LIPH_DANRE
ID LIPH_DANRE Reviewed; 454 AA.
AC Q6DBU8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lipase member H;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=liph; ORFNames=zgc:91985;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-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; BC078354; AAH78354.1; -; mRNA.
DR RefSeq; NP_001003499.1; NM_001003499.1.
DR AlphaFoldDB; Q6DBU8; -.
DR SMR; Q6DBU8; -.
DR STRING; 7955.ENSDARP00000014304; -.
DR ESTHER; danre-LIPH; Phospholipase.
DR PaxDb; Q6DBU8; -.
DR Ensembl; ENSDART00000023838; ENSDARP00000014304; ENSDARG00000007108.
DR GeneID; 445105; -.
DR KEGG; dre:445105; -.
DR CTD; 445105; -.
DR ZFIN; ZDB-GENE-040801-242; lipia.
DR eggNOG; ENOG502QUQT; Eukaryota.
DR GeneTree; ENSGT00940000156285; -.
DR HOGENOM; CLU_027171_3_0_1; -.
DR InParanoid; Q6DBU8; -.
DR OMA; YPCSSYK; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q6DBU8; -.
DR TreeFam; TF324997; -.
DR Reactome; R-DRE-1483166; Synthesis of PA.
DR PRO; PR:Q6DBU8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000007108; Expressed in mature ovarian follicle and 26 other tissues.
DR ExpressionAtlas; Q6DBU8; baseline and differential.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..454
FT /note="Lipase member H"
FT /id="PRO_0000273325"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 240..253
FT /evidence="ECO:0000250"
FT DISULFID 277..288
FT /evidence="ECO:0000250"
FT DISULFID 291..299
FT /evidence="ECO:0000250"
FT DISULFID 430..449
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 51811 MW; F95FF45E71113AB6 CRC64;
MIYRKIIWGI LYVTLMLFDT HRAQECEEMT DLNFKDSLAG TSLKVRLLLY TRADPSCGQL
LSHQEPFSNS QFNVSSVTTF LIHGYRPTGS PPVWMKQFVE FLLNRRDMNV IVVDWNRGAT
NMNYWQVVKN TRKVANNLTD LIQKMKDNGA NLSSIHMIGV SLGAHISGFT GANFNGEIGR
ITALDPAGPE FNGRPPEDRL DPSDALFVEA LHTDMDALGY RNLLGHIDYY ANGGADQPGC
PKTILSGSEY FKCDHQRSVF LYMSSVNGSC PIIAYPCESY TDFQDGTCMD CGKFKSAGCP
IFGYDSVRWR DTLVQLEQTR TYFQTNKASP FCKVGYKVDI VSWNQKTHWG YLTIKLSNGT
EETQVELNHK SLKFERFQET SVLAQFERDI QPVKKITLKF CPRKGLRPRK KLRLLHIRLT
PLQNHLRPLC RYDLLLEESK DVTFKPIPCE DSNF
