ID   LIPH_XENTR              Reviewed;         460 AA.
AC   Q5XGE9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Lipase member H;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=liph;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-
CC       acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and
CC       fatty acid (By similarity). Does not hydrolyze other phospholipids,
CC       like phosphatidylserine (PS), phosphatidylcholine (PC) and
CC       phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WWY8}.
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:0000250|UniProtKB:Q8WWY8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944;
CC         Evidence={ECO:0000250|UniProtKB:Q8WWY8};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8WWY8}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8WWY8}; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; BC084493; AAH84493.1; -; mRNA.
DR   RefSeq; NP_001011098.1; NM_001011098.1.
DR   AlphaFoldDB; Q5XGE9; -.
DR   SMR; Q5XGE9; -.
DR   STRING; 8364.ENSXETP00000012870; -.
DR   ESTHER; xentr-q5xge9; Phospholipase.
DR   PaxDb; Q5XGE9; -.
DR   DNASU; 496511; -.
DR   GeneID; 496511; -.
DR   KEGG; xtr:496511; -.
DR   CTD; 200879; -.
DR   Xenbase; XB-GENE-5847665; liph.
DR   eggNOG; ENOG502QUQT; Eukaryota.
DR   InParanoid; Q5XGE9; -.
DR   OrthoDB; 534956at2759; -.
DR   Reactome; R-XTR-1483166; Synthesis of PA.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000005849; Expressed in egg cell and 8 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR   GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 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; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..460
FT                   /note="Lipase member H"
FT                   /id="PRO_0000273328"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        187
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        242..255
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..301
FT                   /evidence="ECO:0000250"
FT   DISULFID        436..455
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  52223 MW;  053819C3C3BA4F3E CRC64;
     MLLRFYFNGL LFVGCLLSWG RSDTEEQCHT FTDLNIHNSI IGTGLKVQLL LYTRENPKCA
     QDLNVDNSTG FQYLNVTRRT VFITHGYRPT GSPPVWIDDI VKKFLDIQDF NVIVVDWNRG
     ATTVLYHNAA ANTRKVADIL KRFIDNMLSQ GATLDSIYMV GVSLGAHISG FVGKMYNGSI
     GRITGLDPAG PLFNGKPPEE RLHYTDAQFV DVVHSDTDGL GYKESLGHID FYPNGGTDQP
     GCPKTILAGS EYFKCDHQRS VFLYIASLTK SCDLVAFPCK SYRDYRIGNC TDCKEFLPLS
     CPVLGFYADK WKDHLVKRNH PGTTAFFDTA AKDPYCIFHY YLDFMTWSSQ IRRGYITIKL
     TSLDGNVTES KLDKDAAVFE QYKEESLLAK FDQDMDPISR ISVTFTTGSV IGPKYKLRVL
     RMRLRPFTNR NRPILCRYDF VLLENIETEF IPIPCEDTNL