Q8BMC0 (LPAR6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	G-protein coupled purinergic nucleotide receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Lysophosphatidic acid receptor 6		PRO_0000070026
Regions
	Topological domain	1 – 25	25	Extracellular Potential
	Transmembrane	26 – 46	21	Helical; Name=1; Potential
	Topological domain	47 – 56	10	Cytoplasmic Potential
	Transmembrane	57 – 77	21	Helical; Name=2; Potential
	Topological domain	78 – 90	13	Extracellular Potential
	Transmembrane	91 – 111	21	Helical; Name=3; Potential
	Topological domain	112 – 134	23	Cytoplasmic Potential
	Transmembrane	135 – 155	21	Helical; Name=4; Potential
	Topological domain	156 – 183	28	Extracellular Potential
	Transmembrane	184 – 204	21	Helical; Name=5; Potential
	Topological domain	205 – 230	26	Cytoplasmic Potential
	Transmembrane	231 – 251	21	Helical; Name=6; Potential
	Topological domain	252 – 272	21	Extracellular Potential
	Transmembrane	273 – 293	21	Helical; Name=7; Potential
	Topological domain	294 – 344	51	Cytoplasmic Potential
Amino acid modifications
	Lipidation	284	1	S-palmitoyl cysteine By similarity
	Glycosylation	5	1	N-linked (GlcNAc...) Potential
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	163	1	N-linked (GlcNAc...) Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Disulfide bond	89 ↔ 168		Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8BMC0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 50270D1D14AEDAB2	FASTA	344	39,439
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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: 18297070] [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: 18297072] [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.
IPI	IPI00222991.
RefSeq	NP_780325.1. NM_175116.4.
UniGene	Mm.390681.
3D structure databases
ProteinModelPortal	Q8BMC0.
SMR	Q8BMC0. Positions 17-307.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BMC0.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	Q8BMC0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000044405; ENSMUSP00000042327; ENSMUSG00000033446.
GeneID	67168.
KEGG	mmu:67168.
UCSC	uc007upq.2. mouse.
Organism-specific databases
CTD	10161.
MGI	MGI:1914418. Lpar6.
Phylogenomic databases
eggNOG	maNOG14545.
GeneTree	ENSGT00590000082782.
HOGENOM	HBG714985.
HOVERGEN	HBG101917.
InParanoid	Q8BMC0.
OMA	LYSLMRT.
OrthoDB	EOG4Q58PX.
PhylomeDB	Q8BMC0.
Gene expression databases
ArrayExpress	Q8BMC0.
Bgee	Q8BMC0.
CleanEx	MM_P2RY5.
Genevestigator	Q8BMC0.
GermOnline	ENSMUSG00000033446. Mus musculus.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_supfam. IPR002188. P2Y5_purnocptor. [Graphical view]
KO	K04273.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR01067. P2Y5ORPHANR.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	323782.
SOURCE	Search...

Entry information

Entry name

LPAR6_MOUSE

Accession

Primary (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:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program