Q4V888 · PP4P2_RAT
- ProteinType 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- GenePip4p2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids257 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity).
Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity).
Negatively regulates the phagocytosis of large particles by reducing phagosomal phosphatidylinositol 4,5-bisphosphate accumulation during cup formation (By similarity).
Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity).
Negatively regulates the phagocytosis of large particles by reducing phagosomal phosphatidylinositol 4,5-bisphosphate accumulation during cup formation (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 107 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | late endosome membrane | |
Cellular Component | lysosomal membrane | |
Cellular Component | phagocytic vesicle membrane | |
Cellular Component | plasma membrane | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity | |
Biological Process | negative regulation of phagocytosis | |
Biological Process | phosphatidylinositol dephosphorylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameType 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- EC number
- Short namesType 2 PtdIns-4,5-P2 4-Ptase
- 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 accessionQ4V888
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Late endosome membrane ; Multi-pass membrane protein
Lysosome membrane ; Multi-pass membrane protein
Cytoplasmic vesicle, phagosome membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 192-212 | Helical | ||||
Sequence: CCAYVTIGMICIFIGVGLTVG | ||||||
Transmembrane | 227-247 | Helical | ||||
Sequence: WAIAYLLGLICLIRACYWGAI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000235230 | 1-257 | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase | |||
Sequence: MAADGVDERSPLLSASHSGNVTPTAPPYLQESSPRAELPPPYTAIASPGTSGIPVINCRVCQSLINLDGKLHQHVVKCTVCNEATPIKTPPTGKKYVRCPCNCLLICKDTSRRIGCPRPNCRRIINLGPIMLISEEQPAQPALPVQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKISSVGSALPRRRCCAYVTIGMICIFIGVGLTVGTQDFSRRFHATYVSWAIAYLLGLICLIRACYWGAIRVSYPEHGFA | ||||||
Modified residue | 22 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 33 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: MAADGVDERSPLLSASHSGNVTPTAPPYLQESSPRAELPPPYT | ||||||
Compositional bias | 13-29 | Polar residues | ||||
Sequence: LSASHSGNVTPTAPPYL | ||||||
Motif | 107-113 | CX5R motif | ||||
Sequence: CKDTSRR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length257
- Mass (Da)28,024
- Last updated2005-07-05 v1
- Checksum783E51EA20B1F71F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AGE6 | A0A8I6AGE6_RAT | Pip4p2 | 253 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-29 | Polar residues | ||||
Sequence: LSASHSGNVTPTAPPYL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC097492 EMBL· GenBank· DDBJ | AAH97492.1 EMBL· GenBank· DDBJ | mRNA |