Q8VCF1
Gene name |
Cant1 |
Protein name |
Soluble calcium-activated nucleotidase 1 |
Names |
SCAN-1, Apyrase homolog |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:76025 |
EC number |
3.6.1.6: In phosphorus-containing anhydrides |
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 Q8VCF1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8VCF1-F1 | Predicted | AlphaFoldDB |
29 variants for Q8VCF1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1133040909 | 19 | R>W | No | EVA | |
| rs1132447207 | 23 | G>E | No | EVA | |
| rs3389223135 | 48 | T>K | No | EVA | |
| rs3389231445 | 92 | T>I | No | EVA | |
| rs3402980532 | 95 | L>P | No | EVA | |
| rs3402214567 | 96 | S>P | No | EVA | |
| rs3389156930 | 134 | G>A | No | EVA | |
| rs3402451689 | 141 | S>R | No | EVA | |
| rs3402933001 | 142 | G>W | No | EVA | |
| rs3389226020 | 164 | G>R | No | EVA | |
| rs3389185202 | 176 | N>K | No | EVA | |
| rs3403151219 | 190 | Y>H | No | EVA | |
| rs3389223147 | 200 | W>* | No | EVA | |
| rs3389185258 | 202 | I>M | No | EVA | |
| rs3389223545 | 227 | Y>F | No | EVA | |
| rs3389238090 | 232 | G>D | No | EVA | |
| rs3389231378 | 261 | H>Y | No | EVA | |
| rs3389223134 | 263 | N>T | No | EVA | |
| rs3402451732 | 282 | Y>* | No | EVA | |
| rs3401600017 | 282 | Y>C | No | EVA | |
| rs3402872111 | 282 | Y>D | No | EVA | |
| rs3402869515 | 287 | S>A | No | EVA | |
| rs3402843430 | 287 | S>F | No | EVA | |
| rs3402451645 | 288 | A>S | No | EVA | |
| rs3389216431 | 326 | A>P | No | EVA | |
| rs3389238082 | 337 | V>M | No | EVA | |
| rs247138130 | 341 | I>V | No | EVA | |
| rs3389216471 | 374 | T>I | No | EVA | |
| rs3389234463 | 394 | T>I | No | EVA |
No associated diseases with Q8VCF1
No regional properties for Q8VCF1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8VCF1 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.1.6 | In phosphorus-containing anhydrides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi cisterna membrane | The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ADP phosphatase activity | Catalysis of the reaction: ADP + H2O = AMP + phosphate. |
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| GDP phosphatase activity | Catalysis of the reaction: GDP + H2O = GMP + phosphate. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| UDP phosphatase activity | Catalysis of the reaction: UDP + H2O = UMP + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| proteoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans. |
| ribonucleoside diphosphate catabolic process | The chemical reactions and pathways resulting in the breakdown of a ribonucleoside diphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with diphosphate on the sugar. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPIQPFDQRE | WNEPMHSLRI | SVGGLPVLAS | MTKATDPRFR | PRWRVILTSF | VGAALLWLLY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SHHQGPVPGR | PPTHNAHNWR | LSQQRISHYN | DTYPLSPPQR | TPGGIRYRIA | VIADLDTGSR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQEENTWFSY | LKKGYLTLSD | SGDRVSVEWD | KDHGVLESHL | AEKGRGMELS | DLIVFNGKLY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SVDDRTGVIY | QIEGTKAVPW | VILSDGDGTV | EKGFKAEWLA | VKDEHLYVGG | LGKEWTTTTG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EVMNENPEWV | KVVGHRGSVD | HENWVSSYNA | LRAAAGIRPP | GYLIHESACW | SDTLQRWFFL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRRASHERYS | EKDDERKGSN | LLLSAAQDFR | DISVRQVGTL | IPTHGFSSFK | FIPNTDDQII |
| 370 | 380 | 390 | 400 | ||
| VALKSEEDNG | RIATYVMAFT | LDGRFLLPET | KIGTVKYEGI | EFI |