O88370 · PI42C_RAT
- ProteinPhosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- GenePip4k2c
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids420 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic activity (PubMed:9685379).
May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity (By similarity).
PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity (By similarity).
PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + GDP + H+This reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | autophagosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | intracellular organelle | |
Cellular Component | plasma membrane | |
Molecular Function | 1-phosphatidylinositol-4-phosphate 5-kinase activity | |
Molecular Function | 1-phosphatidylinositol-5-phosphate 4-kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Biological Process | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process | |
Biological Process | negative regulation of insulin receptor signaling pathway | |
Biological Process | phosphatidylinositol biosynthetic process | |
Biological Process | phosphatidylinositol phosphate biosynthetic process | |
Biological Process | positive regulation of autophagosome assembly | |
Biological Process | regulation of autophagy |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO88370
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000285753 | 2-420 | Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma | |||
Sequence: ASSSVPPATAPAAAGGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEGPVREEESEWDGDCNLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPEGGVFHGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFISNIFA | ||||||
Modified residue | 26 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 349 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated, phosphorylation is induced by EGF.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with the most abundant expression in kidney.
Gene expression databases
Interaction
Subunit
Interacts with PIP5K1A; the interaction inhibits PIP5K1A kinase activity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-419 | PIPK | ||||
Sequence: AADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEGPVREEESEWDGDCNLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPEGGVFHGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFISNIF | ||||||
Region | 69-75 | Required for interaction with PIP5K1A | ||||
Sequence: VMLLPDD |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length420
- Mass (Da)47,049
- Last updated1998-11-01 v1
- ChecksumBDB07F67FA81E943
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2RB78 | A0A8L2RB78_RAT | Pip4k2c | 432 | ||
G3V9W5 | G3V9W5_RAT | Pip4k2c | 421 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF030558 EMBL· GenBank· DDBJ | AAC40202.1 EMBL· GenBank· DDBJ | mRNA |