A7E300
Gene name |
DLC1 (ARHGAP7, STARD12) |
Protein name |
Rho GTPase-activating protein 7 |
Names |
Deleted in liver cancer 1 protein homolog, DLC-1, Rho-type GTPase-activating protein 7, START domain-containing protein 12, StARD12, StAR-related lipid transfer protein 12 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
bta:511433 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
662-868 (Rho-GAP domain) |
Relief mechanism |
Cleavage |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A7E300
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7E300-F1 | Predicted | AlphaFoldDB |
No variants for A7E300
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A7E300 | |||||
No associated diseases with A7E300
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
| lipid binding | Binding to a lipid. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| regulation of Rho protein signal transduction | Any process that modulates the frequency, rate or extent of Rho protein signal transduction. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| B9VTT2 | DLC1 | Rho GTPase-activating protein 7 | Canis lupus familiaris (Dog) (Canis familiaris) | SS |
| Q9P2N2 | ARHGAP28 | Rho GTPase-activating protein 28 | Homo sapiens (Human) | PR |
| Q8BN58 | Arhgap28 | Rho GTPase-activating protein 28 | Mus musculus (Mouse) | PR |
| Q9R0Z9 | Dlc1 | Rho GTPase-activating protein 7 | Mus musculus (Mouse) | SS |
| Q63744 | Dlc1 | Rho GTPase-activating protein 7 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTQAHSKSCF | HQFWDGLQIK | RSSDSFTVEL | LPSLGATINH | SNKLQKFIIS | PYDPRYRSWE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LFLIVLVVYS | AWICPFELAF | LRDLPSKLLL | VENIVDIFFA | IDIVLTFFVA | YVDSKTHLLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DDRKRIAMRY | LSTWFIFDVC | STAPFQPIIL | LFTHKGNDIA | FKVLNLLRLW | RLHRVSSLFA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLEKDIRFNY | FWTRCSKLIS | VTLFAVHCAG | CFNYMIADRY | PNPEKTWIGA | VMSTFRSESL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WTRYITALYW | SITTLTTTGY | GDLHAENPTE | MLFDIVYMMF | NLGLTAYLIG | NMTNLVVHGT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SRTRKFRDSI | QAASEFAARN | QLPENIKQQV | LSHFCLQFKT | EGLNQQVMLD | CLPKGIRSSI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AYSLFFPIIR | QAYLFNGVSG | NFIAELVMEV | QAEYFPPKED | IILQNEGEAD | VYIVVSGAVN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IITTIHGNEQ | VYEKIAEGEM | FGEVGSLCNI | PQPFTCRTAE | LSQLLRISKT | RLREIIEENR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EDSNILMNNL | VQKLKLRESL | PDMNQPDRRF | LSKYELFHVP | REAWLLKKSQ | LHYTEHTSRD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SSNNTPVFGG | DRYSRQLLGE | ATRSSASENE | NSSMTDKEEN | HDEVHTNCEI | KKRTEEHCIQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| INSEDSSSTY | SQRTMNATVQ | TGSPHKTEEN | ITRRIPDEYY | IKEANKRVTI | HKYRHNSTVS |
| 670 | 680 | 690 | 700 | 710 | |
| AAQNGKLIKL | PTSLEELFKI | GSQKFQGFHP | RKVVSRDYAE | IDDVSVIRDG | DHLFLLEM |