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Q9WVG5 (LIPE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endothelial lipase
EC=3.1.1.3
Alternative name(s):
Endothelial cell-derived lipase
Short name=EDL
Gene names
Name:Lipg
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Head to tail homodimer By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed in placenta, lung, liver, testis and spleen.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 500480Endothelial lipase
PRO_0000017798

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

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation3931N-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

Experimental info

Sequence conflict281Q → E in AAH20991. Ref.3
Sequence conflict4241Y → C in AAD30435. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WVG5 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: D4B8A4A291810759

FASTA50056,629
        10         20         30         40         50         60 
MRNTVFLLGF WSVYCYFPAG SITTLRPQGS LRDEHHKPTG VPATARPSVA FNIRTSKDPE 

        70         80         90        100        110        120 
QEGCNLSLGD SKLLENCGFN MTAKTFFIIH GWTMSGMFES WLHKLVSALQ MREKDANVVV 

       130        140        150        160        170        180 
VDWLPLAHQL YTDAVNNTRV VGQRVAGMLD WLQEKEEFSL GNVHLIGYSL GAHVAGYAGN 

       190        200        210        220        230        240 
FVKGTVGRIT GLDPAGPMFE GVDINRRLSP DDADFVDVLH TYTLSFGLSI GIRMPVGHID 

       250        260        270        280        290        300 
IYPNGGDFQP GCGFNDVIGS FAYGTISEMV KCEHERAVHL FVDSLVNQDK PSFAFQCTDS 

       310        320        330        340        350        360 
SRFKRGICLS CRKNRCNNIG YNAKKMRKKR NSKMYLKTRA GMPFKVYHYQ LKVHMFSYNN 

       370        380        390        400        410        420 
SGDTQPTLYI TLYGSNADSQ NLPLEIVEKI ELNATNTFLV YTEEDLGDLL KMRLTWEGVA 

       430        440        450        460        470        480 
HSWYNLWNEF RNYLSQPSNP SRELYIRRIR VKSGETQRKV TFCTQDPTKS SISPGQELWF 

       490        500 
HKCQDGWKMK NKTSPFVNLA

« Hide

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: 10318835] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF118768 mRNA. Translation: AAD30435.1.
AC125122 Genomic DNA. No translation available.
BC020991 mRNA. Translation: AAH20991.1.
IPIIPI00323023.
RefSeqNP_034850.3. NM_010720.3.
UniGeneMm.299647.

3D structure databases

ProteinModelPortalQ9WVG5.
SMRQ9WVG5. Positions 13-483.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9WVG5.

Proteomic databases

PRIDEQ9WVG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066532; ENSMUSP00000066536; ENSMUSG00000053846.
GeneID16891.
KEGGmmu:16891.

Organism-specific databases

CTD9388.
MGIMGI:1341803. Lipg.

Phylogenomic databases

GeneTreeENSGT00560000077136.
HOGENOMHBG445376.
HOVERGENHBG002259.
InParanoidQ9WVG5.
OrthoDBEOG4320Z4.

Gene expression databases

ArrayExpressQ9WVG5.
BgeeQ9WVG5.
CleanExMM_LIPG.
GenevestigatorQ9WVG5.
GermOnlineENSMUSG00000053846. Mus musculus.

Family and domain databases

InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002330. Lipo_Lipase.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
KOK01046.
PANTHERPTHR11610. Lipase. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameLIPE_MOUSE
AccessionPrimary (citable) accession number: Q9WVG5
Secondary accession number(s): Q8VDU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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