Reviewed,
UniProtKB/Swiss-Prot Q29524 (LIPL_SHEEP)
Last modified
February 9, 2010.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lipoprotein lipase Short name=LPL EC=3.1.1.34 | ||
| Gene names |
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| Organism | Ovis aries (Sheep) | ||
| Taxonomic identifier | 9940 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 478 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 | The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium. |
| Catalytic activity | Triacylglycerol + H2O = diacylglycerol + a carboxylate. |
| Subunit structure | Homodimer. Interacts with apolipoprotein C-2. Interacts with GPIHBP1. |
| Subcellular location | |
| Post-translational modification | Tyrosine nitrated in vivo after lipopolysaccharide (LPS) challenge, which down-regulates lipoprotein lipase activity By similarity. |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Cell membrane Chylomicron Membrane VLDL |
| Domain | Signal |
| Ligand | Heparin-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond GPI-anchor Glycoprotein Lipoprotein Nitration |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell chylomicronInferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-KW very-low-density lipoprotein particleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipoprotein 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 – 27 | 27 | Potential | ||||||||
| Chain | 28 – 478 | 451 | Lipoprotein lipase | PRO_0000017781 | |||||||
Regions | |||||||||||
| Domain | 344 – 467 | 124 | PLAT | ||||||||
| Region | 322 – 334 | 13 | Heparin-binding Potential | ||||||||
Sites | |||||||||||
| Active site | 162 | 1 | Nucleophile | ||||||||
| Active site | 186 | 1 | Charge relay system | ||||||||
| Active site | 271 | 1 | Charge relay system | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 124 | 1 | Nitrated tyrosine By similarity | ||||||||
| Modified residue | 130 | 1 | Nitrated tyrosine By similarity | ||||||||
| Modified residue | 318 | 1 | Nitrated tyrosine By similarity | ||||||||
| Glycosylation | 73 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 389 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 57 ↔ 70 | By similarity | |||||||||
| Disulfide bond | 246 ↔ 269 | By similarity | |||||||||
| Disulfide bond | 294 ↔ 313 | By similarity | |||||||||
| Disulfide bond | 305 ↔ 308 | By similarity | |||||||||
| Disulfide bond | 448 ↔ 468 | By similarity | |||||||||
Sequences
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References
| [1] | "Cloning and sequencing of a full length cDNA encoding ovine lipoprotein lipase." Edwards W.D., Daniels S.W., Page R.A., Volpe C.P., Kille P., Sweeney G.E., Cryer A. Biochim. Biophys. Acta 1172:167-170(1993) [PubMed: 8439555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Welsh Mountain/Dorset. Tissue: Adipose tissue. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X68308 mRNA. Translation: CAA48384.1. |
| PIR | S29846. |
| RefSeq | NP_001009394.1. |
| UniGene | Oar.13297 |
3D structure databases | |
| SMR | Q29524. Positions 38-454. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 443408. |
Organism-specific databases | |
| CTD | 443408. |
Phylogenomic databases | |
| HOVERGEN | Q29524. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.34. 271. |
Family and domain databases | |
| InterPro | IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view] |
| PANTHER | PTHR11610. Lipase. 1 hit. PTHR11610:SF3. Lipase_lipo. 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] |
| TIGRFAMs | TIGR03230. lipo_lipase. 1 hit. |
| PROSITE | PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIPL_SHEEP | ||||||||
| Accession | Primary (citable) accession number: Q29524 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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