Reviewed,
UniProtKB/Swiss-Prot Q8VBX1 (LIPE_RAT)
Last modified
November 3, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Endothelial lipase EC=3.1.1.3 Alternative name(s): Endothelial-derived lipase Short name=EDL | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 493 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Heparin-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | cell proliferation Inferred from direct assay. Source: RGD lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW response to nutrientInferred from expression pattern. Source: RGD |
| Cellular component | extracellular space Inferred from direct assay. Source: RGD |
| Molecular function | heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipoprotein lipase activityInferred from electronic annotation. Source: InterPro triglyceride lipase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 493 | 470 | Endothelial lipase | PRO_0000043409 | |||||||
Regions | |||||||||||
| Domain | 349 – 484 | 136 | PLAT | ||||||||
| Region | 327 – 339 | 13 | Heparin-binding By similarity | ||||||||
Sites | |||||||||||
| Active site | 171 | 1 | Nucleophile By similarity | ||||||||
| Active site | 195 | 1 | Charge relay system By similarity | ||||||||
| Active site | 276 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 67 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 82 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 395 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 66 ↔ 79 | By similarity | |||||||||
| Disulfide bond | 254 ↔ 274 | By similarity | |||||||||
| Disulfide bond | 299 ↔ 318 | By similarity | |||||||||
| Disulfide bond | 310 ↔ 313 | By similarity | |||||||||
| Disulfide bond | 465 ↔ 485 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 275 – 277 | 3 | EHE → KHK in AAK14774. Ref.2 | ||||||||
| Sequence conflict | 275 – 277 | 3 | EHE → KHK in AAK14775. Ref.2 | ||||||||
Sequences
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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. | |
| IPI | IPI00555274. |
| RefSeq | NP_001012759.1. |
| UniGene | Rn.199051 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LPB based on UniProtKB P16233. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8VBX1. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000025257; ENSRNOP00000025257; ENSRNOG00000018694; Rattus norvegicus. [Genome view] |
| GeneID | 291437. |
| KEGG | rno:291437. |
| NMPDR | fig|10116.3.peg.14388. |
| UCSC | NM_001012741. rat. |
Organism-specific databases | |
| CTD | 291437. |
| RGD | 1310740. Lipg. |
Phylogenomic databases | |
| HOVERGEN | Q8VBX1. |
| OMA | SQSWYNL. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.3. 248. |
Gene expression databases | |
| ArrayExpress | Q8VBX1. |
| Genevestigator | Q8VBX1. |
| GermOnline | ENSRNOG00000018694. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000734. Lipase. IPR013818. Lipase_N. IPR008262. Lipase_Ser_AS. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view] |
| PANTHER | PTHR11610. Lipase. 1 hit. |
| Pfam | PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view] |
| PIRSF | PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit. |
| PRINTS | PR00822. LIPOLIPASE. PR00821. TAGLIPASE. |
| SMART | SM00308. LH2. 1 hit. [Graphical view] |
| PROSITE | PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 632583. |
Entry information
| Entry name | LIPE_RAT | ||||||||
| Accession | Primary (citable) accession number: Q8VBX1 Secondary accession number(s): Q5D216 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


