LPAR6_MOUSE
ID LPAR6_MOUSE Reviewed; 344 AA.
AC Q8BMC0; A6H6N5; Q3TEJ6;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lysophosphatidic acid receptor 6;
DE Short=LPA receptor 6;
DE Short=LPA-6;
DE AltName: Full=Oleoyl-L-alpha-lysophosphatidic acid receptor;
DE AltName: Full=P2Y purinoceptor 5;
DE Short=P2Y5;
DE AltName: Full=Purinergic receptor 5;
GN Name=Lpar6; Synonyms=P2ry5, P2y5;
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, and NOD; TISSUE=Mesonephros, and Thymus;
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 MRNA].
RC TISSUE=Bone, Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18297070; DOI=10.1038/ng.84;
RA Pasternack S.M., von Kuegelgen I., Aboud K.A., Lee Y.-A., Rueschendorf F.,
RA Voss K., Hillmer A.M., Molderings G.J., Franz T., Ramirez A., Nuernberg P.,
RA Noethen M.M., Betz R.C.;
RT "G protein-coupled receptor P2Y5 and its ligand LPA are involved in
RT maintenance of human hair growth.";
RL Nat. Genet. 40:329-334(2008).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18297072; DOI=10.1038/ng.100;
RA Shimomura Y., Wajid M., Ishii Y., Shapiro L., Petukhova L., Gordon D.,
RA Christiano A.M.;
RT "Disruption of P2RY5, an orphan G protein-coupled receptor, underlies
RT autosomal recessive woolly hair.";
RL Nat. Genet. 40:335-339(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA).
CC Intracellular cAMP is involved in the receptor activation. Important
CC for the maintenance of hair growth and texture (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in the hair
CC follicles and skin (at protein level). {ECO:0000269|PubMed:18297070,
CC ECO:0000269|PubMed:18297072}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK032901; BAC28077.1; -; mRNA.
DR EMBL; AK169602; BAE41252.1; -; mRNA.
DR EMBL; BC145940; AAI45941.1; -; mRNA.
DR EMBL; BC145942; AAI45943.1; -; mRNA.
DR EMBL; BC069991; AAH69991.1; -; mRNA.
DR EMBL; BC047931; AAH47931.1; -; mRNA.
DR CCDS; CCDS27268.1; -.
DR RefSeq; NP_780325.1; NM_175116.4.
DR AlphaFoldDB; Q8BMC0; -.
DR SMR; Q8BMC0; -.
DR STRING; 10090.ENSMUSP00000042327; -.
DR GuidetoPHARMACOLOGY; 163; -.
DR SwissLipids; SLP:000001580; -.
DR GlyGen; Q8BMC0; 4 sites.
DR iPTMnet; Q8BMC0; -.
DR PhosphoSitePlus; Q8BMC0; -.
DR jPOST; Q8BMC0; -.
DR MaxQB; Q8BMC0; -.
DR PaxDb; Q8BMC0; -.
DR PRIDE; Q8BMC0; -.
DR ProteomicsDB; 292355; -.
DR Antibodypedia; 9381; 150 antibodies from 28 providers.
DR DNASU; 67168; -.
DR Ensembl; ENSMUST00000044405; ENSMUSP00000042327; ENSMUSG00000033446.
DR GeneID; 67168; -.
DR KEGG; mmu:67168; -.
DR UCSC; uc007upq.2; mouse.
DR CTD; 10161; -.
DR MGI; MGI:1914418; Lpar6.
DR VEuPathDB; HostDB:ENSMUSG00000033446; -.
DR eggNOG; ENOG502QSC2; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q8BMC0; -.
DR OMA; NMYGSML; -.
DR OrthoDB; 921450at2759; -.
DR PhylomeDB; Q8BMC0; -.
DR TreeFam; TF350009; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-417957; P2Y receptors.
DR BioGRID-ORCS; 67168; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Lpar6; mouse.
DR PRO; PR:Q8BMC0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BMC0; protein.
DR Bgee; ENSMUSG00000033446; Expressed in dorsal pancreas and 195 other tissues.
DR Genevisible; Q8BMC0; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IMP: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:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Lysophosphatidic acid receptor 6"
FT /id="PRO_0000070026"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 284
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 344 AA; 39439 MW; 50270D1D14AEDAB2 CRC64;
MVSSNGSQCP YDDSFKYTLY GCMFSMVFVL GLISNCVAIY IFICALKVRN ETTTYMINLA
MSDLLFVFTL PFRIFYFATR NWPFGDLLCK ISVMLFYTNM YGSILFLTCI SVDRFLAIVY
PFKSKTLRTK RNAKIVCIAV WFTVMGGSAP AVFFQSTHSQ GNNTSEACFE NFPAATWKTY
LSRIVIFIEI VGFFIPLILN VTCSSMVLRT LNKPVTLSRS KMNKTKVLKM IFVHLVIFCF
CFVPYNINLI LYSLMRTQTF VNCSVVAAVR TMYPITLCIA VSNCCFDPIV YYFTSDTIQN
SIKMKNWSVR RSDSRFSEVQ GTENFIQHNL QTLKNKIFDN ESAI
