LIPE_MOUSE
ID LIPE_MOUSE Reviewed; 500 AA.
AC Q9WVG5; Q8VDU2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Endothelial lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:Q9Y5X9};
DE AltName: Full=Endothelial cell-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 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], AND TISSUE SPECIFICITY.
RC TISSUE=Endothelial cell;
RX PubMed=10318835; DOI=10.1074/jbc.274.20.14170;
RA Hirata K., Dichek H.L., Cioffi J.A., Choi S.Y., Leeper N.J., Quintana L.,
RA Kronmal G.S., Cooper A.D., Quertermous T.;
RT "Cloning of a unique lipase from endothelial cells extends the lipase gene
RT family.";
RL J. Biol. Chem. 274:14170-14175(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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: 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. {ECO:0000250|UniProtKB:Q9Y5X9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y5X9}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta, lung, liver, testis and
CC spleen. {ECO:0000269|PubMed:10318835}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF118768; AAD30435.1; -; mRNA.
DR EMBL; AC125122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020991; AAH20991.1; -; mRNA.
DR CCDS; CCDS29343.1; -.
DR RefSeq; NP_034850.3; NM_010720.3.
DR AlphaFoldDB; Q9WVG5; -.
DR SMR; Q9WVG5; -.
DR BioGRID; 201170; 1.
DR STRING; 10090.ENSMUSP00000066536; -.
DR BindingDB; Q9WVG5; -.
DR ChEMBL; CHEMBL2380190; -.
DR ESTHER; mouse-Lipg; Lipoprotein_Lipase.
DR GlyGen; Q9WVG5; 6 sites.
DR iPTMnet; Q9WVG5; -.
DR PhosphoSitePlus; Q9WVG5; -.
DR MaxQB; Q9WVG5; -.
DR PaxDb; Q9WVG5; -.
DR PRIDE; Q9WVG5; -.
DR ProteomicsDB; 292332; -.
DR Antibodypedia; 1561; 1074 antibodies from 32 providers.
DR Ensembl; ENSMUST00000066532; ENSMUSP00000066536; ENSMUSG00000053846.
DR GeneID; 16891; -.
DR KEGG; mmu:16891; -.
DR UCSC; uc008fpu.2; mouse.
DR CTD; 9388; -.
DR MGI; MGI:1341803; Lipg.
DR VEuPathDB; HostDB:ENSMUSG00000053846; -.
DR eggNOG; ENOG502QU8P; Eukaryota.
DR GeneTree; ENSGT00940000159394; -.
DR HOGENOM; CLU_027171_1_2_1; -.
DR InParanoid; Q9WVG5; -.
DR OMA; QMPVGHV; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q9WVG5; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-8964058; HDL remodeling.
DR BioGRID-ORCS; 16891; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9WVG5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9WVG5; protein.
DR Bgee; ENSMUSG00000053846; Expressed in placenta labyrinth and 148 other tissues.
DR ExpressionAtlas; Q9WVG5; baseline and differential.
DR Genevisible; Q9WVG5; 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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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:0055091; P:phospholipid homeostasis; ISO:MGI.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; ISO:MGI.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..500
FT /note="Endothelial lipase"
FT /id="PRO_0000017798"
FT DOMAIN 347..482
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 325..337
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 252..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 297..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 308..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 463..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 28
FT /note="Q -> E (in Ref. 3; AAH20991)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="Y -> C (in Ref. 1; AAD30435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56629 MW; D4B8A4A291810759 CRC64;
MRNTVFLLGF WSVYCYFPAG SITTLRPQGS LRDEHHKPTG VPATARPSVA FNIRTSKDPE
QEGCNLSLGD SKLLENCGFN MTAKTFFIIH GWTMSGMFES WLHKLVSALQ MREKDANVVV
VDWLPLAHQL YTDAVNNTRV VGQRVAGMLD WLQEKEEFSL GNVHLIGYSL GAHVAGYAGN
FVKGTVGRIT GLDPAGPMFE GVDINRRLSP DDADFVDVLH TYTLSFGLSI GIRMPVGHID
IYPNGGDFQP GCGFNDVIGS FAYGTISEMV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS
SRFKRGICLS CRKNRCNNIG YNAKKMRKKR NSKMYLKTRA GMPFKVYHYQ LKVHMFSYNN
SGDTQPTLYI TLYGSNADSQ NLPLEIVEKI ELNATNTFLV YTEEDLGDLL KMRLTWEGVA
HSWYNLWNEF RNYLSQPSNP SRELYIRRIR VKSGETQRKV TFCTQDPTKS SISPGQELWF
HKCQDGWKMK NKTSPFVNLA
