Q9D6D8
Gene name |
Ppil6 |
Protein name |
Probable inactive peptidyl-prolyl cis-trans isomerase-like 6 |
Names |
PPIase, Cyclophilin-like protein PPIL6 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:73075 |
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 Q9D6D8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9D6D8-F1 | Predicted | AlphaFoldDB |
11 variants for Q9D6D8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs261018098 | 16 | C>Y | No | EVA | |
| rs226330880 | 17 | H>R | No | EVA | |
| rs242400779 | 18 | V>L | No | EVA | |
| rs3389096512 | 55 | Y>* | No | EVA | |
| rs3389107304 | 159 | R>S | No | EVA | |
| rs47934396 | 161 | I>V | No | EVA | |
| rs224888467 | 163 | E>D | No | EVA | |
| rs3389092103 | 204 | V>D | No | EVA | |
| rs3389100694 | 205 | Q>* | No | EVA | |
| rs3389096550 | 213 | D>Y | No | EVA | |
| rs215082958 | 252 | H>R | No | EVA |
No associated diseases with Q9D6D8
1 regional properties for Q9D6D8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain | 147 - 310 | IPR002130 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein peptidyl-prolyl isomerization | The modification of a protein by cis-trans isomerization of a proline residue. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATQQPCRPK | SKPPACHVRL | PPEPPLKLKV | VGLFKSSSFQ | VSKTIAETLK | TSYPYRFEDP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIVPLQEFAW | DQFLEEKKRE | LKGETWVYSS | YVMCFVNDQL | LGNAFDLKKW | AQKVWDVIDV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RPSALYEALT | LDYATKFLKD | TKHDFVYLDI | CIDLSPIGRL | IFELYCDACP | RTCTNFQVLC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TGTSGFSERG | TKLHYKDSIF | HRVVQNGWIQ | GGDIVQGRGD | DGESIYGPTF | EDENFSIPHN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KRGVLGMVNK | GHHTNGSQFY | ITLQAAPYLD | KKYVAFGQLI | EGTHVLKQLE | LVPTENERPL |
| 310 | |||||
| LLCSIADSGV | LYT |