Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y5X9

- LIPE_HUMAN

UniProt

Q9Y5X9 - LIPE_HUMAN

Protein

Endothelial lipase

Gene

LIPG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    ArrayExpressiQ9Y5X9.
    BgeeiQ9Y5X9.
    CleanExiHS_LIPG.
    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.
    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

    MSNSVPLLCF WSLCYCFAAG SPVPFGPEGR LEDKLHKPKA TQTEVKPSVR    50
    FNLRTSKDPE HEGCYLSVGH SQPLEDCSFN MTAKTFFIIH GWTMSGIFEN 100
    WLHKLVSALH TREKDANVVV VDWLPLAHQL YTDAVNNTRV VGHSIARMLD 150
    WLQEKDDFSL GNVHLIGYSL GAHVAGYAGN FVKGTVGRIT GLDPAGPMFE 200
    GADIHKRLSP DDADFVDVLH TYTRSFGLSI GIQMPVGHID IYPNGGDFQP 250
    GCGLNDVLGS IAYGTITEVV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS 300
    NRFKKGICLS CRKNRCNSIG YNAKKMRNKR NSKMYLKTRA GMPFRVYHYQ 350
    MKIHVFSYKN MGEIEPTFYV TLYGTNADSQ TLPLEIVERI EQNATNTFLV 400
    YTEEDLGDLL KIQLTWEGAS QSWYNLWKEF RSYLSQPRNP GRELNIRRIR 450
    VKSGETQRKL TFCTEDPENT SISPGRELWF RKCRDGWRMK NETSPTVELP 500
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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

    ArrayExpressi Q9Y5X9.
    Bgeei Q9Y5X9.
    CleanExi HS_LIPG.
    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

    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 1, 2014
    This is version 133 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