ID LPAR6_HUMAN Reviewed; 344 AA.
AC P43657; A4FTW9; B3KVF2; F2YGU4; O15133; Q3KPF5; Q53FA0; Q5VW44; Q7Z3S0;
AC Q7Z3S6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 3.
DT 24-JAN-2024, entry version 190.
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;
DE AltName: Full=RB intron encoded G-protein coupled receptor;
GN Name=LPAR6; Synonyms=P2RY5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7902321; DOI=10.1006/geno.1993.1368;
RA Toguchida J., McGee T.L., Paterson J.C., Eagle J.R., Tucker S.,
RA Yandell D.W., Dryja T.P.;
RT "Complete genomic sequence of the human retinoblastoma susceptibility
RT gene.";
RL Genomics 17:535-543(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8889552; DOI=10.1101/gr.6.9.858;
RA Herzog H., Darby K., Hort Y.J., Shine J.;
RT "Intron 17 of the human retinoblastoma susceptibility gene encodes an
RT actively transcribed G protein-coupled receptor gene.";
RL Genome Res. 6:858-861(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bohm S.K., Trumpp A., Khitin L.M., Kong W., Payan D.G., Bunnett N.W.;
RT "The human purinergic receptor P2Y5 is encoded in intron 17 of the
RT retinoblastoma gene.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium, and Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Peripheral blood leukocyte;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-137.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Placenta, and Testis;
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 [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11004484; DOI=10.1016/s0167-4781(00)00094-4;
RA Adrian K., Bernhard M.K., Breitinger H.-G., Ogilvie A.;
RT "Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic
RT P2Y1-11) during myeloid differentiation of HL60 cells.";
RL Biochim. Biophys. Acta 1492:127-138(2000).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN
RP HYPT8.
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 [14]
RP VARIANT ARWH1 TYR-278.
RX PubMed=18692127; DOI=10.1016/j.ygeno.2008.06.009;
RA Petukhova L., Sousa E.C. Jr., Martinez-Mir A., Vitebsky A.,
RA Dos Santos L.G., Shapiro L., Haynes C., Gordon D., Shimomura Y.,
RA Christiano A.M.;
RT "Genome-wide linkage analysis of an autosomal recessive hypotrichosis
RT identifies a novel P2RY5 mutation.";
RL Genomics 92:273-278(2008).
RN [15]
RP VARIANTS HYPT8 THR-3; VAL-63; ARG-146 AND LYS-189, AND INVOLVEMENT IN
RP HYPT8.
RX PubMed=18461368; DOI=10.1007/s00439-008-0507-7;
RA Azeem Z., Jelani M., Naz G., Tariq M., Wasif N., Kamran-Ul-Hassan Naqvi S.,
RA Ayub M., Yasinzai M., Amin-Ud-Din M., Wali A., Ali G., Chishti M.S.,
RA Ahmad W.;
RT "Novel mutations in G protein-coupled receptor gene (P2RY5) in families
RT with autosomal recessive hypotrichosis (LAH3).";
RL Hum. Genet. 123:515-519(2008).
RN [16]
RP VARIANTS ARWH1 VAL-63; PHE-188 AND LYS-189, AND 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 [17]
RP VARIANTS HYPT8 VAL-63; ARG-146; PHE-188; TYR-248 AND PRO-277.
RX PubMed=19292720; DOI=10.1111/j.1365-2133.2009.09046.x;
RA Tariq M., Ayub M., Jelani M., Basit S., Naz G., Wasif N., Raza S.I.,
RA Naveed A.K., ullah Khan S., Azeem Z., Yasinzai M., Wali A., Ali G.,
RA Chishti M.S., Ahmad W.;
RT "Mutations in the P2RY5 gene underlie autosomal recessive hypotrichosis in
RT 13 Pakistani families.";
RL Br. J. Dermatol. 160:1006-1010(2009).
RN [18]
RP VARIANT HYPT8 LEU-196.
RX PubMed=21070332; DOI=10.1111/j.1365-2230.2010.03944.x;
RA Nahum S., Morice-Picard F., Taieb A., Sprecher E.;
RT "A novel mutation in LPAR6 causes autosomal recessive hypotrichosis of the
RT scalp.";
RL Clin. Exp. Dermatol. 36:188-194(2011).
RN [19]
RP VARIANTS ARWH1 VAL-63 AND PHE-188, AND VARIANT HYPT8 ARG-146.
RX PubMed=21426374; DOI=10.1111/j.1365-2230.2011.04014.x;
RA Khan S., Habib R., Mir H., Kalsoom U., Naz G., Ayub M., Shafique S.,
RA Yamin T., Ali N., Basit S., Wasif N., Kamran-Ul-Hassan Naqvi S., Ali G.,
RA Wali A., Ansar M., Ahmad W.;
RT "Mutations in the LPAR6 and LIPH genes underlie autosomal recessive
RT hypotrichosis/woolly hair in 17 consanguineous families from Pakistan.";
RL Clin. Exp. Dermatol. 36:652-654(2011).
