ID   LIPH_RAT                Reviewed;         451 AA.
AC   Q32PY2; Q6P6S8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Lipase member H;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=Liph;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Prostate;
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).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAH62045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC062045; AAH62045.1; ALT_INIT; mRNA.
DR   EMBL; BC107932; AAI07933.1; -; mRNA.
DR   RefSeq; NP_001037744.1; NM_001044279.1.
DR   AlphaFoldDB; Q32PY2; -.
DR   SMR; Q32PY2; -.
DR   STRING; 10116.ENSRNOP00000065168; -.
DR   ESTHER; ratno-q6p6s8; Phospholipase.
DR   GlyGen; Q32PY2; 1 site.
DR   PaxDb; Q32PY2; -.
DR   PRIDE; Q32PY2; -.
DR   GeneID; 681694; -.
DR   KEGG; rno:681694; -.
DR   CTD; 200879; -.
DR   RGD; 1592849; Liph.
DR   eggNOG; ENOG502QUQT; Eukaryota.
DR   InParanoid; Q32PY2; -.
DR   OrthoDB; 534956at2759; -.
DR   PhylomeDB; Q32PY2; -.
DR   Reactome; R-RNO-1483166; Synthesis of PA.
DR   PRO; PR:Q32PY2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0008201; F:heparin binding; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..451
FT                   /note="Lipase member H"
FT                   /id="PRO_0000273324"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
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        66
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   CONFLICT        203
FT                   /note="V -> I (in Ref. 1; AAH62045)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  50826 MW;  E8EE38B33C348ACB CRC64;
     MLRLCFLLSF MCLVKSDTDE TCPSFTRLSF HSAVVGTGLS VRLMLYTQRD QTCAQVINST
     ALGSLNVTKK TTFIIHGFRP TGSPPVWMEE LVQSLISVQE MNVVVVDWNR GATTVIYPHA
     SSKTRKVALI LKEFIDQMLA KGASLDNIYM IGVSLGAHIA GFVGEMYSGK LGRITGLDPA
     GPLFNGRPPE DRLDPSDAQF VDVIHSDTDA LGYREALGHI DFYPNGGLDQ PGCPKTIFGG
     IKYFKCDHQM SVFLYLASLQ NNCSITAYPC DSYRDYRNGK CVSCGAGHIV SCPSLGYYAD
     NWREYLWDRD PPMTKAFFDT AETKPYCIYH YFVDIISWNK SVRRGFITIK LRGEDGNITE
     SKIDHEPSAF QKYHQVSLLA RFNRDLDKVA EISLLFSTKS VVGPKYKLRV LRMKLRSLAH
     PDRPHLCRYD LVLMENVETF FQPILCSKQQ M