LIPC_BOVIN
ID LIPC_BOVIN Reviewed; 500 AA.
AC Q3SZ79;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Hepatic triacylglycerol lipase;
DE Short=HL;
DE Short=Hepatic lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P07867};
DE AltName: Full=Lipase member C;
DE AltName: Full=Lysophospholipase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:P07867};
DE AltName: Full=Phospholipase A1;
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:P07867};
DE Flags: Precursor;
GN Name=LIPC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids
CC present in circulating plasma lipoproteins, including chylomicrons,
CC intermediate density lipoproteins (IDL), low density lipoproteins (LDL)
CC of large size and high density lipoproteins (HDL), releasing free fatty
CC acids (FFA) and smaller lipoprotein particles (By similarity). Also
CC exhibits lysophospholipase activity (By similarity). Can hydrolyze both
CC neutral lipid and phospholipid substrates but shows a greater binding
CC affinity for neutral lipid substrates than phospholipid substrates (By
CC similarity). In native LDL, preferentially hydrolyzes the
CC phosphatidylcholine species containing polyunsaturated fatty acids at
CC sn-2 position (By similarity). {ECO:0000250|UniProtKB:P07867,
CC ECO:0000250|UniProtKB:P11150}.
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:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P11150};
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:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000250|UniProtKB:P11150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:P11150};
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:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000250|UniProtKB:P11150};
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:0000250|UniProtKB:P07867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512;
CC Evidence={ECO:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392;
CC Evidence={ECO:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:P07867};
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:0000250|UniProtKB:P07867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652;
CC Evidence={ECO:0000250|UniProtKB:P07867};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11150}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; BC103072; AAI03073.1; -; mRNA.
DR RefSeq; NP_001030487.1; NM_001035410.1.
DR AlphaFoldDB; Q3SZ79; -.
DR SMR; Q3SZ79; -.
DR STRING; 9913.ENSBTAP00000007206; -.
DR ESTHER; bovin-q3sz79; Hepatic_Lipase.
DR Ensembl; ENSBTAT00000007206; ENSBTAP00000007206; ENSBTAG00000005479.
DR GeneID; 535192; -.
DR KEGG; bta:535192; -.
DR CTD; 3990; -.
DR VEuPathDB; HostDB:ENSBTAG00000005479; -.
DR VGNC; VGNC:58357; LIPC.
DR GeneTree; ENSGT00940000157602; -.
DR InParanoid; Q3SZ79; -.
DR OMA; YIGGKHK; -.
DR OrthoDB; 534956at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000005479; Expressed in liver and 50 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0034185; F:apolipoprotein binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:Ensembl.
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; 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; PTHR11610; 1.
DR PANTHER; PTHR11610:SF2; PTHR11610:SF2; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; HDL; Heparin-binding; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P11150"
FT CHAIN 22..500
FT /note="Hepatic triacylglycerol lipase"
FT /id="PRO_0000246183"
FT DOMAIN 353..487
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 23..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..277
FT /note="Essential for determining substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P11150"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 56826 MW; 65EECAF16C01B266 CRC64;
MENPLCVSIF LFYCILIQSS AHGQSLGPES FGRRSRAAET NKTPQETRTK FLLFRGETDK
GCQILLNHSD TLQQCGFNSS LPLVMIVHGW LVDDILEDWV WEMVAALKSQ LAQSVNVGLA
EWVTLAHNHY TTAVRNTRLV GQEIAALLQW LQESVQFSPS HVHLIGYSLG AHVSGFAGSY
MSRKHKIGRI TGLDAAGPLF EKASLSDRLS PDDANFVDAI HTFTWEHMGL SVGMKQPIAH
YDFYPNGGSY QPGCHFLELY KHFAKHGLNA ITRTVKCAHE RSVHLFIDSL LHADMQSMAY
LCRDMDRFSQ GLCLSCKKGR CNTLGYHTRQ ERQSKKSKSL FLVTRAQSPF KVYHYQFKIR
FINQTENPVE PTFTVSFLGT RGERQKIPIT LSKGITSNET YSFLITLDVD IGELIMIKFK
WENRMVWSNV WNTVQTIIPW GRGSLHSGLA LKSIRVKVGE TQQRMTFCSE NMNDLLLHPA
REKTFVRCEA NSETLKRKIR
