoplasmic Potential
Transmembrane137 – 15721Helical; Name=4; Potential
Topological domain158 – 17922Extracellular Potential
Transmembrane180 – 20021Helical; Name=5; Potential
Topological domain201 – 23939Cytoplasmic Potential
Transmembrane240 – 26021Helical; Name=6; Potential
Topological domain261 – 27919Extracellular Potential
Transmembrane280 – 30021Helical; Name=7; Potential
Topological domain301 – 32727Cytoplasmic Potential

Amino acid modifications

Glycosylation81N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict226 – 2316WVQKRA → LGTKREP in BAE27205. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UJF0 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 4B33F94E3CCAEA1C

FASTA32738,090
        10         20         30         40         50         60 
MSQPERDNCS FDSVDKLTRT LQLAVHIPTF LLGLVLNLLA IRGFSAFLKK RKLDYIATSI 

        70         80         90        100        110        120 
YMINLAVFDL LLVLSLPFKM VLPQVESPLP SFCTLVECLY FISMYGSVFT ICFISLDRFL 

       130        140        150        160        170        180 
AIQYPILASH LRSPRKTFGI CCIIWMLVWI GSIPIYTFHR EVERYKCFHN MSDVTWSASV 

       190        200        210        220        230        240 
FFPLEIFGFL LPMGIMGFCS YRSIHILLRR PDSTEDWVQQ RDTKGWVQKR ACIWTIATNL 

       250        260        270        280        290        300 
VIFVVSFLPV HLGFFLQYLV RNRFILDCRM KQGISLFLQL SLCFSNINCC LDVFCYYFVI 

       310        320 
KEFRMRIKAH RPSTIKLVNQ DTMVSRG 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The putative cannabinoid receptor GPR55 plays a role in mechanical hyperalgesia associated with inflammatory and neuropathic pain."
Staton P.C., Hatcher J.P., Walker D.J., Morrison A.D., Shapland E.M., Hughes J.P., Chong E., Mander P.K., Green P.J., Billinton A., Fulleylove M., Lancaster H.C., Smith J.C., Bailey L.T., Wise A., Brown A.J., Richardson J.C., Chessell I.P.
Pain 139:225-236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK146484 mRNA. Translation: BAE27205.1.
AC102506 Genomic DNA. No translation available.
AC107707 Genomic DNA. No translation available.
CCDSCCDS15115.1.
RefSeqNP_001028462.2. NM_001033290.2.
XP_006529525.1. XM_006529462.1.
XP_006529526.1. XM_006529463.1.
UniGeneMm.244158.

3D structure databases

ProteinModelPortalQ3UJF0.
SMRQ3UJF0. Positions 9-308.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY109.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ3UJF0.

Proteomic databases

PRIDEQ3UJF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086975; ENSMUSP00000084196; ENSMUSG00000049608.
GeneID227326.
KEGGmmu:227326.

Organism-specific databases

CTD9290.
MGIMGI:2685064. Gpr55.

Phylogenomic databases

eggNOGNOG145477.
GeneTreeENSGT00730000110768.
HOGENOMHOG000013155.
HOVERGENHBG096388.
InParanoidQ3UJF0.
KOK08413.
OMACFHNMSD.
OrthoDBEOG7327PC.
TreeFamTF335700.

Gene expression databases

CleanExMM_GPR55.
GenevestigatorQ3UJF0.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR028334. GPR55.
[Graphical view]
PANTHERPTHR24232:SF8. PTHR24232:SF8. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ3UJF0.
SOURCESearch...

Entry information

Entry nameGPR55_MOUSE
AccessionPrimary (citable) accession number: Q3UJF0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries