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Q8BMC0 (LPAR6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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:
Lysophosphatidic acid receptor 6

Short name=LPA receptor 6
Short name=LPA-6
Alternative name(s):
Oleoyl-L-alpha-lysophosphatidic acid receptor
P2Y purinoceptor 5
Short name=P2Y5
Purinergic receptor 5
Gene names
Name:Lpar6
Synonyms:P2ry5, P2y5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Ubiquitously expressed. Detected in the hair follicles and skin (at protein level). Ref.3 Ref.4

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Lysophosphatidic acid receptor 6
PRO_0000070026

Regions

Topological domain1 – 2525Extracellular Potential
Transmembrane26 – 4621Helical; Name=1; Potential
Topological domain47 – 5610Cytoplasmic Potential
Transmembrane57 – 7721Helical; Name=2; Potential
Topological domain78 – 9013Extracellular Potential
Transmembrane91 – 11121Helical; Name=3; Potential
Topological domain112 – 13423Cytoplasmic Potential
Transmembrane135 – 15521Helical; Name=4; Potential
Topological domain156 – 18328Extracellular Potential
Transmembrane184 – 20421Helical; Name=5; Potential
Topological domain205 – 23026Cytoplasmic Potential
Transmembrane231 – 25121Helical; Name=6; Potential
Topological domain252 – 27221Extracellular Potential
Transmembrane273 – 29321Helical; Name=7; Potential
Topological domain294 – 34451Cytoplasmic Potential

Amino acid modifications

Lipidation2841S-palmitoyl cysteine By similarity
Glycosylation51N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Disulfide bond89 ↔ 168 Potential

Sequences

Sequence LengthMass (Da)Tools
Q8BMC0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 50270D1D14AEDAB2

FASTA34439,439
        10         20         30         40         50         60 
MVSSNGSQCP YDDSFKYTLY GCMFSMVFVL GLISNCVAIY IFICALKVRN ETTTYMINLA 

        70         80         90        100        110        120 
MSDLLFVFTL PFRIFYFATR NWPFGDLLCK ISVMLFYTNM YGSILFLTCI SVDRFLAIVY 

       130        140        150        160        170        180 
PFKSKTLRTK RNAKIVCIAV WFTVMGGSAP AVFFQSTHSQ GNNTSEACFE NFPAATWKTY 

       190        200        210        220        230        240 
LSRIVIFIEI VGFFIPLILN VTCSSMVLRT LNKPVTLSRS KMNKTKVLKM IFVHLVIFCF 

       250        260        270        280        290        300 
CFVPYNINLI LYSLMRTQTF VNCSVVAAVR TMYPITLCIA VSNCCFDPIV YYFTSDTIQN 

       310        320        330        340 
SIKMKNWSVR RSDSRFSEVQ GTENFIQHNL QTLKNKIFDN ESAI 

« 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 and NOD.
Tissue: Mesonephros and Thymus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone, Brain and Mammary gland.
[3]"G protein-coupled receptor P2Y5 and its ligand LPA are involved in maintenance of human hair growth."
Pasternack S.M., von Kuegelgen I., Aboud K.A., Lee Y.-A., Rueschendorf F., Voss K., Hillmer A.M., Molderings G.J., Franz T., Ramirez A., Nuernberg P., Noethen M.M., Betz R.C.
Nat. Genet. 40:329-334(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Disruption of P2RY5, an orphan G protein-coupled receptor, underlies autosomal recessive woolly hair."
Shimomura Y., Wajid M., Ishii Y., Shapiro L., Petukhova L., Gordon D., Christiano A.M.
Nat. Genet. 40:335-339(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK032901 mRNA. Translation: BAC28077.1.
AK169602 mRNA. Translation: BAE41252.1.
BC145940 mRNA. Translation: AAI45941.1.
BC145942 mRNA. Translation: AAI45943.1.
BC069991 mRNA. Translation: AAH69991.1.
BC047931 mRNA. Translation: AAH47931.1.
CCDSCCDS27268.1.
RefSeqNP_780325.1. NM_175116.4.
UniGeneMm.390681.

3D structure databases

ProteinModelPortalQ8BMC0.
SMRQ8BMC0. Positions 23-300.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY163.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ8BMC0.

Proteomic databases

PRIDEQ8BMC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044405; ENSMUSP00000042327; ENSMUSG00000033446.
GeneID67168.
KEGGmmu:67168.
UCSCuc007upq.2. mouse.

Organism-specific databases

CTD10161.
MGIMGI:1914418. Lpar6.

Phylogenomic databases

eggNOGNOG289230.
GeneTreeENSGT00750000117402.
HOGENOMHOG000231307.
HOVERGENHBG101917.
InParanoidQ8BMC0.
KOK04273.
OMAFRIFYFA.
OrthoDBEOG71VSSZ.
PhylomeDBQ8BMC0.
TreeFamTF350009.

Gene expression databases

BgeeQ8BMC0.
CleanExMM_P2RY5.
GenevestigatorQ8BMC0.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
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

NextBio323782.
PROQ8BMC0.
SOURCESearch...

Entry information

Entry nameLPAR6_MOUSE
AccessionPrimary (citable) accession number: Q8BMC0
Secondary accession number(s): A6H6N5, Q3TEJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 96 of the entry and version 1 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