Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8VBX1 (LIPE_RAT)

Last modified November 3, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Endothelial lipase
    EC=3.1.1.3
Alternative name(s):
    Endothelial-derived lipase
      Short name=EDL
Gene names
Name: Lipg
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length493 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

Homodimer. Interacts with apolipoprotein C-2 By similarity.

Subcellular location

Secreted By similarity.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 493470Endothelial lipase
PRO_0000043409

Regions

Domain349 – 484136PLAT
Region327 – 33913Heparin-binding By similarity

Sites

Active site1711Nucleophile By similarity
Active site1951Charge relay system By similarity
Active site2761Charge relay system By similarity

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Disulfide bond66 ↔ 79 By similarity
Disulfide bond254 ↔ 274 By similarity
Disulfide bond299 ↔ 318 By similarity
Disulfide bond310 ↔ 313 By similarity
Disulfide bond465 ↔ 485 By similarity

Experimental info

Sequence conflict275 – 2773EHE → KHK in AAK14774. Ref.2
Sequence conflict275 – 2773EHE → KHK in AAK14775. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8VBX1-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 11F8E39B2E2FCBC5

FASTA49355,924
        10         20         30         40         50         60 
MRDPVFLLGF WSLYCCFPAG SLTTLRPQGS LRDEHHKPTG VPVTITTKPS VTFNIRTSKD 

        70         80         90        100        110        120 
PEHEGCNLSL GDSKLLENCG FNMTAKTFFI IHGWTMSGMF ESWLHKLVSA LQTREKEANV 

       130        140        150        160        170        180 
VVVDWLPLAH QLYIDAVSNT RVVGRRVAGM LNWLQEKGEF SLGDVHLIGY SLGAHVAGYA 

       190        200        210        220        230        240 
GNFVKGTVGR ITGLDPAGPM FEGVDINRRL SPDDADFVDV LHTYTLSFGL SIGIRMPVGH 

       250        260        270        280        290        300 
IDIYPNGGDF QPGCGFNDVM GSFAYGTISE MVKCEHERAV HLFVDSLVNQ DKPSFAFQCT 

       310        320        330        340        350        360 
DPNRFKRGIC LSCRKNRCNN IGYNAKKMRK KRNSKMYLKT RAGMPFRVYH YQLKVHMFSY 

       370        380        390        400        410        420 
KNSGDIQPDL YITLYGSNAD SQNLPLEIVE KIELNATNTF LVYTEEYLGD LFKIRLTWEG 

       430        440        450        460        470        480 
VSSSWYNLWN EFRSYLSQPS SPSRELHIRR IRVKSGETQR KVAFCVQDPM KNSISPGQEL 

       490 
WFYKCQNDCR VKN 

« Hide

References

[1]"Increased expression of endothelial lipase in rat models of hypertension."
Shimokawa Y., Hirata K., Ishida T., Kojima Y., Inoue N., Quertermous T., Yokoyama M.
Cardiovasc. Res. 66:594-600(2005) [PubMed: 15914124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Aortic smooth muscle.
[2]"Sequencing and chromosomal assignment of the rat endothelial-derived lipase gene (Lipg)."
Bonne A.C.M., den Bieman M.G., van Lith H., van Zutphen B.F.M.
DNA Seq. 12:285-287(2001) [PubMed: 11924532] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-293.
Strain: BN-Lx/Cub and SHR/OlaIpcv.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY916123 mRNA. Translation: AAX11354.1.
AY027561 Genomic DNA. Translation: AAK14774.1.
AY027562 Genomic DNA. Translation: AAK14775.1.
IPIIPI00555274.
RefSeqNP_001012759.1.
UniGeneRn.199051

3D structure databases

HSSPHSSP built from PDB template 1LPB based on UniProtKB P16233.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8VBX1.

Genome annotation databases

EnsemblENSRNOT00000025257; ENSRNOP00000025257; ENSRNOG00000018694; Rattus norvegicus. [Genome view]
GeneID291437.
KEGGrno:291437.
NMPDRfig|10116.3.peg.14388.
UCSCNM_001012741. rat.

Organism-specific databases

CTD291437.
RGD1310740. Lipg.

Phylogenomic databases

HOVERGENQ8VBX1.
OMASQSWYNL.

Enzyme and pathway databases

BRENDA3.1.1.3. 248.

Gene expression databases

ArrayExpressQ8VBX1.
GenevestigatorQ8VBX1.
GermOnlineENSRNOG00000018694. Rattus norvegicus.

Family and domain databases

InterProIPR000734. Lipase.
IPR013818. Lipase_N.
IPR008262. Lipase_Ser_AS.
IPR002330. Lipo_Lipase.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
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]
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio632583.

Entry information

Entry nameLIPE_RAT
AccessionPrimary (citable) accession number: Q8VBX1
Secondary accession number(s): Q5D216
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 6, 2005
Last modified: November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents