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 = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+This reaction proceeds in the forward direction.
- 1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H+This reaction proceeds in the forward direction.
- all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H+ + hexadecanoateThis reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 169 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 193 | Charge relay system | ||||
Sequence: D | ||||||
Binding site | 204 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 207 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 209 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 212 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 280 | Charge relay system | ||||
Sequence: H |
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 | triglyceride 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 | |||||
Sequence: MLLIWTLSLLLGAVLG | ||||||
Chain | PRO_5005126508 | 17-465 | Triacylglycerol lipase | |||
Sequence: SEVCFPRLGCFSDDAPWAGIVQRPLKILPWDPKDVNTRFLLYTNENQDNYQELVADPSTITDSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQVVGHLDFFPNGGKEMPGCQKNILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPCPSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSNEFDSDVEVGDLQKVKFIWYNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLTPC | ||||||
Disulfide bond | 20↔26 | |||||
Sequence: CFPRLGC | ||||||
Disulfide bond | 107↔118 | |||||
Sequence: CKNLFKVESVNC | ||||||
Disulfide bond | 254↔278 | |||||
Sequence: CQKNILSQIVDIDGIWEGTRDFVAC | ||||||
Disulfide bond | 302↔313 | |||||
Sequence: CDSYNVFTANKC | ||||||
Disulfide bond | 316↔321 | |||||
Sequence: CPSEGC | ||||||
Disulfide bond | 449↔465 | |||||
Sequence: CSQETVREEVLLTLTPC |
Keywords
- PTM
Interaction
Subunit
Forms a 1:1 stoichiometric complex with (pro)colipase/CLPS.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 355-465 | PLAT | ||||
Sequence: WRYKVSVTLSGKKVTGHILVSLFGNEGNSRQYEIYKGTLQPDNTHSNEFDSDVEVGDLQKVKFIWYNNVINPTLPRVGASKITVERNDGKVYDFCSQETVREEVLLTLTPC |
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
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 |