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Q9Y5X9 (LIPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endothelial lipase

EC=3.1.1.3
Alternative name(s):
Endothelial cell-derived lipase
Short name=EDL
Short name=EL
Gene names
Name:LIPG
ORF Names:UNQ387/PRO719
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulation

Inhibited by serum.

Subunit structure

Head to tail homodimer. Ref.9

Subcellular location

Secreted.

Tissue specificity

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.

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.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

lipid metabolic process

Traceable author statement Ref.2Ref.1. Source: ProtInc

phospholipid catabolic process

Non-traceable author statement PubMed 19136670. Source: BHF-UCL

phospholipid homeostasis

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

positive regulation of cholesterol transport

Inferred from direct assay PubMed 19136670. Source: BHF-UCL

positive regulation of high-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

regulation of lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

   Cellular_componentextracellular space

Inferred from direct assay Ref.2. Source: BHF-UCL

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein lipase activity

Inferred from electronic annotation. Source: InterPro

phosphatidylcholine 1-acylhydrolase activity

Inferred from direct assay Ref.1. Source: MGI

phospholipase activity

Inferred from direct assay Ref.2. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5X9-1)

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.
Isoform 2 (identifier: Q9Y5X9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     346-354: VYHYQMKIH → GNLQSLECP
     355-500: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 500480Endothelial lipase
PRO_0000017797

Regions

Domain347 – 482136PLAT
Region325 – 33713Heparin-binding By similarity
Compositional bias118 – 1214Poly-Val

Sites

Active site1691Nucleophile By similarity
Active site1931Charge relay system By similarity
Active site2741Charge relay system By similarity

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Ref.8
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 77 By similarity
Disulfide bond252 ↔ 272 By similarity
Disulfide bond297 ↔ 316 By similarity
Disulfide bond308 ↔ 311 By similarity
Disulfide bond463 ↔ 483 By similarity

Natural variations

Alternative sequence346 – 3549VYHYQMKIH → GNLQSLECP in isoform 2.
VSP_013302
Alternative sequence355 – 500146Missing in isoform 2.
VSP_013303
Natural variant261G → S.
Corresponds to variant rs9963243 [ dbSNP | Ensembl ].
VAR_034082
Natural variant961G → S. Ref.10
VAR_017027
Natural variant1111T → I. Ref.10
Corresponds to variant rs2000813 [ dbSNP | Ensembl ].
VAR_017028
Natural variant3121R → H. Ref.10
VAR_017029

Experimental info

Sequence conflict4761R → Q in AAH60825. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 96EC95125CD2A3FD

FASTA50056,795
        10         20         30         40         50         60 
MSNSVPLLCF WSLCYCFAAG SPVPFGPEGR LEDKLHKPKA TQTEVKPSVR FNLRTSKDPE 

        70         80         90        100        110        120 
HEGCYLSVGH SQPLEDCSFN MTAKTFFIIH GWTMSGIFEN WLHKLVSALH TREKDANVVV 

       130        140        150        160        170        180 
VDWLPLAHQL YTDAVNNTRV VGHSIARMLD WLQEKDDFSL GNVHLIGYSL GAHVAGYAGN 

       190        200        210        220        230        240 
FVKGTVGRIT GLDPAGPMFE GADIHKRLSP DDADFVDVLH TYTRSFGLSI GIQMPVGHID 

       250        260        270        280        290        300 
IYPNGGDFQP GCGLNDVLGS IAYGTITEVV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS 

       310        320        330        340        350        360 
NRFKKGICLS CRKNRCNSIG YNAKKMRNKR NSKMYLKTRA GMPFRVYHYQ MKIHVFSYKN 

       370        380        390        400        410        420 
MGEIEPTFYV TLYGTNADSQ TLPLEIVERI EQNATNTFLV YTEEDLGDLL KIQLTWEGAS 

       430        440        450        460        470        480 
QSWYNLWKEF RSYLSQPRNP GRELNIRRIR VKSGETQRKL TFCTEDPENT SISPGRELWF 

       490        500 
RKCRDGWRMK NETSPTVELP 

« Hide

Isoform 2 [UniParc].

Checksum: 939A47B18F97B7FA
Show »

FASTA35439,362

References

« Hide 'large scale' references
[1]"Cloning of a unique lipase from endothelial cells extends the lipase gene family."
Hirata K., Dichek H.L., Cioffi J.A., Choi S.Y., Leeper N.J., Quintana L., Kronmal G.S., Cooper A.D., Quertermous T.
J. Biol. Chem. 274:14170-14175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Endothelial cell.
[2]"A novel endothelial-derived lipase that modulates HDL metabolism."
Jaye M., Lynch K.J., Krawiec J., Marchadier D., Maugeais C., Doan K., South V., Amin D., Perrone M., Rader D.J.
Nat. Genet. 21:424-428(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[7]"Characterization of the lipolytic activity of endothelial lipase."
McCoy M.G., Sun G.-S., Marchadier D., Maugeais C., Glick J.M., Rader D.J.
J. Lipid Res. 43:921-929(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-393.
Tissue: Plasma.
[9]"Identification of the active form of endothelial lipase, a homodimer in a head-to-tail conformation."
Griffon N., Jin W., Petty T.J., Millar J., Badellino K.O., Saven J.G., Marchadier D.H., Kempner E.S., Billheimer J., Glick J.M., Rader D.J.
J. Biol. Chem. 284:23322-23330(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-96; ILE-111 AND HIS-312.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11938.1. [Q9Y5X9-1]
RefSeqNP_006024.1. NM_006033.2. [Q9Y5X9-1]
UniGeneHs.465102.

3D structure databases

ProteinModelPortalQ9Y5X9.
SMRQ9Y5X9. Positions 13-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114788. 3 interactions.
IntActQ9Y5X9. 2 interactions.
STRING9606.ENSP00000261292.

Chemistry

BindingDBQ9Y5X9.
ChEMBLCHEMBL5080.
GuidetoPHARMACOLOGY2591.

Polymorphism databases

DMDM22001808.

Proteomic databases

MaxQBQ9Y5X9.
PaxDbQ9Y5X9.
PRIDEQ9Y5X9.

Protocols and materials databases

DNASU9388.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261292; ENSP00000261292; ENSG00000101670. [Q9Y5X9-1]
ENST00000580036; ENSP00000462420; ENSG00000101670. [Q9Y5X9-2]
GeneID9388.
KEGGhsa:9388.
UCSCuc002ldu.1. human. [Q9Y5X9-2]
uc002ldv.3. human. [Q9Y5X9-1]

Organism-specific databases

CTD9388.
GeneCardsGC18P047088.
HGNCHGNC:6623. LIPG.
HPAHPA016966.
MIM603684. gene.
neXtProtNX_Q9Y5X9.
PharmGKBPA30395.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidQ9Y5X9.
KOK01046.
OMACCFAAGS.
PhylomeDBQ9Y5X9.
TreeFamTF324997.

Gene expression databases

ArrayExpressQ9Y5X9.
BgeeQ9Y5X9.
CleanExHS_LIPG.
GenevestigatorQ9Y5X9.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIPG. human.
GenomeRNAi9388.
NextBio35175.
PMAP-CutDBQ9Y5X9.
PROQ9Y5X9.
SOURCESearch...

Entry information

Entry nameLIPE_HUMAN
AccessionPrimary (citable) accession number: Q9Y5X9
Secondary accession number(s): B0LPG6, Q6P9C8, Q6UW82
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM