D4P6H2 · D4P6H2_PIG
- ProteinTriacylglycerol lipase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids465 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-octadecenoylglycerol + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + butanoate + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + hexadecanoate + H+This reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 169 | Nucleophile | |||
Active site | 193 | Charge relay system | |||
Binding site | 204 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 207 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 209 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 212 | Ca2+ (UniProtKB | ChEBI) | |||
Active site | 280 | Charge relay system | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity | |
Molecular Function | metal ion binding | |
Molecular Function | triacylglycerol lipase activity | |
Biological Process | lipid catabolic process |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTriacylglycerol lipase
- EC number
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionD4P6H2
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-16 | ||||
Chain | PRO_5005126508 | 17-465 | Triacylglycerol lipase | ||
Disulfide bond | 20↔26 | ||||
Disulfide bond | 107↔118 | ||||
Disulfide bond | 254↔278 | ||||
Disulfide bond | 302↔313 | ||||
Disulfide bond | 316↔321 | ||||
Disulfide bond | 449↔465 | ||||
Keywords
- PTM
Interaction
Subunit
Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length465
- Mass (Da)51,680
- Last updated2010-05-18 v1
- Checksum24E703643C4986FA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GU576971 EMBL· GenBank· DDBJ | ADD71520.1 EMBL· GenBank· DDBJ | mRNA |