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Protein

Endothelial lipase

Gene

LIPG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

Inhibited by serum.

Sites

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

GO - Molecular functioni

  • heparin binding Source: UniProtKB-KW
  • lipoprotein lipase activity Source: Reactome
  • phosphatidylcholine 1-acylhydrolase activity Source: MGI
  • phospholipase activity Source: BHF-UCL

GO - Biological processi

  • cell proliferation Source: Ensembl
  • cholesterol homeostasis Source: BHF-UCL
  • high-density lipoprotein particle remodeling Source: BHF-UCL
  • lipid digestion Source: Reactome
  • lipid metabolic process Source: ProtInc
  • phospholipid catabolic process Source: BHF-UCL
  • phospholipid homeostasis Source: BHF-UCL
  • positive regulation of cholesterol transport Source: BHF-UCL
  • positive regulation of high-density lipoprotein particle clearance Source: BHF-UCL
  • regulation of lipoprotein metabolic process Source: Ensembl
  • response to nutrient Source: Ensembl
  • reverse cholesterol transport Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:HS02298-MONOMER.
ReactomeiR-HSA-192456. Digestion of dietary lipid.

Protein family/group databases

ESTHERihuman-LIPG. Lipoprotein_Lipase.

Chemistry databases

SwissLipidsiSLP:000000567.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelial lipase (EC:3.1.1.3)
Alternative name(s):
Endothelial cell-derived lipase
Short name:
EDL
Short name:
EL
Gene namesi
Name:LIPG
ORF Names:UNQ387/PRO719
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:6623. LIPG.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • early endosome Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • Golgi apparatus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi9388.
OpenTargetsiENSG00000101670.
PharmGKBiPA30395.

Chemistry databases

ChEMBLiCHEMBL5080.
GuidetoPHARMACOLOGYi2591.

Polymorphism and mutation databases

BioMutaiLIPG.
DMDMi22001808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001779721 – 500Endothelial lipaseAdd BLAST480

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi64 ↔ 77PROSITE-ProRule annotation
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Glycosylationi136N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi252 ↔ 272PROSITE-ProRule annotation
Disulfide bondi297 ↔ 316PROSITE-ProRule annotation
Disulfide bondi308 ↔ 311PROSITE-ProRule annotation
Glycosylationi393N-linked (GlcNAc...)1 Publication1
Disulfide bondi463 ↔ 483PROSITE-ProRule annotation
Glycosylationi469N-linked (GlcNAc...)Sequence analysis1
Glycosylationi491N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y5X9.
PeptideAtlasiQ9Y5X9.
PRIDEiQ9Y5X9.

PTM databases

iPTMnetiQ9Y5X9.
PhosphoSitePlusiQ9Y5X9.

Miscellaneous databases

PMAP-CutDBQ9Y5X9.

Expressioni

Tissue specificityi

High level of expression in the liver, placenta, lung, thyroid, kidney, testis and in the corpus luteum of the ovary. Expressed also in coronary artery endothelial cells, umbilical vein endothelial cells and in hepatocytes and osteosarcoma cell lines. Not detected in heart, brain and muscle.

Gene expression databases

BgeeiENSG00000101670.
CleanExiHS_LIPG.
ExpressionAtlasiQ9Y5X9. baseline and differential.
GenevisibleiQ9Y5X9. HS.

Organism-specific databases

HPAiHPA016966.

Interactioni

Subunit structurei

Head to tail homodimer.1 Publication

Protein-protein interaction databases

BioGridi114788. 22 interactors.
IntActiQ9Y5X9. 2 interactors.
STRINGi9606.ENSP00000261292.

Chemistry databases

BindingDBiQ9Y5X9.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5X9.
SMRiQ9Y5X9.
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
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ9Y5X9.
KOiK01046.
OMAiQSWYNLW.
OrthoDBiEOG091G052B.
PhylomeDBiQ9Y5X9.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y5X9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSNSVPLLCF WSLCYCFAAG SPVPFGPEGR LEDKLHKPKA TQTEVKPSVR
60 70 80 90 100
FNLRTSKDPE HEGCYLSVGH SQPLEDCSFN MTAKTFFIIH GWTMSGIFEN
110 120 130 140 150
WLHKLVSALH TREKDANVVV VDWLPLAHQL YTDAVNNTRV VGHSIARMLD
160 170 180 190 200
WLQEKDDFSL GNVHLIGYSL GAHVAGYAGN FVKGTVGRIT GLDPAGPMFE
210 220 230 240 250
GADIHKRLSP DDADFVDVLH TYTRSFGLSI GIQMPVGHID IYPNGGDFQP
260 270 280 290 300
GCGLNDVLGS IAYGTITEVV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS
310 320 330 340 350
NRFKKGICLS CRKNRCNSIG YNAKKMRNKR NSKMYLKTRA GMPFRVYHYQ
360 370 380 390 400
MKIHVFSYKN MGEIEPTFYV TLYGTNADSQ TLPLEIVERI EQNATNTFLV
410 420 430 440 450
YTEEDLGDLL KIQLTWEGAS QSWYNLWKEF RSYLSQPRNP GRELNIRRIR
460 470 480 490 500
VKSGETQRKL TFCTEDPENT SISPGRELWF RKCRDGWRMK NETSPTVELP
Length:500
Mass (Da):56,795
Last modified:November 1, 1999 - v1
Checksum:i96EC95125CD2A3FD
GO
Isoform 2 (identifier: Q9Y5X9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     346-354: VYHYQMKIH → GNLQSLECP
     355-500: Missing.

