ID   LIPHB_XENLA             Reviewed;         460 AA.
AC   Q641F6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Lipase member H-B;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=liph-b;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-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; BC082381; AAH82381.1; -; mRNA.
DR   RefSeq; NP_001087855.1; NM_001094386.1.
DR   AlphaFoldDB; Q641F6; -.
DR   SMR; Q641F6; -.
DR   ESTHER; xenla-q641f6; Phospholipase.
DR   DNASU; 447716; -.
DR   GeneID; 447716; -.
DR   KEGG; xla:447716; -.
DR   CTD; 447716; -.
DR   Xenbase; XB-GENE-6253404; liph.S.
DR   OrthoDB; 534956at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 447716; Expressed in egg cell and 12 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-B"
FT                   /id="PRO_0000273327"
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;  51890 MW;  85DEE6E88CCAE251 CRC64;
     MLLSFYFNGL LLVGCLLSWG RSDTEGQCHS FTDLNIHNSI IGTALKVQLL LYTPENPKCA
     QDLNEDNSTG FQYLNVTRKT VFITHGYRPT GSPPVWIDNI VTKFLDIQDF NVILVDWNRG
     ATTVLYHNAA AKTRKVADIL KRLIDNMLSQ GATLDSIYMV GVSLGAHISG FVGKMYNGSI
     GRITGLDPAG PLFNGKPPEE RLHYTDAQFV DVVHTDTDGL GYKESLGHID FYPNGGTDQP
     GCPKTILSGS EYFKCDHQRS VFLYIASLTN NGDLVGFPCK SYRDYRIGNC TNCKEFLPLS
     CPVFGFYADK WKDHLVKKNP PGTKAFFDTA AKDPFCIFHY YLDIMTWSSQ TRRGYITIRL
     MSLNGNVTES KLDKDHATFE QYKEVSLLAK FDQDLDPMTR ISVTFTTGSV IGPKFKLRVL
     RMRLRPLTNT NRPILCRYDF VLLENVEMEF NPIPCEDTNL