ID   A6H8L5_HUMAN            Unreviewed;       499 AA.
AC   A6H8L5;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
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|EMBL:AAI46660.1};
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|EMBL:AAI46660.1};
RN   [1] {ECO:0000313|EMBL:AAI46660.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   -!- 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; BC146659; AAI46660.1; -; mRNA.
DR   RefSeq; NP_000227.2; NM_000236.2.
DR   AlphaFoldDB; A6H8L5; -.
DR   SMR; A6H8L5; -.
DR   ESTHER; human-LIPC; Hepatic_Lipase.
DR   PeptideAtlas; A6H8L5; -.
DR   DNASU; 3990; -.
DR   GeneID; 3990; -.
DR   KEGG; hsa:3990; -.
DR   CTD; 3990; -.
DR   PharmGKB; PA230; -.
DR   OrthoDB; 3428256at2759; -.
DR   BioGRID-ORCS; 3990; 6 hits in 1140 CRISPR screens.
DR   ChiTaRS; LIPC; human.
DR   GenomeRNAi; 3990; -.
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.
DR   Genevisible; A6H8L5; HS.
PE   2: Evidence at transcript 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   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_5002698104"
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;  55556 MW;  735D9932D201C8AE CRC64;
     MDTSPLCFSI LLVLCIFIQS SALGQSLKPE PFGRRAQAVE TNKTLHEMKT RFLLFGETNQ
     GCQIRINHPD TLQECGFNSS LPLVMIIHGW SVDGVLENWI WQMVAALKSQ PAQPVNVGLV
     DWITLAHDHY TIAVRNTRLV GKEVAALLRW LEESVQLSRS HVHLIGYSLG AHVSGFAGSS
     IGGTHKIGRI TGLDAAGPLF EGSAPSNRLS PDDASFVDAI HTFTREHMGL SVGIKQPIGH
     YDFYPNGGSF QPGCHFLELY RHIAQHGFNA ITQTIKCSHE RSVHLFIDSL LHAGTQSMAY
     PCGDMNSFSQ GLCLSCKKGR CNTLGYHVRQ EPRSKSKRLF LVTRAQSPFK VYHYQLKIQF
     INQTETPIQT TFTMSLLGTK EKMQKIPITL GKGIASNKTY SFLITLDVDI GELIMIKFKW
     ENSAVWANVW DTVQTIIPWS TGPRHSGLVL KTIRVKAGET QQRSPNRINL GRLNCSLLFC
     TELFSHDSLA HWSSAASEL
//