A0A5C6NN03 · A0A5C6NN03_9TELE
- ProteinHepatic triacylglycerol lipase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids513 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles. Also exhibits lysophospholipase activity. Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates. In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position.
Catalytic activity
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = 2,3-di-(9Z)-octadecenoyl-sn-glycerol + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 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)-sn-glycero-3-phosphocholine + H2O = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+This reaction proceeds in the forward direction.
- 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = 3-(9Z-octadecenoyl)-sn-glycerol + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + hexadecanoate + H+This reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | high-density lipoprotein particle | |
Molecular Function | 1-acyl-2-lysophosphatidylserine acylhydrolase activity | |
Molecular Function | apolipoprotein binding | |
Molecular Function | heparin binding | |
Molecular Function | lipoprotein lipase activity | |
Molecular Function | lysophospholipase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylserine 1-acylhydrolase activity | |
Molecular Function | phospholipase A1 activity | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | triglyceride catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHepatic triacylglycerol lipase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Takifugu
Accessions
- Primary accessionA0A5C6NN03
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MLVVKVLCCLLVVYQLNEA | ||||||
Chain | PRO_5022988649 | 20-513 | Hepatic triacylglycerol lipase | |||
Sequence: KKIKGSRAAEPNGALKAPHASLTSFRLFPEDEDECTVDPLQLHTLTSCGFNSSNPLIIITHGWSVDGMLESWILKLATALKSNLIHVNVVITDWLSLAQTHYPTAVKSTRAVGKDIAHLLQALRVHYRYPLKKVHLIGYSLGAHISGFAGSYLEGPEKIGRITGLDPAGPLFEGVSPSDRLSPDDADFVDAIHTFTRESMGFSVGINQAVAHYDFYPNGGDFQPGCDLRNIYEHISQHGLLGFEQTVKCAHERSVHLFIDSLINKDKQSRAYRCGDKSSFDRGVCLDCRRHRCNTLGYHINKAHTGASKRLYLKTRSQMPYKLYHYQFRVQFVNQMERIQPSLTISLTGTKEESGDIPITITEPISGKASLTFLITLDRDLGDLMLLKLRWEGTDVWKSVWNRVKTMIPWGGAEKQPLLTVGKISIKAGETQESGLLPAHLMSVTMFLCPRTTFCAMTHEEQQVQMSQDKVFVRCKEDSAKQRRRKRSGSVRDL |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 343-486 | PLAT | ||||
Sequence: YHYQFRVQFVNQMERIQPSLTISLTGTKEESGDIPITITEPISGKASLTFLITLDRDLGDLMLLKLRWEGTDVWKSVWNRVKTMIPWGGAEKQPLLTVGKISIKAGETQESGLLPAHLMSVTMFLCPRTTFCAMTHEEQQVQMS |
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)57,515
- Last updated2019-11-13 v1
- Checksum82C5899C5855E29B
Keywords
- Technical term