A0A9W7FYV9 · A0A9W7FYV9_9STRA
- ProteinInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1135 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Catalytic activity
- 1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | diphosphoinositol-pentakisphosphate kinase activity | |
Molecular Function | inositol heptakisphosphate kinase activity | |
Molecular Function | inositol hexakisphosphate kinase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Sar > Stramenopiles > Ochrophyta > Bolidophyceae > Parmales > Triparmaceae > Triparma
Accessions
- Primary accessionA0A9W7FYV9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1099-1119 | Helical | ||||
Sequence: WLWGAIASVSLGLGMMCFTMA |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-102 | VIP1 N-terminal | ||||
Sequence: IILGVCAMDKKSRSKPMAEILSRLDPYLFDIIIFGNKCILEDEVEDWPVVDVLIAFYSAGFPLDKAESYVSLRNPFVLNDLGMQRTLMD | ||||||
Compositional bias | 360-385 | Polar residues | ||||
Sequence: PTKSSGGGIMGDTFFTDPGQTSEPST | ||||||
Region | 360-469 | Disordered | ||||
Sequence: PTKSSGGGIMGDTFFTDPGQTSEPSTPEREGDQEVRTINTPSMSQPTTLSEGAPHVREISNAPSANSESSDQPQDSKSRVRVGTSEPGRDRGMSNAESNEDSWNRGGEVK | ||||||
Compositional bias | 395-410 | Polar residues | ||||
Sequence: RTINTPSMSQPTTLSE | ||||||
Compositional bias | 419-440 | Polar residues | ||||
Sequence: SNAPSANSESSDQPQDSKSRVR | ||||||
Region | 997-1034 | Disordered | ||||
Sequence: RFSFVPDYATSRETSPTKKEETGGDGLGGSVATPKKAG |
Sequence similarities
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,135
- Mass (Da)127,621
- Last updated2023-11-08 v1
- Checksum332D7CD59F6CAE1A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 360-385 | Polar residues | ||||
Sequence: PTKSSGGGIMGDTFFTDPGQTSEPST | ||||||
Compositional bias | 395-410 | Polar residues | ||||
Sequence: RTINTPSMSQPTTLSE | ||||||
Compositional bias | 419-440 | Polar residues | ||||
Sequence: SNAPSANSESSDQPQDSKSRVR |
Keywords
- Technical term