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Q99MT7 (GPR87_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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 87
Gene names
Name:Gpr87
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for lysophosphatidic acid (LPA). Necessary for p53/TP53-dependent survival in response to DNA damage By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed at high levels in testis and brain and to a lesser extent placenta, ovary, prostate, and skeletal muscle but not in heart, lung, kidney, liver or intestine. Ref.3

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358G-protein coupled receptor 87
PRO_0000069596

Regions

Topological domain1 – 4747Extracellular Potential
Transmembrane48 – 6821Helical; Name=1; Potential
Topological domain69 – 757Cytoplasmic Potential
Transmembrane76 – 9621Helical; Name=2; Potential
Topological domain97 – 11620Extracellular Potential
Transmembrane117 – 13721Helical; Name=3; Potential
Topological domain138 – 15922Cytoplasmic Potential
Transmembrane160 – 18021Helical; Name=4; Potential
Topological domain181 – 20828Extracellular Potential
Transmembrane209 – 22921Helical; Name=5; Potential
Topological domain230 – 25627Cytoplasmic Potential
Transmembrane257 – 27721Helical; Name=6; Potential
Topological domain278 – 29720Extracellular Potential
Transmembrane298 – 31821Helical; Name=7; Potential
Topological domain319 – 35840Cytoplasmic Potential

Amino acid modifications

Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation331N-linked (GlcNAc...) Potential
Disulfide bond114 ↔ 192 By similarity

Experimental info

Sequence conflict1 – 1111MGLNLTLTKLP → MAVPNVNVSTFA Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99MT7 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: 6D258E98CB3BE4B9

FASTA35841,414
        10         20         30         40         50         60 
MGLNLTLTKL PGNELYSQAS HTANSTSEGH GKNSTLHNKF DTIILPVLYL VIFVASILLN 

        70         80         90        100        110        120 
GLAVWIFFHI RNKTSFIFYL KNIVVADLIM TLTFPFRIVR DAGFGPWYFE FILCRYTSVL 

       130        140        150        160        170        180 
FYANMYTSIV FLGLISVDRY LKVVKPFGDS RMYSITFTKV LSVCVWVIMA ILSLPNIILT 

       190        200        210        220        230        240 
NGQPTKENIH DCMKLKSPLG AKWHMAVTYV DSCLFVAVLV ILIGCYIAIS RYIHKSSRQF 

       250        260        270        280        290        300 
ISQSSRKRKH NQSIRVVVAV FFTCFLPYHL CRIPFTFSNL DRLLDESAHK ILYYCKEMTL 

       310        320        330        340        350 
FLSACNVCLD PIIYFFMCKS FSRRLFKKSN IRTRSESIRS LQSVRRSEVR IYYDYTDV 

« Hide

References

« Hide 'large scale' references
[1]"An expressed sequence tag (EST) data mining strategy succeeding in the discovery of new G-protein coupled receptors."
Wittenberger T., Schaller H.C., Hellebrand S.
J. Mol. Biol. 307:799-813(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Thymus.
[3]"The orphan GPCR GPR87 was deorphanized and shown to be a lysophosphatidic acid receptor."
Tabata K., Baba K., Shiraishi A., Ito M., Fujita N.
Biochem. Biophys. Res. Commun. 363:861-866(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF295366 mRNA. Translation: AAK01866.1.
AK080394 mRNA. Translation: BAC37905.1.
RefSeqNP_115775.1. NM_032399.1.
XP_006502456.1. XM_006502393.1.
UniGeneMm.60267.

3D structure databases

ProteinModelPortalQ99MT7.
SMRQ99MT7. Positions 38-327.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY122.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ99MT7.

Proteomic databases

PRIDEQ99MT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID84111.
KEGGmmu:84111.
UCSCuc008pip.1. mouse.

Organism-specific databases

CTD53836.
MGIMGI:1934133. Gpr87.

Phylogenomic databases

eggNOGNOG146234.
HOVERGENHBG108228.
InParanoidQ99MT7.
KOK08389.
PhylomeDBQ99MT7.

Gene expression databases

CleanExMM_GPR87.
GenevestigatorQ99MT7.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR008109. P2Y13_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01735. P2Y13PRNCPTR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350890.
PROQ99MT7.
SOURCESearch...

Entry information

Entry nameGPR87_MOUSE
AccessionPrimary (citable) accession number: Q99MT7
Secondary accession number(s): Q8C4Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 100 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