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 24-JAN-2024, entry version 86.
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 -!- SUBUNIT: Interacts with TTMP/C3orf52. {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.ENSRNOP00000069088; -.
DR ESTHER; ratno-q6p6s8; Phospholipase.
DR GlyCosmos; Q32PY2; 1 site, No reported glycans.
DR GlyGen; Q32PY2; 1 site.
DR PhosphoSitePlus; Q32PY2; -.
DR PaxDb; 10116-ENSRNOP00000065168; -.
DR GeneID; 681694; -.
DR KEGG; rno:681694; -.
DR AGR; RGD:1592849; -.
DR CTD; 200879; -.
DR RGD; 1592849; Liph.
DR eggNOG; ENOG502QUQT; Eukaryota.
DR InParanoid; Q32PY2; -.
DR OrthoDB; 3428256at2759; -.
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:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0004620; F:phospholipase activity; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; LIPASE; 1.
DR PANTHER; PTHR11610:SF12; LIPASE MEMBER H; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
