Q5FWK3
Gene name |
Arhgap1 |
Protein name |
Rho GTPase-activating protein 1 |
Names |
Rho-type GTPase-activating protein 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:228359 |
EC number |
|
Protein Class |
|
Descriptions
(Annotation based on sequence homology with Q07960)
Rho GTPase-activating protein 1 (p50RhoGAP) comprises an N-terminal BCH domain and a C-terminal GAP domain separated by a proline-rich region. p50RhoGAP contains a non-canonical RhoA-binding motif in its BCH domain and is associated with GAP-mediated cell rounding. In the autoinhibited state, the GAP catalytic residue is being occluded and incapable of RhoA inactivation, and it only becomes accessible upon the release of autoinhibition of GAP from the BCH domain. The lipid binding to BCH domain may initiate the transition for the release of GAP domain from the inactive state to the active state of p50RhoGAP. This leads to the activation of the GAP domain of p50RhoGAP, resulting in the GAP-mediated GTPase inactivation of RhoA.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5FWK3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5FWK3-F1 | Predicted | AlphaFoldDB |
16 variants for Q5FWK3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388569655 | 55 | V>L | No | EVA | |
| rs3388572348 | 94 | P>T | No | EVA | |
| rs3388570102 | 149 | R>P | No | EVA | |
| rs3388567618 | 186 | I>N | No | EVA | |
| rs3388566408 | 196 | S>G | No | EVA | |
| rs3388572424 | 207 | P>L | No | EVA | |
| rs3388567608 | 207 | P>S | No | EVA | |
| rs3388572241 | 221 | Q>* | No | EVA | |
| rs3388567611 | 256 | Q>H | No | EVA | |
| rs13474079 | 257 | D>E | No | EVA | |
| rs3413037099 | 270 | L>F | No | EVA | |
| rs3388569690 | 272 | A>V | No | EVA | |
| rs3388574168 | 284 | S>A | No | EVA | |
| rs3388570355 | 368 | L>R | No | EVA | |
| rs3388569660 | 406 | A>V | No | EVA | |
| rs218608657 | 437 | Q>* | No | EVA |
No associated diseases with Q5FWK3
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell leading edge | The area of a motile cell closest to the direction of movement. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| endosome membrane | The lipid bilayer surrounding an endosome. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
| sorting endosome | A multivesicular body surrounded by and connected with multiple tubular compartments with associated vesicles. |
3 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. |
| SH3 domain binding | Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. |
| small GTPase binding | Binding to a small monomeric GTPase. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| endosomal transport | The directed movement of substances mediated by an endosome, a membrane-bounded organelle that carries materials enclosed in the lumen or located in the endosomal membrane. |
| negative regulation of endocytic recycling | Any process that stops, prevents or reduces the frequency, rate or extent of endocytic recycling. |
| regulation of GTPase activity | Any process that modulates the rate of GTP hydrolysis by a GTPase. |
| small GTPase mediated signal transduction | The series of molecular signals in which a small monomeric GTPase relays a signal. |
| transferrin transport | The directed movement of transferrin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDPLSELQDD | LTLDDTSQAL | NQLKLASIDE | KNWPSDEMPD | FPKSDDSKSS | SPEPVTHLKW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DDPYYDIARH | QIVEVAGDDK | YGRKIIVFSA | CRMPPSHQLD | HSKLLGYLKH | TLDQYVESDY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLLYLHHGLT | SDNKPSLSWL | RDAYREFDRK | YKKNIKALYI | VHPTMFIKTL | LILFKPLISF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KFGRKIFYVN | YLSELSEHVK | LEQLGIPRQV | LKYDDFLKST | QKSPATAPKP | MPPRPPLPNQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QFGVSLQHLQ | EKSPGQDPIP | IVLRETVAYL | QAHALTTEGI | FRRSANTQVV | REVQQKYNMG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPVDFDQYNE | LHLPAVILKT | FLRELPEPLL | TFDLYPHVVG | FLNIDESQRV | EVTQQVLQTL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PEENYQVLHF | LTAFLVQISA | HCDQNKMTNT | NLAVVFGPNL | LWAKDAAITL | KAINPINTFT |
| 430 | |||||
| KFLLDHQGEL | FPSTDAQGV |