ID   LIPH_HUMAN              Reviewed;         451 AA.
AC   Q8WWY8; A2IBA7; Q8TEC7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Lipase member H;
DE            Short=LIPH;
DE            EC=3.1.1.- {ECO:0000269|PubMed:12963729};
DE   AltName: Full=LPD lipase-related protein;
DE   AltName: Full=Membrane-associated phosphatidic acid-selective phospholipase A1-alpha;
DE            Short=mPA-PLA1 alpha;
DE   AltName: Full=Phospholipase A1 member B;
DE   Flags: Precursor;
GN   Name=LIPH; Synonyms=LPDLR, MPAPLA1, PLA1B;
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 [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-154.
RX   PubMed=12063250; DOI=10.1074/jbc.m201659200;
RA   Sonoda H., Aoki J., Hiramatsu T., Ishida M., Bandoh K., Nagai Y.,
RA   Taguchi R., Inoue K., Arai H.;
RT   "A novel phosphatidic acid-selective phospholipase A1 that produces
RT   lysophosphatidic acid.";
RL   J. Biol. Chem. 277:34254-34263(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12213196; DOI=10.1006/geno.2002.6837;
RA   Jin W., Broedl U., Monajemi H., Glick J., Rader D.;
RT   "Lipase h, a new member of the triglyceride lipase family synthesized by
RT   the intestine.";
RL   Genomics 80:268-273(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT HYPT7 172-GLY--HIS-205 DEL, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Pancreas;
RX   PubMed=17095700; DOI=10.1126/science.1133276;
RA   Kazantseva A., Goltsov A., Zinchenko R., Grigorenko A.P., Abrukova A.V.,
RA   Moliaka Y.K., Kirillov A.G., Guo Z., Lyle S., Ginter E.K., Rogaev E.I.;
RT   "Human hair growth deficiency is linked to a genetic defect in the
RT   phospholipase gene LIPH.";
RL   Science 314:982-985(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=12719377; DOI=10.1093/hmg/ddg124;
RA   Wen X.-Y., Hegele R.A., Wang J., Wang D.Y., Cheung J., Wilson M.,
RA   Yahyapour M., Bai Y., Zhuang L., Skaug J., Young T.K., Connelly P.W.,
RA   Koop B.F., Tsui L.-C., Stewart A.K.;
RT   "Identification of a novel lipase gene mutated in lpd mice with
RT   hypertriglyceridemia and associated with dyslipidemia in humans.";
RL   Hum. Mol. Genet. 12:1131-1143(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12963729; DOI=10.1074/jbc.m213018200;
RA   Hiramatsu T., Sonoda H., Takanezawa Y., Morikawa R., Ishida M.,
RA   Kasahara K., Sanai Y., Taguchi R., Aoki J., Arai H.;
RT   "Biochemical and molecular characterization of two phosphatidic acid-
RT   selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.";
RL   J. Biol. Chem. 278:49438-49447(2003).
RN   [9]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH TTMP.
RX   PubMed=32336749; DOI=10.1038/s41436-020-0794-5;
RA   Malki L., Sarig O., Cesarato N., Mohamad J., Canter T., Assaf S.,
RA   Pavlovsky M., Vodo D., Anis Y., Bihari O., Malovitski K., Gat A.,
RA   Thiele H., White B.E.P., Samuelov L., Nanda A., Paller A.S., Betz R.C.,
RA   Sprecher E.;
RT   "Loss-of-function variants in C3ORF52 result in localized autosomal
RT   recessive hypotrichosis.";
RL   Genet. Med. 22:1227-1234(2020).
RN   [10]
RP   VARIANT HYPT7 ARG-108.
RX   PubMed=19167195; DOI=10.1016/j.jdermsci.2008.12.001;
RA   Naz G., Khan B., Ali G., Azeem Z., Wali A., Ansar M., Ahmad W.;
RT   "Novel missense mutations in lipase H (LIPH) gene causing autosomal
RT   recessive hypotrichosis (LAH2).";
RL   J. Dermatol. Sci. 54:12-16(2009).
RN   [11]
RP   VARIANT ARWH2 ARG-108.
RX   PubMed=18830268; DOI=10.1038/jid.2008.290;
RA   Shimomura Y., Wajid M., Petukhova L., Shapiro L., Christiano A.M.;
RT   "Mutations in the lipase H gene underlie autosomal recessive woolly
RT   hair/hypotrichosis.";
RL   J. Invest. Dermatol. 129:622-628(2009).
RN   [12]
RP   VARIANT ARWH2 ARG-108.
