LIPE_RAT
ID LIPE_RAT Reviewed; 493 AA.
AC Q8VBX1; Q5D216;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Endothelial lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:Q9Y5X9};
DE AltName: Full=Endothelial-derived lipase;
DE Short=EDL;
DE AltName: Full=Phospholipase A1;
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q9Y5X9};
DE Flags: Precursor;
GN Name=Lipg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Aortic smooth muscle;
RX PubMed=15914124; DOI=10.1016/j.cardiores.2005.01.013;
RA Shimokawa Y., Hirata K., Ishida T., Kojima Y., Inoue N., Quertermous T.,
RA Yokoyama M.;
RT "Increased expression of endothelial lipase in rat models of
RT hypertension.";
RL Cardiovasc. Res. 66:594-600(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-293.
RC STRAIN=BN-Lx/Cub, and SHR/OlaIpcv;
RX PubMed=11924532; DOI=10.3109/10425170109025004;
RA Bonne A.C.M., den Bieman M.G., van Lith H., van Zutphen B.F.M.;
RT "Sequencing and chromosomal assignment of the rat endothelial-derived
RT lipase gene (Lipg).";
RL DNA Seq. 12:285-287(2001).
CC -!- FUNCTION: Exerts both phospholipase and triglyceride lipase activities
CC (By similarity). More active as a phospholipase than a triglyceride
CC lipase (By similarity). Hydrolyzes triglycerides, both with short-chain
CC fatty acyl groups (tributyrin) and long-chain fatty acyl groups
CC (triolein) with similar levels of activity toward both types of
CC substrates (By similarity). Hydrolyzes high density lipoproteins (HDL)
CC more efficiently than other lipoproteins (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5X9}.
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:Q9Y5X9};
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:Q9Y5X9};
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:Q9Y5X9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5X9};
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:Q9Y5X9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5X9};
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:Q9Y5X9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5X9};
CC -!- SUBUNIT: Head to tail Homodimer. Interacts with apolipoprotein C-2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y5X9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y5X9}.
CC -!- MISCELLANEOUS: It is termed endothelial lipase due to the fact that it
CC is synthesized in endothelial cells, a characteristic that
CC distinguishes it from other members of the family. However, this
CC protein is also expressed in other cell types.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AY916123; AAX11354.1; -; mRNA.
DR EMBL; AY027561; AAK14774.1; -; Genomic_DNA.
DR EMBL; AY027562; AAK14775.1; -; Genomic_DNA.
DR RefSeq; NP_001012759.1; NM_001012741.1.
DR AlphaFoldDB; Q8VBX1; -.
DR SMR; Q8VBX1; -.
DR STRING; 10116.ENSRNOP00000025257; -.
DR BindingDB; Q8VBX1; -.
DR ChEMBL; CHEMBL3638354; -.
DR GlyGen; Q8VBX1; 3 sites.
DR PaxDb; Q8VBX1; -.
DR Ensembl; ENSRNOT00000025257; ENSRNOP00000025257; ENSRNOG00000018694.
DR GeneID; 291437; -.
DR KEGG; rno:291437; -.
DR CTD; 9388; -.
DR RGD; 1310740; Lipg.
DR eggNOG; ENOG502QU8P; Eukaryota.
DR GeneTree; ENSGT00940000159394; -.
DR HOGENOM; CLU_027171_1_2_1; -.
DR InParanoid; Q8VBX1; -.
DR OMA; QMPVGHV; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q8VBX1; -.
DR TreeFam; TF324997; -.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR PRO; PR:Q8VBX1; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000018694; Expressed in ovary and 14 other tissues.
DR Genevisible; Q8VBX1; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
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:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
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; ISO:RGD.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
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; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002330; Lipo_Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00822; LIPOLIPASE.
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 Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..493
FT /note="Endothelial lipase"
FT /id="PRO_0000043409"
FT DOMAIN 349..484
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 171
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 276
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 327..339
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 254..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 299..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 310..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 465..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 275..277
FT /note="EHE -> KHK (in Ref. 2; AAK14774/AAK14775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55924 MW; 11F8E39B2E2FCBC5 CRC64;
MRDPVFLLGF WSLYCCFPAG SLTTLRPQGS LRDEHHKPTG VPVTITTKPS VTFNIRTSKD
PEHEGCNLSL GDSKLLENCG FNMTAKTFFI IHGWTMSGMF ESWLHKLVSA LQTREKEANV
VVVDWLPLAH QLYIDAVSNT RVVGRRVAGM LNWLQEKGEF SLGDVHLIGY SLGAHVAGYA
GNFVKGTVGR ITGLDPAGPM FEGVDINRRL SPDDADFVDV LHTYTLSFGL SIGIRMPVGH
IDIYPNGGDF QPGCGFNDVM GSFAYGTISE MVKCEHERAV HLFVDSLVNQ DKPSFAFQCT
DPNRFKRGIC LSCRKNRCNN IGYNAKKMRK KRNSKMYLKT RAGMPFRVYH YQLKVHMFSY
KNSGDIQPDL YITLYGSNAD SQNLPLEIVE KIELNATNTF LVYTEEYLGD LFKIRLTWEG
VSSSWYNLWN EFRSYLSQPS SPSRELHIRR IRVKSGETQR KVAFCVQDPM KNSISPGQEL
WFYKCQNDCR VKN
