Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endothelial lipase

Gene

Lipg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin (By similarity).By similarity

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei169NucleophileBy similarity1
Active sitei193Charge relay systemPROSITE-ProRule annotation1
Active sitei274Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-8964058. HDL remodeling.

Protein family/group databases

ESTHERimouse-Lipg. Lipoprotein_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelial lipase (EC:3.1.1.3)
Alternative name(s):
Endothelial cell-derived lipase
Short name:
EDL
Gene namesi
Name:Lipg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1341803. Lipg.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2380190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001779821 – 500Endothelial lipaseAdd BLAST480

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi64 ↔ 77PROSITE-ProRule annotation
Glycosylationi65N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi80N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi136N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi252 ↔ 272PROSITE-ProRule annotation
Disulfide bondi297 ↔ 316PROSITE-ProRule annotation
Disulfide bondi308 ↔ 311PROSITE-ProRule annotation
Glycosylationi359N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi393N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi463 ↔ 483PROSITE-ProRule annotation
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9WVG5.
PaxDbiQ9WVG5.
PRIDEiQ9WVG5.

PTM databases

iPTMnetiQ9WVG5.
PhosphoSitePlusiQ9WVG5.

Expressioni

Tissue specificityi

Expressed in placenta, lung, liver, testis and spleen.

Gene expression databases

BgeeiENSMUSG00000053846.
CleanExiMM_LIPG.
ExpressionAtlasiQ9WVG5. baseline and differential.
GenevisibleiQ9WVG5. MM.

Interactioni

Subunit structurei

Head to tail homodimer.By similarity

Protein-protein interaction databases

BioGridi201170. 1 interactor.
STRINGi10090.ENSMUSP00000066536.

Chemistry databases

BindingDBiQ9WVG5.

Structurei

3D structure databases

ProteinModelPortaliQ9WVG5.
SMRiQ9WVG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini347 – 482PLATPROSITE-ProRule annotationAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni325 – 337Heparin-bindingBy similarityAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi118 – 121Poly-Val4

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ9WVG5.
KOiK01046.
OMAiLKIKLTW.
OrthoDBiEOG091G052B.
TreeFamiTF324997.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiView protein in InterPro
IPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiView protein in Pfam
PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiView protein in SMART
SM00308. LH2. 1 hit.
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiView protein in PROSITE
PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNTVFLLGF WSVYCYFPAG SITTLRPQGS LRDEHHKPTG VPATARPSVA
60 70 80 90 100
FNIRTSKDPE QEGCNLSLGD SKLLENCGFN MTAKTFFIIH GWTMSGMFES
110 120 130 140 150
WLHKLVSALQ MREKDANVVV VDWLPLAHQL YTDAVNNTRV VGQRVAGMLD
160 170 180 190 200
WLQEKEEFSL GNVHLIGYSL GAHVAGYAGN FVKGTVGRIT GLDPAGPMFE
210 220 230 240 250
GVDINRRLSP DDADFVDVLH TYTLSFGLSI GIRMPVGHID IYPNGGDFQP
260 270 280 290 300
GCGFNDVIGS FAYGTISEMV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS
310 320 330 340 350
SRFKRGICLS CRKNRCNNIG YNAKKMRKKR NSKMYLKTRA GMPFKVYHYQ
360 370 380 390 400
LKVHMFSYNN SGDTQPTLYI TLYGSNADSQ NLPLEIVEKI ELNATNTFLV
410 420 430 440 450
YTEEDLGDLL KMRLTWEGVA HSWYNLWNEF RNYLSQPSNP SRELYIRRIR
460 470 480 490 500
VKSGETQRKV TFCTQDPTKS SISPGQELWF HKCQDGWKMK NKTSPFVNLA
Length:500
Mass (Da):56,629
Last modified:July 27, 2011 - v3
Checksum:iD4B8A4A291810759
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28Q → E in AAH20991 (PubMed:15489334).Curated1
Sequence conflicti424Y → C in AAD30435 (PubMed:10318835).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118768 mRNA. Translation: AAD30435.1.
AC125122 Genomic DNA. No translation available.
BC020991 mRNA. Translation: AAH20991.1.
CCDSiCCDS29343.1.
RefSeqiNP_034850.3. NM_010720.3.
UniGeneiMm.299647.

Genome annotation databases

EnsembliENSMUST00000066532; ENSMUSP00000066536; ENSMUSG00000053846.
GeneIDi16891.
KEGGimmu:16891.
UCSCiuc008fpu.2. mouse.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiLIPE_MOUSE
AccessioniPrimary (citable) accession number: Q9WVG5
Secondary accession number(s): Q8VDU2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 27, 2011
Last modified: June 7, 2017
This is version 133 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families