Q9CZX7
Gene name |
Pip4p2 (Tmem55a) |
Protein name |
Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase |
Names |
Type 2 PtdIns-4,5-P2 4-Ptase, PtdIns-4,5-P2 4-Ptase II, Transmembrane protein 55A |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:72519 |
EC number |
3.1.3.78: Phosphoric monoester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9CZX7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9CZX7-F1 | Predicted | AlphaFoldDB |
11 variants for Q9CZX7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3412028286 | 86 | P>S | No | EVA | |
| rs3388667177 | 102 | N>T | No | EVA | |
| rs3388663141 | 116 | C>Y | No | EVA | |
| rs3412829884 | 175 | P>L | No | EVA | |
| rs3388674356 | 179 | K>N | No | EVA | |
| rs3388678586 | 192 | C>Y | No | EVA | |
| rs3388668769 | 210 | T>A | No | EVA | |
| rs3388660113 | 212 | G>D | No | EVA | |
| rs3388671317 | 216 | F>S | No | EVA | |
| rs3388671239 | 238 | L>R | No | EVA | |
| rs3388668764 | 251 | Y>C | No | EVA |
No associated diseases with Q9CZX7
No regional properties for Q9CZX7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9CZX7 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.78 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| late endosome membrane | The lipid bilayer surrounding a late endosome. |
| lysosomal membrane | The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. |
| phagocytic vesicle membrane | The lipid bilayer surrounding a phagocytic vesicle. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity | Catalysis of the reaction: 1-phosphatidyl-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of phagocytosis | Any process that stops, prevents, or reduces the frequency, rate or extent of phagocytosis. |
| phosphatidylinositol dephosphorylation | The process of removing one or more phosphate groups from a phosphatidylinositol. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3SZ48 | PIP4P2 | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase | Bos taurus (Bovine) | PR |
| Q8N4L2 | PIP4P2 | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase | Homo sapiens (Human) | PR |
| Q4V888 | Pip4p2 | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase | Rattus norvegicus (Rat) | PR |
| Q6DIE4 | pip4p2 | Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAADGVDERS | PLLSASHSGN | VTPTAPPYLQ | ESSPRAELPP | PYTAIASPGT | SGIPVINCRV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CQSLINLDGK | LHQHVVKCTV | CNEATPIKTP | PTGKKYVRCP | CNCLLICKDT | SRRIGCPRPN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CRRIINLGPV | MLISEEQPAQ | PALPIQPEGT | RVVCGHCGNT | FLWMELRFNT | LAKCPHCKKI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SSVGSALPRR | RCCAYVTIGM | ICIFIAVGLT | VGTQDFSRRF | HATYVSWAIA | YLLGLICLIR |
| 250 | |||||
| ACYWGAIRVS | YPEHGFA |