A7TK50
Gene name |
SFH5 (Kpol_1060p52) |
Protein name |
Phosphatidylinositol transfer protein SFH5 |
Names |
PITP SFH5 |
Species |
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus) |
KEGG Pathway |
vpo:Kpol_1060p52 |
EC number |
|
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 A7TK50
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7TK50-F1 | Predicted | AlphaFoldDB |
No variants for A7TK50
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A7TK50 | |||||
No associated diseases with A7TK50
1 regional properties for A7TK50
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | CRAL-TRIO lipid binding domain | 97 - 266 | IPR001251 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| phosphatidylinositol transfer activity | Removes phosphatidylinositol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNFSNDSEEK | VFNEIFDQLP | TLIKDKCSDY | DELYGYKLNY | NDSKEKLVEQ | YYDEDIAKAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IFKICKAYQF | DKTKIITSIV | DILNWRKSFN | PLSAAYKETH | NEALQTVGLL | TSYPDDEPNK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RVVTWNLYGQ | IVKKKELFKD | SSKFIRYRIG | LMERGLRLLD | FNNDANNYMT | QVHDYKGVSM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRLDSEIKAC | TKQVIAIFQK | YYPELLYAKY | FVNVPSILSW | MYDLMKSFID | EQTRKKFVVL |
| 250 | 260 | 270 | 280 | 290 | |
| NDGNKLGNYL | KSCPSENYGG | TDKKNNLQKQ | DVDTPRPTPY | ALYILESQAN | EDID |