ID   LIPHA_XENLA             Reviewed;         460 AA.
AC   Q6PA23;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Lipase member H-A;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=liph-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC060482; AAH60482.1; -; mRNA.
DR   RefSeq; NP_001083362.1; NM_001089893.1.
DR   AlphaFoldDB; Q6PA23; -.
DR   SMR; Q6PA23; -.
DR   ESTHER; xenla-LIPHA; Phospholipase.
DR   DNASU; 398885; -.
DR   GeneID; 398885; -.
DR   KEGG; xla:398885; -.
DR   CTD; 398885; -.
DR   Xenbase; XB-GENE-6079134; liph.L.
DR   OrthoDB; 534956at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 398885; Expressed in intestine and 10 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..460
FT                   /note="Lipase member H-A"
FT                   /id="PRO_0000273326"
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;  52063 MW;  265D2DEA263E3720 CRC64;
     MLLSFYFNGL LLVGCLLSWG RSDTEGQCHT FTDLNIHNAI IGTGLKVQLL LYTRENPNCA
     QDLNEDNSTG FQYLNVTRKT VFIIHGYRPT GSPPVWIDDI VKKFLDIQDF NVIVVDWNRG
     ATTVLYHNAA ANTRKVADIL KRLIDNMLSQ GATLDSVYMV GVSLGAHISG FVGKMYNGSI
     GRITGLDPAG PLFNGKPPEE RLHYTDAQFV DVVHTDIDGL GYKESLGHID FYPNGGTDQP
     GCPKTILAGS EYFKCDHQRS VYLYISSLKK NCDLVGFPCK SYRDYRIGNC TDCKEFLPLS
     CPVLGFYADK WKDHLVEKNP PGTKAFFDTA AKDPFCKFHY YLDFMTWSSQ TKRGYITIKL
     KSLDGNVTES KLDKDHATFQ QYKETSLLAK FDQDLDQISK ISVTFTTGSI IGPKYKLRVL
     RMRLRPLTNR DRPILCRYDF VLLENIEMEF IPIPCEDTNL