RN [20]
RP VARIANT ARWH1 VAL-63.
RX PubMed=28425126; DOI=10.1111/cga.12226;
RA Ahmad F., Sharif S., Furqan Ubaid M., Shah K., Khan M.N., Umair M.,
RA Azeem Z., Ahmad W.;
RT "Novel sequence variants in the LIPH and LPAR6 genes underlies autosomal
RT recessive woolly hair/hypotrichosis in consanguineous families.";
RL Congenit. Anom. (Kyoto) 58:24-28(2018).
RN [21]
RP CHARACTERIZATION OF VARIANTS HYPT8 THR-3; ARG-146; TYR-248 AND PRO-277,
RP CHARACTERIZATION OF VARIANTS ARWH1 VAL-63; PHE-188; LYS-189 AND TYR-278,
RP MUTAGENESIS OF ASN-246, AND SUBCELLULAR LOCATION.
RX PubMed=36173926; DOI=10.1093/hmg/ddac244;
RA Yanagida K., Masago K., Yasuda D., Hamano F., Kurikawa Y., Shimizu T.,
RA Ishii S.;
RT "Cell-trafficking impairment in disease-associated LPA6 missense mutants
RT and a potential pharmacoperone therapy for autosomal recessive woolly
RT hair/hypotrichosis.";
RL Hum. Mol. Genet. 32:825-834(2023).
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.
CC {ECO:0000269|PubMed:18297070}.
CC -!- INTERACTION:
CC P43657; P54849: EMP1; NbExp=3; IntAct=EBI-2876949, EBI-4319440;
CC P43657; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2876949, EBI-1052363;
CC P43657; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2876949, EBI-8652744;
CC P43657; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-2876949, EBI-741850;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18297070,
CC ECO:0000269|PubMed:36173926}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18297070}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, including in skin and hair
CC follicle cells. Detected in both Henle's and Huxley's layers of the
CC inner root sheath of the hair follicle and in suprabasal layers of the
CC epidermis (at protein level). Expressed at low levels in peripheral
CC blood leukocytes. {ECO:0000269|PubMed:11004484,
CC ECO:0000269|PubMed:18297070, ECO:0000269|PubMed:18297072}.
CC -!- DEVELOPMENTAL STAGE: Markedly up-regulated in promyelocytic HL60 cells
CC induced to differentiate along the monocyte/macrophage pathway. Not
CC detectable in undifferentiated HL60 cells and only low levels after the
CC induction of differentiation along the granulocytic pathway.
CC {ECO:0000269|PubMed:11004484}.
CC -!- DISEASE: Woolly hair autosomal recessive 1 with or without
CC hypotrichosis (ARWH1) [MIM:278150]: A hair shaft disorder characterized
CC by fine and tightly curled hair. Compared to normal curly hair that is
CC observed in some populations, woolly hair grows slowly and stops
CC growing after a few inches. Under light microscopy, woolly hair shows
CC some structural anomalies, including trichorrhexis nodosa and tapered
CC ends. Some individuals exhibit features of hypotrichosis.
CC {ECO:0000269|PubMed:18297070, ECO:0000269|PubMed:18297072,
CC ECO:0000269|PubMed:18461368, ECO:0000269|PubMed:18692127,
CC ECO:0000269|PubMed:21426374, ECO:0000269|PubMed:28425126,
CC ECO:0000269|PubMed:36173926}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Hypotrichosis 8 (HYPT8) [MIM:278150]: A condition
CC characterized by the presence of less than the normal amount of hair
CC and abnormal hair follicles and shafts, which are thin and atrophic.
CC The disorder affects the trunk and extremities as well as the scalp,
CC and the eyebrows and eyelashes may also be involved, whereas beard,
CC pubic, and axillary hairs are largely spared. In addition, patients can
CC develop hyperkeratotic follicular papules, erythema, and pruritus in
CC affected areas. In some patients with congenital hypotrichosis,
CC monilethrix-like hairs showing elliptical nodes have been observed.
CC HYPT8 inheritance is autosomal recessive. {ECO:0000269|PubMed:18297070,
CC ECO:0000269|PubMed:18461368, ECO:0000269|PubMed:19292720,
CC ECO:0000269|PubMed:21070332, ECO:0000269|PubMed:21426374,
CC ECO:0000269|PubMed:36173926}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This is a nested gene within intron 17 of the
CC retinoblastoma gene.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L11910; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L11910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L78805; AAL40065.1; -; Genomic_DNA.
DR EMBL; AF000546; AAB62190.1; -; mRNA.
