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 Q40224
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q40224-F1 | Predicted | AlphaFoldDB |
No variants for Q40224
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q40224 | |||||
No associated diseases with Q40224
5 regional properties for Q40224
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ionotropic glutamate receptor, C-terminal | 459 - 799 | IPR001320-1 |
| domain | Ionotropic glutamate receptor, C-terminal | 798 - 830 | IPR001320-2 |
| domain | Solute-binding protein family 3/N-terminal domain of MltF | 472 - 797 | IPR001638 |
| domain | Receptor, ligand binding region | 48 - 400 | IPR001828 |
| domain | Plant glutamate receptor, periplasmic ligand-binding domain | 31 - 419 | IPR044440 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| heterotrimeric G-protein complex | Any of a family of heterotrimeric GTP-binding and hydrolyzing proteins; they belong to a superfamily of GTPases that includes monomeric proteins such as EF-Tu and RAS. Heterotrimeric G-proteins consist of three subunits; the alpha subunit contains the guanine nucleotide binding site and possesses GTPase activity; the beta and gamma subunits are tightly associated and function as a beta-gamma heterodimer; extrinsic plasma membrane proteins (cytoplasmic face) that function as a complex to transduce signals from G protein-coupled receptors to an effector protein. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| G protein-coupled receptor binding | Binding to a G protein-coupled receptor. |
| G-protein beta/gamma-subunit complex binding | Binding to a complex of G-protein beta/gamma subunits. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| adenylate cyclase-modulating G protein-coupled receptor signaling pathway | A G protein-coupled receptor signaling pathway in which the signal is transmitted via the activation or inhibition of adenylyl cyclase activity and a subsequent change in the intracellular concentration of cyclic AMP (cAMP). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGLLCSRNRR | YNDADAEENA | QAAEIERRIE | LETKAEKHIQ | KLLLLGAGES | GKSTIFKQIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLFQTGFDEA | ELKSYLPVIH | ANVFQTIKLL | HDGSKELAQN | DVDSSKYVIS | DENKDIGEKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SEIGSKLDYP | YLTTELAKEI | ETLWEDAAIQ | ETYARGNELQ | VPGCAHYFME | NLQRLSDANY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VPTKEDVLYA | RVRTTGVVEI | QFSPVGENKR | SGEVYRLFDV | GGQRNERRKW | IHLFEGVSAV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IFCAAISEYD | QTLFEDENKN | RMTETKELFE | WILKQPCFEK | TSFMLFLNKF | DIFEKKILKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLNVCEWFKD | YQPVSTGKQE | IEHAYEFVKK | KFEELYFQST | APERVDRVFK | VYRTTALDQK |
| 370 | 380 | ||||
| LIKKTFKLVD | ESLRRRNLFE | AGLL |