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Q9Y5X9

- LIPE_HUMAN

UniProt

Q9Y5X9 - LIPE_HUMAN

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Protein

Endothelial lipase

Gene

LIPG

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691NucleophileBy similarity
Active sitei193 – 1931Charge relay systemPROSITE-ProRule annotation
Active sitei274 – 2741Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. lipoprotein lipase activity Source: InterPro
  3. phosphatidylcholine 1-acylhydrolase activity Source: MGI
  4. phospholipase activity Source: BHF-UCL

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. cholesterol homeostasis Source: BHF-UCL
  3. high-density lipoprotein particle remodeling Source: BHF-UCL
  4. lipid metabolic process Source: ProtInc
  5. phospholipid catabolic process Source: BHF-UCL
  6. phospholipid homeostasis Source: BHF-UCL
  7. positive regulation of cholesterol transport Source: BHF-UCL
  8. positive regulation of high-density lipoprotein particle clearance Source: BHF-UCL
  9. regulation of lipoprotein metabolic process Source: Ensembl
  10. response to nutrient Source: Ensembl
  11. reverse cholesterol transport Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

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
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6623. LIPG.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30395.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 500480Endothelial lipasePRO_0000017797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 77PROSITE-ProRule annotation
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi252 ↔ 272PROSITE-ProRule annotation
Disulfide bondi297 ↔ 316PROSITE-ProRule annotation
Disulfide bondi308 ↔ 311PROSITE-ProRule annotation
Glycosylationi393 – 3931N-linked (GlcNAc...)1 Publication
Disulfide bondi463 ↔ 483PROSITE-ProRule annotation
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Y5X9.
PaxDbiQ9Y5X9.
PRIDEiQ9Y5X9.

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

BgeeiQ9Y5X9.
CleanExiHS_LIPG.
ExpressionAtlasiQ9Y5X9. baseline and differential.
GenevestigatoriQ9Y5X9.

Organism-specific databases

HPAiHPA016966.

Interactioni

Subunit structurei

Head to tail homodimer.1 Publication

Protein-protein interaction databases

BioGridi114788. 3 interactions.
IntActiQ9Y5X9. 2 interactions.
STRINGi9606.ENSP00000261292.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5X9.
SMRiQ9Y5X9. Positions 13-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini347 – 482136PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 33713Heparin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 1214Poly-Val

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40923.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiQ9Y5X9.
KOiK01046.
OMAiCCFAAGS.
PhylomeDBiQ9Y5X9.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti476 – 4761R → Q in AAH60825. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261G → S.
Corresponds to variant rs9963243 [ dbSNP | Ensembl ].
VAR_034082
Natural varianti96 – 961G → S.1 Publication
VAR_017027
Natural varianti111 – 1111T → I.1 Publication
Corresponds to variant rs2000813 [ dbSNP | Ensembl ].
VAR_017028
Natural varianti312 – 3121R → H.1 Publication
VAR_017029

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei346 – 3549VYHYQMKIH → GNLQSLECP in isoform 2. 1 PublicationVSP_013302
Alternative sequencei355 – 500146Missing in isoform 2. 1 PublicationVSP_013303Add
BLAST

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_006024.1. NM_006033.2. [Q9Y5X9-1]
UniGeneiHs.465102.

Genome annotation databases

EnsembliENST00000261292; ENSP00000261292; ENSG00000101670. [Q9Y5X9-1]
ENST00000580036; ENSP00000462420; ENSG00000101670. [Q9Y5X9-2]
GeneIDi9388.
KEGGihsa:9388.
UCSCiuc002ldu.1. human. [Q9Y5X9-2]
uc002ldv.3. human. [Q9Y5X9-1]

Polymorphism databases

DMDMi22001808.

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 .
CCDSi CCDS11938.1. [Q9Y5X9-1 ]
RefSeqi NP_006024.1. NM_006033.2. [Q9Y5X9-1 ]
UniGenei Hs.465102.

3D structure databases

ProteinModelPortali Q9Y5X9.
SMRi Q9Y5X9. Positions 13-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114788. 3 interactions.
IntActi Q9Y5X9. 2 interactions.
STRINGi 9606.ENSP00000261292.

Chemistry

BindingDBi Q9Y5X9.
ChEMBLi CHEMBL5080.
GuidetoPHARMACOLOGYi 2591.

Polymorphism databases

DMDMi 22001808.

Proteomic databases

MaxQBi Q9Y5X9.
PaxDbi Q9Y5X9.
PRIDEi Q9Y5X9.

Protocols and materials databases

DNASUi 9388.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261292 ; ENSP00000261292 ; ENSG00000101670 . [Q9Y5X9-1 ]
ENST00000580036 ; ENSP00000462420 ; ENSG00000101670 . [Q9Y5X9-2 ]
GeneIDi 9388.
KEGGi hsa:9388.
UCSCi uc002ldu.1. human. [Q9Y5X9-2 ]
uc002ldv.3. human. [Q9Y5X9-1 ]

Organism-specific databases

CTDi 9388.
GeneCardsi GC18P047088.
HGNCi HGNC:6623. LIPG.
HPAi HPA016966.
MIMi 603684. gene.
neXtProti NX_Q9Y5X9.
PharmGKBi PA30395.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40923.
GeneTreei ENSGT00760000119069.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.
InParanoidi Q9Y5X9.
KOi K01046.
OMAi CCFAAGS.
PhylomeDBi Q9Y5X9.
TreeFami TF324997.

Miscellaneous databases

ChiTaRSi LIPG. human.
GenomeRNAii 9388.
NextBioi 35175.
PMAP-CutDB Q9Y5X9.
PROi Q9Y5X9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5X9.
CleanExi HS_LIPG.
ExpressionAtlasi Q9Y5X9. baseline and differential.
Genevestigatori Q9Y5X9.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. 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. 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.

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: October 29, 2014
This is version 134 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

External Data

Dasty 3