ID   E7EUJ1_HUMAN            Unreviewed;       499 AA.
AC   E7EUJ1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Hepatic triacylglycerol lipase {ECO:0000256|ARBA:ARBA00019624};
DE            EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
DE            EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274};
DE   AltName: Full=Lipase member C {ECO:0000256|ARBA:ARBA00030539};
DE   AltName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00029723};
DE   AltName: Full=Phospholipase A1 {ECO:0000256|ARBA:ARBA00031180};
GN   Name=LIPC {ECO:0000313|Ensembl:ENSP00000395569.3};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000395569.3, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000395569.3, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M., Stewart S.,
RA   Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R.,
RA   Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000395569.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824;
CC         Evidence={ECO:0000256|ARBA:ARBA00001610};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392;
CC         Evidence={ECO:0000256|ARBA:ARBA00001610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC         octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC         Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000256|ARBA:ARBA00000652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC         (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC         H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC         Evidence={ECO:0000256|ARBA:ARBA00001885};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC         Evidence={ECO:0000256|ARBA:ARBA00001885};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC         octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+);
CC         Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990;
CC         Evidence={ECO:0000256|ARBA:ARBA00001101};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512;
CC         Evidence={ECO:0000256|ARBA:ARBA00001101};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000256|ARBA:ARBA00000879};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC         Evidence={ECO:0000256|ARBA:ARBA00000879};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75735, ChEBI:CHEBI:75938;
CC         Evidence={ECO:0000256|ARBA:ARBA00000265};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652;
CC         Evidence={ECO:0000256|ARBA:ARBA00000265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC         Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC         Evidence={ECO:0000256|ARBA:ARBA00000111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001024};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   EMBL; AC018904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF456063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7EUJ1; -.
DR   SMR; E7EUJ1; -.
DR   ESTHER; human-LIPC; Hepatic_Lipase.
DR   MassIVE; E7EUJ1; -.
DR   PeptideAtlas; E7EUJ1; -.
DR   ProteomicsDB; 18443; -.
DR   Antibodypedia; 4249; 408 antibodies from 30 providers.
DR   Ensembl; ENST00000414170.7; ENSP00000395569.3; ENSG00000166035.11.
DR   UCSC; uc010bfz.2; human.
DR   HGNC; HGNC:6619; LIPC.
DR   VEuPathDB; HostDB:ENSG00000166035; -.
DR   GeneTree; ENSGT00940000157602; -.
DR   PhylomeDB; E7EUJ1; -.
DR   ChiTaRS; LIPC; human.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000166035; Expressed in right lobe of liver and 99 other cell types or tissues.
DR   ExpressionAtlas; E7EUJ1; baseline and differential.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR002333; Lipase_hep.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF2; HEPATIC TRIACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00824; HEPLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW   HDL {ECO:0000256|ARBA:ARBA00022850};
KW   Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Proteomics identification {ECO:0007829|MaxQB:E7EUJ1,
KW   ECO:0007829|PeptideAtlas:E7EUJ1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..499
FT                   /note="Hepatic triacylglycerol lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003219506"
FT   DOMAIN          352..493
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        279
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ   SEQUENCE   499 AA;  55617 MW;  C5FED21BD5574072 CRC64;
     MDTSPLCFSI LLVLCIFIQS SALGQSLKPE PFGRRAQAVE TNKTLHEMKT RFLLFGETNQ
     GCQIRINHPD TLQECGFNSS LPLVMIIHGW SVDGVLENWI WQMVAALKSQ PAQPVNVGLV
     DWITLAHDHY TIAVRNTRLV GKEVAALLRW LEESVQLSRS HVHLIGYSLG AHVSGFAGSS
     IGGTHKIGRI TGLDAAGPLF EGSAPSNRLS PDDANFVDAI HTFTREHMGL SVGIKQPIGH
     YDFYPNGGSF QPGCHFLELY RHIAQHGFNA ITQTIKCSHE RSVHLFIDSL LHAGTQSMAY
     PCGDMNSFSQ GLCLSCKKGR CNTLGYHVRQ EPRSKSKRLF LVTRAQSPFK VYHYQFKIQF
     INQTETPIQT TFTMSLLGTK EKMQKIPITL GKGIASNKTY SFLITLDVDI GELIMIKFKW
     ENSAVWANVW DTVQTIIPWS TGPRHSGLVL KTIRVKAGET QQRSPNRINL GRLNCSLLFC
     TELFSHDSLA HWSSAASEL
//