LIPC_RABIT
ID LIPC_RABIT Reviewed; 499 AA.
AC O46559;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Hepatic triacylglycerol lipase;
DE Short=HL;
DE Short=Hepatic lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:1770315};
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1770315;
RA Warren R.J., Ebert D.L., Mitchell A., Barter P.J.;
RT "Rabbit hepatic lipase cDNA sequence: low activity is associated with low
RT messenger RNA levels.";
RL J. Lipid Res. 32:1333-1339(1991).
RN [2]
RP SEQUENCE REVISION.
RA Warren R.J., Ebert D.L., Mitchell A., Barter P.J.;
RL Submitted (JAN-1998) 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 (PubMed:1770315). 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, ECO:0000269|PubMed:1770315}.
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:0000269|PubMed:1770315};
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; AF041202; AAB96786.1; -; mRNA.
DR RefSeq; NP_001075501.1; NM_001082032.1.
DR AlphaFoldDB; O46559; -.
DR SMR; O46559; -.
DR STRING; 9986.ENSOCUP00000001411; -.
DR ESTHER; rabit-1hlip; Hepatic_Lipase.
DR GeneID; 100008678; -.
DR KEGG; ocu:100008678; -.
DR CTD; 3990; -.
DR eggNOG; ENOG502QVTG; Eukaryota.
DR InParanoid; O46559; -.
DR OrthoDB; 534956at2759; -.
DR Proteomes; UP000001811; Unplaced.
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: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:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 1: Evidence at protein 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..499
FT /note="Hepatic triacylglycerol lipase"
FT /id="PRO_0000233341"
FT DOMAIN 352..486
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
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 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 55814 MW; 4DA7D65EE815A0A5 CRC64;
MGSPLCVPIF LAVCILIQSS THGQSLRPEP FGRRARVTAT KKTLLETETR FLLFKDKANK
GCQIRLHHAD TLQECGFNSS LPLVMIVHGW SVDGLLESWI WQMVAALKSQ PARPVNVGLV
DWISLAHSHY AVAVRNARLV GQEVAALLQW LEESAPFSRS NVHLIGYSLG AHVAGFAGSY
ISGKHKIGRI TGLDAAGPLF EGTSASDRLS PDDATFVDAI HTFTREHMGL SVGIKQPVGH
YDFYPNGGSF QPGCHFLELY KHIAQHGLNA LSQTIKCAHE RSVHLFIDSL LHPSMQSTAY
QCSDMDSFSQ GLCLGCTKGR CNTLGYHIRQ EPLSKGKRLF LVTQAQSPFR VYHYQFKIQF
INQIEKPLEP TFTMSLLGTK EEMQKIPITL GEGITSNKTY SFLITLNLDI GELMVIKFKW
ENSAVWANVW NTVQTIIPWG IKPRNSGLIL KTIRVKAGET QQRMTFCSEN MDDLQLHPTQ
EKNFVRCEVN PKKLKLKIK
