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Protein

Endothelial lipase

Gene

Lipg

Organism
Rattus norvegicus (Rat)
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 sitei171NucleophileBy similarity1
Active sitei195Charge relay systemPROSITE-ProRule annotation1
Active sitei276Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-RNO-192456. Digestion of dietary lipid.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelial lipase (EC:3.1.1.3)
Alternative name(s):
Endothelial-derived lipase
Short name:
EDL
Gene namesi
Name:Lipg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi1310740. Lipg.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: Ensembl
  • early endosome Source: Ensembl
  • extracellular space Source: RGD
  • Golgi apparatus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3638354.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000004340924 – 493Endothelial lipaseAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi66 ↔ 79PROSITE-ProRule annotation
Glycosylationi67N-linked (GlcNAc...)Sequence analysis1
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi254 ↔ 274PROSITE-ProRule annotation
Disulfide bondi299 ↔ 318PROSITE-ProRule annotation
Disulfide bondi310 ↔ 313PROSITE-ProRule annotation
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi465 ↔ 485PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8VBX1.
PRIDEiQ8VBX1.

Expressioni

Gene expression databases

BgeeiENSRNOG00000018694.
GenevisibleiQ8VBX1. RN.

Interactioni

Subunit structurei

Head to tail Homodimer. Interacts with apolipoprotein C-2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025257.

Chemistry databases

BindingDBiQ8VBX1.

Structurei

3D structure databases

ProteinModelPortaliQ8VBX1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini349 – 484PLATPROSITE-ProRule annotationAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni327 – 339Heparin-bindingBy similarityAdd BLAST13

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ8VBX1.
KOiK01046.
OMAiQSWYNLW.
OrthoDBiEOG091G052B.
PhylomeDBiQ8VBX1.
TreeFamiTF324997.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 2 hits.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8VBX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDPVFLLGF WSLYCCFPAG SLTTLRPQGS LRDEHHKPTG VPVTITTKPS
60 70 80 90 100
VTFNIRTSKD PEHEGCNLSL GDSKLLENCG FNMTAKTFFI IHGWTMSGMF
110 120 130 140 150
ESWLHKLVSA LQTREKEANV VVVDWLPLAH QLYIDAVSNT RVVGRRVAGM
160 170 180 190 200
LNWLQEKGEF SLGDVHLIGY SLGAHVAGYA GNFVKGTVGR ITGLDPAGPM
210 220 230 240 250
FEGVDINRRL SPDDADFVDV LHTYTLSFGL SIGIRMPVGH IDIYPNGGDF
260 270 280 290 300
QPGCGFNDVM GSFAYGTISE MVKCEHERAV HLFVDSLVNQ DKPSFAFQCT
310 320 330 340 350
DPNRFKRGIC LSCRKNRCNN IGYNAKKMRK KRNSKMYLKT RAGMPFRVYH
360 370 380 390 400
YQLKVHMFSY KNSGDIQPDL YITLYGSNAD SQNLPLEIVE KIELNATNTF
410 420 430 440 450
LVYTEEYLGD LFKIRLTWEG VSSSWYNLWN EFRSYLSQPS SPSRELHIRR
460 470 480 490
IRVKSGETQR KVAFCVQDPM KNSISPGQEL WFYKCQNDCR VKN
Length:493
Mass (Da):55,924
Last modified:December 6, 2005 - v2
Checksum:i11F8E39B2E2FCBC5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti275 – 277EHE → KHK in AAK14774 (PubMed:11924532).Curated3
Sequence conflicti275 – 277EHE → KHK in AAK14775 (PubMed:11924532).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY916123 mRNA. Translation: AAX11354.1.
AY027561 Genomic DNA. Translation: AAK14774.1.
AY027562 Genomic DNA. Translation: AAK14775.1.
RefSeqiNP_001012759.1. NM_001012741.1.
UniGeneiRn.199051.

Genome annotation databases

EnsembliENSRNOT00000025257; ENSRNOP00000025257; ENSRNOG00000018694.
GeneIDi291437.
KEGGirno:291437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY916123 mRNA. Translation: AAX11354.1.
AY027561 Genomic DNA. Translation: AAK14774.1.
AY027562 Genomic DNA. Translation: AAK14775.1.
RefSeqiNP_001012759.1. NM_001012741.1.
UniGeneiRn.199051.

3D structure databases

ProteinModelPortaliQ8VBX1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025257.

Chemistry databases

BindingDBiQ8VBX1.
ChEMBLiCHEMBL3638354.

Proteomic databases

PaxDbiQ8VBX1.
PRIDEiQ8VBX1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025257; ENSRNOP00000025257; ENSRNOG00000018694.
GeneIDi291437.
KEGGirno:291437.

Organism-specific databases

CTDi9388.
RGDi1310740. Lipg.

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ8VBX1.
KOiK01046.
OMAiQSWYNLW.
OrthoDBiEOG091G052B.
PhylomeDBiQ8VBX1.
TreeFamiTF324997.

Enzyme and pathway databases

ReactomeiR-RNO-192456. Digestion of dietary lipid.

Miscellaneous databases

PROiQ8VBX1.

Gene expression databases

BgeeiENSRNOG00000018694.
GenevisibleiQ8VBX1. RN.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 2 hits.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIPE_RAT
AccessioniPrimary (citable) accession number: Q8VBX1
Secondary accession number(s): Q5D216
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 6, 2005
Last modified: November 30, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

It is termed endothelial lipase due to the fact that it is synthesized in endothelial cells, a characteristic that distinguishes it from other members of the family. However, this protein is also expressed in other cell types.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.