DR EMBL; BX537392; CAD97634.1; -; mRNA.
DR EMBL; BX537438; CAD97680.1; -; mRNA.
DR EMBL; BX537445; CAD97687.1; -; mRNA.
DR EMBL; AK122856; BAG53764.1; -; mRNA.
DR EMBL; AK223389; BAD97109.1; -; mRNA.
DR EMBL; HQ995530; ADZ31975.1; -; mRNA.
DR EMBL; JF810890; AEP43757.1; -; mRNA.
DR EMBL; AF551763; AAN64134.1; -; Genomic_DNA.
DR EMBL; AL392048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08796.1; -; Genomic_DNA.
DR EMBL; BC040850; AAH40850.1; -; mRNA.
DR EMBL; BC045651; AAH45651.1; -; mRNA.
DR EMBL; BC070295; AAH70295.1; -; mRNA.
DR EMBL; BC106756; AAI06757.1; -; mRNA.
DR CCDS; CCDS9410.1; -.
DR PIR; T09508; T09508.
DR RefSeq; NP_001155969.1; NM_001162497.1.
DR RefSeq; NP_001155970.1; NM_001162498.1.
DR RefSeq; NP_005758.2; NM_005767.5.
DR AlphaFoldDB; P43657; -.
DR SMR; P43657; -.
DR BioGRID; 115463; 67.
DR IntAct; P43657; 36.
DR MINT; P43657; -.
DR STRING; 9606.ENSP00000367691; -.
DR BindingDB; P43657; -.
DR ChEMBL; CHEMBL2331058; -.
DR DrugBank; DB01069; Promethazine.
DR GuidetoPHARMACOLOGY; 163; -.
DR SwissLipids; SLP:000001579; -.
DR GlyCosmos; P43657; 1 site, No reported glycans.
DR GlyGen; P43657; 1 site.
DR iPTMnet; P43657; -.
DR PhosphoSitePlus; P43657; -.
DR BioMuta; LPAR6; -.
DR DMDM; 34223726; -.
DR MassIVE; P43657; -.
DR PaxDb; 9606-ENSP00000367691; -.
DR PeptideAtlas; P43657; -.
DR ProteomicsDB; 55648; -.
DR Antibodypedia; 9381; 169 antibodies from 28 providers.
DR DNASU; 10161; -.
DR Ensembl; ENST00000345941.2; ENSP00000344353.2; ENSG00000139679.16.
DR Ensembl; ENST00000378434.8; ENSP00000367691.3; ENSG00000139679.16.
DR Ensembl; ENST00000620633.5; ENSP00000482660.1; ENSG00000139679.16.
DR GeneID; 10161; -.
DR KEGG; hsa:10161; -.
DR MANE-Select; ENST00000620633.5; ENSP00000482660.1; NM_001162498.3; NP_001155970.1.
DR UCSC; uc001vce.4; human.
DR AGR; HGNC:15520; -.
DR CTD; 10161; -.
DR DisGeNET; 10161; -.
DR GeneCards; LPAR6; -.
DR HGNC; HGNC:15520; LPAR6.
DR HPA; ENSG00000139679; Low tissue specificity.
DR MalaCards; LPAR6; -.
DR MIM; 278150; phenotype.
DR MIM; 609239; gene.
DR neXtProt; NX_P43657; -.
DR OpenTargets; ENSG00000139679; -.
DR Orphanet; 55654; Hypotrichosis simplex.
DR Orphanet; 170; Woolly hair.
DR PharmGKB; PA165505129; -.
DR VEuPathDB; HostDB:ENSG00000139679; -.
DR eggNOG; ENOG502QSC2; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P43657; -.
DR OMA; NMYGSML; -.
DR OrthoDB; 5351855at2759; -.
DR PhylomeDB; P43657; -.
DR TreeFam; TF350009; -.
DR PathwayCommons; P43657; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-417957; P2Y receptors.
DR SignaLink; P43657; -.
DR SIGNOR; P43657; -.
DR BioGRID-ORCS; 10161; 12 hits in 1112 CRISPR screens.
DR ChiTaRS; LPAR6; human.
DR GenomeRNAi; 10161; -.
DR Pharos; P43657; Tchem.
DR PRO; PR:P43657; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P43657; Protein.
DR Bgee; ENSG00000139679; Expressed in gingival epithelium and 181 other cell types or tissues.
DR ExpressionAtlas; P43657; baseline and differential.