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   [13]
RP   VARIANT ARWH2 230-GLN--LEU-451 DEL.
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).
CC   -!- FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-
CC       acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and
CC       fatty acid. Does not hydrolyze other phospholipids, like
CC       phosphatidylserine (PS), phosphatidylcholine (PC) and
CC       phosphatidylethanolamine (PE) or triacylglycerol (TG).
CC       {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12963729}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC         H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839,
CC         ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:12963729};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944;
CC         Evidence={ECO:0000305|PubMed:12963729};
CC   -!- ACTIVITY REGULATION: Inhibited by sodium vanadate.
CC       {ECO:0000269|PubMed:12963729}.
CC   -!- SUBUNIT: Interacts with TTMP/C3orf52. {ECO:0000269|PubMed:32336749}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12963729}. Cell
CC       membrane {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12963729};
CC       Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Present in intestine (at protein level). Expressed
CC       in colon, prostate, kidney, pancreas, ovary, testis, intestine, lung
CC       and pancreas. Expressed at lower level in brain, spleen and heart. In
CC       the skin, it is prominently expressed in hair follicles, including the
CC       stem cell-rich bulge region and the inner root sheath (PubMed:17095700,
CC       PubMed:32336749). {ECO:0000269|PubMed:12063250,
CC       ECO:0000269|PubMed:12213196, ECO:0000269|PubMed:12719377,
CC       ECO:0000269|PubMed:17095700, ECO:0000269|PubMed:32336749}.
CC   -!- DISEASE: Hypotrichosis 7 (HYPT7) [MIM:604379]: A condition
CC       characterized by the presence of less than the normal amount of hair.
CC       Affected individuals have sparse or absent scalp, axillary and body
CC       hair and sparse eyebrows and eyelashes. HYPT7 inheritance is autosomal
CC       recessive. {ECO:0000269|PubMed:17095700, ECO:0000269|PubMed:19167195}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Woolly hair autosomal recessive 2 (ARWH2) [MIM:604379]: A hair
CC       shaft disorder characterized by fine and tightly curled hair. Compared
CC       to normal curly hair that is observed in some populations, woolly hair
CC       grows slowly and stops growing after a few inches. Under light
CC       microscopy, woolly hair shows some structural anomalies, including
CC       trichorrhexis nodosa and tapered ends. Some individuals may present
CC       with hypotrichosis. {ECO:0000269|PubMed:18830268,
CC       ECO:0000269|PubMed:21426374, ECO:0000269|PubMed:28425126}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB85023.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY036912; AAK63178.1; -; mRNA.
DR   EMBL; AY093498; AAM18803.1; -; mRNA.
DR   EMBL; EF186229; ABM67095.1; -; mRNA.
DR   EMBL; AK074229; BAB85023.1; ALT_INIT; mRNA.
DR   EMBL; AK122651; BAG53642.1; -; mRNA.
DR   EMBL; CH471052; EAW78218.1; -; Genomic_DNA.
DR   EMBL; BC064941; AAH64941.1; -; mRNA.
DR   CCDS; CCDS3272.1; -.
DR   RefSeq; NP_640341.1; NM_139248.2.
DR   AlphaFoldDB; Q8WWY8; -.
DR   SMR; Q8WWY8; -.
DR   BioGRID; 128352; 98.
DR   IntAct; Q8WWY8; 26.
DR   STRING; 9606.ENSP00000296252; -.
DR   SwissLipids; SLP:000000625; -.
DR   ESTHER; human-LIPH; Phospholipase.
DR   GlyCosmos; Q8WWY8; 3 sites, No reported glycans.
DR   GlyGen; Q8WWY8; 3 sites.
DR   iPTMnet; Q8WWY8; -.
DR   PhosphoSitePlus; Q8WWY8; -.
DR   BioMuta; LIPH; -.
DR   DMDM; 74762634; -.
DR   EPD; Q8WWY8; -.
DR   MassIVE; Q8WWY8; -.
DR   PaxDb; 9606-ENSP00000296252; -.
DR   PeptideAtlas; Q8WWY8; -.
DR   ProteomicsDB; 74960; -.
DR   Antibodypedia; 33838; 99 antibodies from 23 providers.
DR   DNASU; 200879; -.
DR   Ensembl; ENST00000296252.9; ENSP00000296252.4; ENSG00000163898.10.
DR   GeneID; 200879; -.
DR   KEGG; hsa:200879; -.
DR   MANE-Select; ENST00000296252.9; ENSP00000296252.4; NM_139248.3; NP_640341.1.
DR   UCSC; uc003fpm.4; human.
