B4I557 · B4I557_DROSE
- ProteinO-acyltransferase
- GeneDsec\GM17212
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids607 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H+ = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2OThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoateThis reaction proceeds in the forward direction.
- hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-dihexadecanoyl-1,2-hexadecanediol + 2 CoAThis reaction proceeds in the forward direction.
- hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; glycerolipid metabolism.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 527 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | diacylglycerol O-acyltransferase activity | |
Molecular Function | retinol O-fatty-acyltransferase activity | |
Biological Process | negative regulation of lipid storage | |
Biological Process | regulation of nurse cell apoptotic process | |
Biological Process | triglyceride biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameO-acyltransferase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionB4I557
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 168-194 | Helical | ||||
Sequence: LFSWSSGFTNFSGLVNWGFLLLCIGGL | ||||||
Transmembrane | 228-245 | Helical | ||||
Sequence: ALILCIYSLVHISLCLAV | ||||||
Transmembrane | 257-278 | Helical | ||||
Sequence: GLGLFIQIVNIVVLVCLPVVTI | ||||||
Transmembrane | 284-305 | Helical | ||||
Sequence: AFSLMGASTVCFFYSVLFLKLW | ||||||
Transmembrane | 394-413 | Helical | ||||
Sequence: LLEVVIGVNVVMALFQQWII | ||||||
Transmembrane | 440-461 | Helical | ||||
Sequence: LPNHLCWLCFFYLLFHSFLNAV | ||||||
Transmembrane | 515-531 | Helical | ||||
Sequence: ASTIVFLFSAVFHEYLV | ||||||
Transmembrane | 567-588 | Helical | ||||
Sequence: MGNIIVWASIILGQPLCIMAYY |
Keywords
- Cellular component
Interaction
Subunit
Homodimer or homotetramer; both forms have similar enzymatic activities.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 26-43 | Polar residues | ||||
Sequence: HFRNVASSPSNRKKTSTM | ||||||
Region | 26-165 | Disordered | ||||
Sequence: HFRNVASSPSNRKKTSTMTTNKDPQDKEPGKAEQPTKNGGSSGVGIMKRLRRSASATEHNLSSLRNRKSTQNLFDQHGNPIDLRQYRKVLDKDENGNGTNGSEKKLRYRRTQSVTRAEEISNKEEKQRRAQPGRPIHQPR | ||||||
Compositional bias | 44-58 | Basic and acidic residues | ||||
Sequence: TTNKDPQDKEPGKAE | ||||||
Compositional bias | 81-103 | Polar residues | ||||
Sequence: ATEHNLSSLRNRKSTQNLFDQHG | ||||||
Compositional bias | 106-160 | Basic and acidic residues | ||||
Sequence: IDLRQYRKVLDKDENGNGTNGSEKKLRYRRTQSVTRAEEISNKEEKQRRAQPGRP |
Sequence similarities
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length607
- Mass (Da)69,771
- Last updated2008-09-23 v1
- ChecksumF24D092CB9D68E44
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 26-43 | Polar residues | ||||
Sequence: HFRNVASSPSNRKKTSTM | ||||||
Compositional bias | 44-58 | Basic and acidic residues | ||||
Sequence: TTNKDPQDKEPGKAE | ||||||
Compositional bias | 81-103 | Polar residues | ||||
Sequence: ATEHNLSSLRNRKSTQNLFDQHG | ||||||
Compositional bias | 106-160 | Basic and acidic residues | ||||
Sequence: IDLRQYRKVLDKDENGNGTNGSEKKLRYRRTQSVTRAEEISNKEEKQRRAQPGRP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH480822 EMBL· GenBank· DDBJ | EDW55513.1 EMBL· GenBank· DDBJ | Genomic DNA |