DR Genevisible; P43657; HS.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0070915; F:lysophosphatidic acid receptor activity; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd15156; 7tmA_LPAR6_P2Y5; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24232:SF3; LYSOPHOSPHATIDIC ACID RECEPTOR 6; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01067; P2Y5ORPHANR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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; Disease variant; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Hypotrichosis; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Lysophosphatidic acid receptor 6"
FT /id="PRO_0000070025"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..253
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..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 DISULFID 89..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 3
FT /note="S -> T (in HYPT8; uncertain significance; no effect
FT on G protein-coupled receptor signaling; no effect on
FT localization to cell membrane; does not affect protein
FT abundance)"
FT /evidence="ECO:0000269|PubMed:18461368,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_088338"
FT VARIANT 33
FT /note="I -> V (in dbSNP:rs1060585)"
FT /id="VAR_022636"
FT VARIANT 63
FT /note="D -> V (in ARWH1 and HYPT8; loss of G protein-
FT coupled receptor signaling; reduced localization to cell
FT membrane; decreased protein abundance; increased protein
FT degradation; dbSNP:rs879255262)"
FT /evidence="ECO:0000269|PubMed:18297072,
FT ECO:0000269|PubMed:18461368, ECO:0000269|PubMed:19292720,
FT ECO:0000269|PubMed:21426374, ECO:0000269|PubMed:28425126,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_044326"
FT VARIANT 137
FT /note="C -> W (in dbSNP:rs4151553)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_016253"
FT VARIANT 146
FT /note="G -> R (in HYPT8; loss of G protein-coupled receptor
FT signaling; reduced localization to cell membrane; decreased
FT protein abundance; increased protein degradation)"
FT /evidence="ECO:0000269|PubMed:18461368,
FT ECO:0000269|PubMed:19292720, ECO:0000269|PubMed:21426374,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_088339"
FT VARIANT 188
FT /note="I -> F (in ARWH1 and HYPT8; loss of G protein-
FT coupled receptor signaling; no effect on localization to
FT cell membrane; does not affect protein abundance;
FT dbSNP:rs121434307)"
FT /evidence="ECO:0000269|PubMed:18297072,
FT ECO:0000269|PubMed:19292720, ECO:0000269|PubMed:21426374,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_044327"
FT VARIANT 189
FT /note="E -> K (in ARWH1 and HYPT8; loss of G protein-
FT coupled receptor signaling; no effect on localization to
FT cell membrane; does not affect protein abundance;
FT dbSNP:rs121434309)"
FT /evidence="ECO:0000269|PubMed:18297072,
FT ECO:0000269|PubMed:18461368, ECO:0000269|PubMed:36173926"
FT /id="VAR_044328"
FT VARIANT 196
FT /note="P -> L (in HYPT8; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:21070332"
FT /id="VAR_088340"
FT VARIANT 248
FT /note="N -> Y (in HYPT8; loss of G protein-coupled receptor
FT signaling; no effect on localization to cell membrane; does
FT not affect protein abundance)"
FT /evidence="ECO:0000269|PubMed:19292720,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_088341"
FT VARIANT 277
FT /note="L -> P (in HYPT8; loss of G protein-coupled receptor
FT signaling; reduced localization to cell membrane; decreased
FT protein abundance; increased protein degradation)"
FT /evidence="ECO:0000269|PubMed:19292720,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_088342"
FT VARIANT 278
FT /note="C -> Y (in ARWH1; loss of G protein-coupled receptor
FT signaling; reduced localization to cell membrane; decreased
FT protein abundance; increased protein degradation)"
FT /evidence="ECO:0000269|PubMed:18692127,
FT ECO:0000269|PubMed:36173926"
FT /id="VAR_088343"
FT VARIANT 307
FT /note="W -> C (in dbSNP:rs17071686)"
FT /id="VAR_049430"
FT MUTAGEN 246
FT /note="N->D: Loss of G protein-coupled receptor signaling.
FT Reduced localization to cell membrane. Decreased protein
FT abundance. Increased protein degradation."
FT /evidence="ECO:0000269|PubMed:36173926"
FT CONFLICT 242
FT /note="F -> I (in Ref. 6; BAD97109)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="K -> I (in Ref. 4; CAD97680)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> G (in Ref. 4; CAD97687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 39392 MW; 699212F3C1249433 CRC64;
MVSVNSSHCF YNDSFKYTLY GCMFSMVFVL GLISNCVAIY IFICVLKVRN ETTTYMINLA
MSDLLFVFTL PFRIFYFTTR NWPFGDLLCK ISVMLFYTNM YGSILFLTCI SVDRFLAIVY
PFKSKTLRTK RNAKIVCTGV WLTVIGGSAP AVFVQSTHSQ GNNASEACFE NFPEATWKTY
LSRIVIFIEI VGFFIPLILN VTCSSMVLKT LTKPVTLSRS KINKTKVLKM IFVHLIIFCF
CFVPYNINLI LYSLVRTQTF VNCSVVAAVR TMYPITLCIA VSNCCFDPIV YYFTSDTIQN
SIKMKNWSVR RSDFRFSEVH GAENFIQHNL QTLKSKIFDN ESAA
//
