A0AAI9SYY1 · A0AAI9SYY1_9ASCO
- ProteinAcyl-coenzyme A diphosphatase SCS3
- GeneSCS3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1065 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis. May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation. May play a role in the regulation of cell morphology and cytoskeletal organization. Involved in phospholipid biosynthesis.
Catalytic activity
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H+ + S-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-4'-phosphopantetheine
- (9Z)-octadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H+ + S-(9Z-octadecenoyl)-4'-phosphopantetheine
- H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H+ + S-hexadecanoyl-4'-phosphopantetheine
- an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-phosphopantetheine + 2 H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 950 | |||||
Sequence: H | ||||||
Active site | 1035 | |||||
Sequence: H |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcyl-coenzyme A diphosphatase SCS3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionA0AAI9SYY1
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 | 20-40 | Helical | ||||
Sequence: GYLVISLINLLCNCAVLSIWW | ||||||
Transmembrane | 47-67 | Helical | ||||
Sequence: VYLLFASINVIEILISISIIQ | ||||||
Transmembrane | 87-110 | Helical | ||||
Sequence: LFVLCGAFMIGQSIMGISIVVLIN | ||||||
Transmembrane | 122-146 | Helical | ||||
Sequence: LIFTYDVLSFCLGLLYVACTAVASV | ||||||
Transmembrane | 161-180 | Helical | ||||
Sequence: ISLPILFGITVGILMIEIGC | ||||||
Transmembrane | 766-786 | Helical | ||||
Sequence: LLIISLYILNFVLSRLIHFGA | ||||||
Transmembrane | 811-831 | Helical | ||||
Sequence: WGWTTLVIMFYYFGHVFRYLI | ||||||
Transmembrane | 843-866 | Helical | ||||
Sequence: AKIGTVIGGAILRYGLATIWWYLF | ||||||
Transmembrane | 1011-1034 | Helical | ||||
Sequence: LAQLSIVFLIALWWFMLLMTNVYF | ||||||
Transmembrane | 1041-1061 | Helical | ||||
Sequence: LVGLMFGYVGIFVIYFIPRWI |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 258-299 | Basic and acidic residues | ||||
Sequence: KHEKVGEQSENQREQQKQQQQHKQQKQQHNKKEKEINENHLE | ||||||
Region | 258-330 | Disordered | ||||
Sequence: KHEKVGEQSENQREQQKQQQQHKQQKQQHNKKEKEINENHLEKLQTESTLASNQPGSHEKKQSHHKKAMHTAF | ||||||
Compositional bias | 300-314 | Polar residues | ||||
Sequence: KLQTESTLASNQPGS | ||||||
Coiled coil | 365-397 | |||||
Sequence: KNQLKKLAKKSKQAKQQKELASLENNTEKFYQE | ||||||
Domain | 592-679 | BioF2-like acetyltransferase | ||||
Sequence: WEFIYNLGNFANDQKYRSLLFLKVGDKIIASCVIFRLGETMTSDIQGLDHEISKKYKAYFVMMQEVIKMGLRENVSFIDFGPTTEEAK |
Sequence similarities
Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,065
- Mass (Da)122,767
- Last updated2024-07-24 v1
- Checksum81AEF50028982D30
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 258-299 | Basic and acidic residues | ||||
Sequence: KHEKVGEQSENQREQQKQQQQHKQQKQQHNKKEKEINENHLE | ||||||
Compositional bias | 300-314 | Polar residues | ||||
Sequence: KLQTESTLASNQPGS |