Note: No experimental confirmation available.
Show »
Length:354
Mass (Da):39,362
Checksum:i939A47B18F97B7FA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti476R → Q in AAH60825 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03408226G → S.Corresponds to variant rs9963243dbSNPEnsembl.1
Natural variantiVAR_01702796G → S.1 PublicationCorresponds to variant rs150879681dbSNPEnsembl.1
Natural variantiVAR_017028111T → I.1 PublicationCorresponds to variant rs2000813dbSNPEnsembl.1
Natural variantiVAR_017029312R → H.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_013302346 – 354VYHYQMKIH → GNLQSLECP in isoform 2. 1 Publication9
Alternative sequenceiVSP_013303355 – 500Missing in isoform 2. 1 PublicationAdd BLAST146

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118767 mRNA. Translation: AAD30434.1.
AY358928 mRNA. Translation: AAQ89287.1.
EU332856 Genomic DNA. Translation: ABY87545.1.
CH471096 Genomic DNA. Translation: EAW62947.1.
BC060825 mRNA. Translation: AAH60825.1.
CCDSiCCDS11938.1. [Q9Y5X9-1]
RefSeqiNP_001294935.1. NM_001308006.1.
NP_006024.1. NM_006033.3. [Q9Y5X9-1]
UniGeneiHs.465102.

Genome annotation databases

EnsembliENST00000261292; ENSP00000261292; ENSG00000101670. [Q9Y5X9-1]
ENST00000580036; ENSP00000462420; ENSG00000101670. [Q9Y5X9-2]
GeneIDi9388.
KEGGihsa:9388.
UCSCiuc002ldu.2. human. [Q9Y5X9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118767 mRNA. Translation: AAD30434.1.
AY358928 mRNA. Translation: AAQ89287.1.
EU332856 Genomic DNA. Translation: ABY87545.1.
CH471096 Genomic DNA. Translation: EAW62947.1.
BC060825 mRNA. Translation: AAH60825.1.
CCDSiCCDS11938.1. [Q9Y5X9-1]
RefSeqiNP_001294935.1. NM_001308006.1.
NP_006024.1. NM_006033.3. [Q9Y5X9-1]
UniGeneiHs.465102.

3D structure databases

ProteinModelPortaliQ9Y5X9.
SMRiQ9Y5X9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114788. 22 interactors.
IntActiQ9Y5X9. 2 interactors.
STRINGi9606.ENSP00000261292.

Chemistry databases

BindingDBiQ9Y5X9.
ChEMBLiCHEMBL5080.
GuidetoPHARMACOLOGYi2591.
SwissLipidsiSLP:000000567.

Protein family/group databases

ESTHERihuman-LIPG. Lipoprotein_Lipase.

PTM databases

iPTMnetiQ9Y5X9.
PhosphoSitePlusiQ9Y5X9.

Polymorphism and mutation databases

BioMutaiLIPG.
DMDMi22001808.

Proteomic databases

PaxDbiQ9Y5X9.
PeptideAtlasiQ9Y5X9.
PRIDEiQ9Y5X9.

Protocols and materials databases

DNASUi9388.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261292; ENSP00000261292; ENSG00000101670. [Q9Y5X9-1]
ENST00000580036; ENSP00000462420; ENSG00000101670. [Q9Y5X9-2]
GeneIDi9388.
KEGGihsa:9388.
UCSCiuc002ldu.2. human. [Q9Y5X9-1]

Organism-specific databases

CTDi9388.
DisGeNETi9388.
GeneCardsiLIPG.
HGNCiHGNC:6623. LIPG.
HPAiHPA016966.
MIMi603684. gene.
neXtProtiNX_Q9Y5X9.
OpenTargetsiENSG00000101670.
PharmGKBiPA30395.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJUA. Eukaryota.
ENOG4111GMM. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ9Y5X9.
KOiK01046.
OMAiQSWYNLW.
OrthoDBiEOG091G052B.
PhylomeDBiQ9Y5X9.
TreeFamiTF324997.

Enzyme and pathway databases

BioCyciZFISH:HS02298-MONOMER.
ReactomeiR-HSA-192456. Digestion of dietary lipid.

Miscellaneous databases

ChiTaRSiLIPG. human.
GenomeRNAii9388.
PMAP-CutDBQ9Y5X9.
PROiQ9Y5X9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101670.
CleanExiHS_LIPG.
ExpressionAtlasiQ9Y5X9. baseline and differential.
GenevisibleiQ9Y5X9. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X9
Secondary accession number(s): B0LPG6, Q6P9C8, Q6UW82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.