DR   AGR; HGNC:18483; -.
DR   CTD; 200879; -.
DR   DisGeNET; 200879; -.
DR   GeneCards; LIPH; -.
DR   HGNC; HGNC:18483; LIPH.
DR   HPA; ENSG00000163898; Tissue enhanced (intestine, stomach).
DR   MalaCards; LIPH; -.
DR   MIM; 604379; phenotype.
DR   MIM; 607365; gene.
DR   neXtProt; NX_Q8WWY8; -.
DR   OpenTargets; ENSG00000163898; -.
DR   Orphanet; 55654; Hypotrichosis simplex.
DR   Orphanet; 170; Woolly hair.
DR   PharmGKB; PA134934352; -.
DR   VEuPathDB; HostDB:ENSG00000163898; -.
DR   eggNOG; ENOG502QUQT; Eukaryota.
DR   GeneTree; ENSGT00940000156285; -.
DR   HOGENOM; CLU_027171_3_0_1; -.
DR   InParanoid; Q8WWY8; -.
DR   OMA; DALHTDM; -.
DR   OrthoDB; 3428256at2759; -.
DR   PhylomeDB; Q8WWY8; -.
DR   TreeFam; TF324997; -.
DR   BRENDA; 3.1.1.32; 2681.
DR   PathwayCommons; Q8WWY8; -.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   SignaLink; Q8WWY8; -.
DR   SIGNOR; Q8WWY8; -.
DR   BioGRID-ORCS; 200879; 9 hits in 1151 CRISPR screens.
DR   ChiTaRS; LIPH; human.
DR   GeneWiki; LIPH; -.
DR   GenomeRNAi; 200879; -.
DR   Pharos; Q8WWY8; Tbio.
DR   PRO; PR:Q8WWY8; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8WWY8; Protein.
DR   Bgee; ENSG00000163898; Expressed in buccal mucosa cell and 132 other cell types or tissues.
DR   ExpressionAtlas; Q8WWY8; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   PANTHER; PTHR11610:SF12; LIPASE MEMBER H; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q8WWY8; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW   Heparin-binding; Hydrolase; Hypotrichosis; Lipid degradation;
KW   Lipid metabolism; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..451
FT                   /note="Lipase member H"
FT                   /id="PRO_0000273321"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        233..246
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..281
FT                   /evidence="ECO:0000250"
FT   DISULFID        284..292
FT                   /evidence="ECO:0000250"
FT   DISULFID        427..446
FT                   /evidence="ECO:0000250"
FT   VARIANT         108
FT                   /note="W -> R (in HYPT7 and ARWH2; dbSNP:rs267607219)"
FT                   /evidence="ECO:0000269|PubMed:18830268,
FT                   ECO:0000269|PubMed:19167195, ECO:0000269|PubMed:21426374"
FT                   /id="VAR_059050"
FT   VARIANT         172..205
FT                   /note="Missing (in HYPT7)"
FT                   /evidence="ECO:0000269|PubMed:17095700"
FT                   /id="VAR_030125"
FT   VARIANT         230..451
FT                   /note="Missing (in ARWH2)"
FT                   /evidence="ECO:0000269|PubMed:28425126"
FT                   /id="VAR_088344"
FT   MUTAGEN         154
FT                   /note="S->A: Loss of lipase activity."
FT                   /evidence="ECO:0000269|PubMed:12063250"
SQ   SEQUENCE   451 AA;  50859 MW;  949CE32B0C15868B CRC64;
     MLRFYLFISL LCLSRSDAEE TCPSFTRLSF HSAVVGTGLN VRLMLYTRKN LTCAQTINSS
     AFGNLNVTKK TTFIVHGFRP TGSPPVWMDD LVKGLLSVED MNVVVVDWNR GATTLIYTHA
     SSKTRKVAMV LKEFIDQMLA EGASLDDIYM IGVSLGAHIS GFVGEMYDGW LGRITGLDPA
     GPLFNGKPHQ DRLDPSDAQF VDVIHSDTDA LGYKEPLGNI DFYPNGGLDQ PGCPKTILGG
     FQYFKCDHQR SVYLYLSSLR ESCTITAYPC DSYQDYRNGK CVSCGTSQKE SCPLLGYYAD
     NWKDHLRGKD PPMTKAFFDT AEESPFCMYH YFVDIITWNK NVRRGDITIK LRDKAGNTTE
     SKINHEPTTF QKYHQVSLLA RFNQDLDKVA AISLMFSTGS LIGPRYKLRI LRMKLRSLAH
     PERPQLCRYD LVLMENVETV FQPILCPELQ L
//