LIPC_MOUSE
ID LIPC_MOUSE Reviewed; 510 AA.
AC P27656; Q8VC44;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
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; Synonyms=Hpl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2025643; DOI=10.1016/0167-4781(91)90078-z;
RA Oka K., Nakano T., Tkalcevic G.T., Scow R.O., Brown W.V.;
RT "Molecular cloning of mouse hepatic triacylglycerol lipase: gene expression
RT in combined lipase-deficient (cld/cld) mice.";
RL Biochim. Biophys. Acta 1089:13-20(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=1840530; DOI=10.1016/0014-5793(91)80910-u;
RA Chang S.F., Netter H.J., Will H.;
RT "Characterization of cDNA encoding the mouse hepatic triglyceride lipase
RT and expression by in vitro translation.";
RL FEBS Lett. 289:69-72(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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: 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; AY228765; AAO73443.1; -; mRNA.
DR EMBL; X58426; CAA41329.1; -; mRNA.
DR EMBL; CH466522; EDL26212.1; -; Genomic_DNA.
DR EMBL; BC021841; AAH21841.1; -; mRNA.
DR EMBL; BC094050; AAH94050.1; -; mRNA.
DR CCDS; CCDS23324.1; -.
DR PIR; S15893; S15893.
DR RefSeq; NP_001311401.1; NM_001324472.1.
DR RefSeq; NP_001311402.1; NM_001324473.1.
DR RefSeq; NP_032306.2; NM_008280.2.
DR AlphaFoldDB; P27656; -.
DR SMR; P27656; -.
DR BioGRID; 200409; 28.
DR STRING; 10090.ENSMUSP00000034731; -.
DR ESTHER; mouse-1hlip; Hepatic_Lipase.
DR GlyGen; P27656; 2 sites.
DR PhosphoSitePlus; P27656; -.
DR MaxQB; P27656; -.
DR PaxDb; P27656; -.
DR PRIDE; P27656; -.
DR ProteomicsDB; 290030; -.
DR Antibodypedia; 4249; 382 antibodies from 30 providers.
DR DNASU; 15450; -.
DR Ensembl; ENSMUST00000034731; ENSMUSP00000034731; ENSMUSG00000032207.
DR GeneID; 15450; -.
DR KEGG; mmu:15450; -.
DR UCSC; uc009qos.1; mouse.
DR CTD; 3990; -.
DR MGI; MGI:96216; Lipc.
DR VEuPathDB; HostDB:ENSMUSG00000032207; -.
DR eggNOG; ENOG502QVTG; Eukaryota.
DR GeneTree; ENSGT00940000157602; -.
DR HOGENOM; CLU_027171_1_1_1; -.
DR InParanoid; P27656; -.
DR OMA; YIGGKHK; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; P27656; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-MMU-8964026; Chylomicron clearance.
DR BioGRID-ORCS; 15450; 6 hits in 75 CRISPR screens.
DR PRO; PR:P27656; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P27656; protein.
DR Bgee; ENSMUSG00000032207; Expressed in left lobe of liver and 44 other tissues.
DR ExpressionAtlas; P27656; baseline and differential.
DR Genevisible; P27656; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; ISO:MGI.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISO:MGI.
DR GO; GO:0035478; F:chylomicron binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016298; F:lipase activity; IDA:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; ISO:MGI.
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; IGI:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IGI:MGI.
DR GO; GO:0030301; P:cholesterol transport; IMP:MGI.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISO:MGI.
DR GO; GO:0034371; P:chylomicron remodeling; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:MGI.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0046461; P:neutral lipid catabolic process; ISO:MGI.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISO:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISO:MGI.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISO:MGI.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISO:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; ISO:MGI.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:MGI.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:MGI.
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..510
FT /note="Hepatic triacylglycerol lipase"
FT /id="PRO_0000017770"
FT DOMAIN 353..487
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 255..278
FT /note="Essential for determining substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P11150"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 286
FT /note="L -> P (in Ref. 2; CAA41329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57389 MW; E30222652D782A05 CRC64;
MGNPLQISIF LVFCIFIQSS ACGQGVGTEP FGRSLGATEA SKPLKKPETR FLLFQDENDR
LGCRLRPQHP ETLQECGFNS SQPLIMIIHG WSVDGLLENW IWKIVSALKS RQSQPVNVGL
VDWISLAYQH YTIAVQNTRI VGQDVAALLL WLEESAKFSR SKVHLIGYSL GAHVSGFAGS
SMDGKNKIGR ITGLDPAGPM FEGTSPNERL SPDDANFVDA IHTFTREHMG LSVGIKQPIA
HYDFYPNGGS FQPGCHFLEL YKHIAEHGLN AITQTIKCAH ERSVHLFIDS LQHSDLQSIG
FQCSDMGSFS QGLCLSCKKG RCNTLGYDIR KDRSGKSKRL FLITRAQSPF KVYHYQFKIQ
FINQIEKPVE PTFTMSLLGT KEEIKRIPIT LGEGITSNKT YSFLITLDKD IGELILLKFK
WENSAVWANV WNTVQTIMLW GIEPHHSGLI LKTIWVKAGE TQQRMTFCPE NLDDLQLHPS
QEKVFVNCEV KSKRLTESKE QMSQETHAKK
