Q7TNR9
Gene name |
Arhgef4 (Kiaa1112) |
Protein name |
Rho guanine nucleotide exchange factor 4 |
Names |
APC-stimulated guanine nucleotide exchange factor, Asef |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:226970 |
EC number |
|
Protein Class |
RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4 (PTHR47544) |
Descriptions
The Rac-specific guanine nucleotide exchange factor (GEF) Asef is activated by binding to the tumor suppressor adenoma- tous polyposis coli mutant, which is found in sporadic and familial colorectal tumors. This activated Asef is involved in the migration of colorectal tumor cells. The GEFs for Rho family GTPases contain the Dbl homology (DH) domain and the pleckstrin homology (PH) domain. When Asef is in the resting state, the GEF activity of the DH-PH module is intramolecularly inhibited by its Src homology 3 (SH3) domain. Binding of the armadillo repeats of APC to a core APC-binding (CAB) motif within ASEF positioned adjacent to the SH3 domain relieves autoinhibition.
Autoinhibitory domains (AIDs)
Target domain |
78-262 (DH domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis, Deletion assay |
Accessory elements
No accessory elements
References
- Hamann MJ et al. (2007) "Asef2 functions as a Cdc42 exchange factor and is stimulated by the release of an autoinhibitory module from a concealed C-terminal activation element", Molecular and cellular biology, 27, 1380-93
- Murayama K et al. (2007) "Crystal structure of the rac activator, Asef, reveals its autoinhibitory mechanism", The Journal of biological chemistry, 282, 4238-4242
- Mitin N et al. (2007) "Release of autoinhibition of ASEF by APC leads to CDC42 activation and tumor suppression", Nature structural & molecular biology, 14, 814-23
Autoinhibited structure
Activated structure
1 structures for Q7TNR9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7TNR9-F1 | Predicted | AlphaFoldDB |
2 variants for Q7TNR9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1132442013 | 132 | R>C | No | Ensembl | |
| rs247305826 | 362 | S>T | No | Ensembl |
No associated diseases with Q7TNR9
4 regional properties for Q7TNR9
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR47544 | RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4 |
| PANTHER Subfamily | PTHR47544:SF1 | RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4 |
| PANTHER Protein Class |
guanyl-nucleotide exchange factor
G-protein modulator protein-binding activity modulator |
|
| PANTHER Pathway Category | No pathway information available | |
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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| guanyl-nucleotide exchange factor activity | Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions. |
| protein domain specific binding | Binding to a specific domain of a protein. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| filopodium assembly | The assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| lamellipodium assembly | Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q58DL7 | ARHGEF9 | Rho guanine nucleotide exchange factor 9 | Bos taurus (Bovine) | SS |
| Q70Z35 | PREX2 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein | Homo sapiens (Human) | SS |
| Q6XZF7 | DNMBP | Dynamin-binding protein | Homo sapiens (Human) | PR |
| A1IGU5 | ARHGEF37 | Rho guanine nucleotide exchange factor 37 | Homo sapiens (Human) | PR |
| Q8TCU6 | PREX1 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein | Homo sapiens (Human) | EV |
| Q96N96 | SPATA13 | Spermatogenesis-associated protein 13 | Homo sapiens (Human) | EV |
| O43307 | ARHGEF9 | Rho guanine nucleotide exchange factor 9 | Homo sapiens (Human) | SS |
| Q9NR80 | ARHGEF4 | Rho guanine nucleotide exchange factor 4 | Homo sapiens (Human) | EV |
| Q3LAC4 | Prex2 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein | Mus musculus (Mouse) | SS |
| Q69ZK0 | Prex1 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein | Mus musculus (Mouse) | SS |
| Q5DU57 | Spata13 | Spermatogenesis-associated protein 13 | Mus musculus (Mouse) | SS |
| Q3UTH8 | Arhgef9 | Rho guanine nucleotide exchange factor 9 | Mus musculus (Mouse) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDDQELGFKA | GDVIEVMDAT | NREWWWGRVA | DGEGWFPASF | VRLRVNQDEP | ADDYEAPRAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AREADDSGPE | AQSCKDQMRT | NVINEILSTE | RDYIKHLRDI | CEGYVRQCRK | REDMFSEEQL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTIFGNIEDI | YRCQKAFVKA | LEQKFNTERP | HLSELGACFL | EHQADFQIYS | EYCNNHPNAC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VELSRLTKLS | KYVYFFEACR | LLQRMIDISL | DGFLLTPVQK | ICKYPLQLAE | LLKYTHPQHR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DFKNVEAALH | AMKNVAQLIN | ERKRRLENID | KIAQWQSSIE | DWEGEDLLVR | SSELIHSGEL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TRVTQPQARS | QQRMFFLFDR | QLIYCKKDLL | RRDVLYYKGR | LDMDDLEVVD | VEDGKDRDLH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VSVKNAFRLY | CGTTGDSHLL | CARKPEQKQR | WLKAFARERE | QVRLDQETGF | SITELQRKQA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MLNASKQQAT | GKPKAVGRPG | YLTRHKHPSL | PASRPQQQVL | VLAEPRRKPS | NFWHSISRLA |
| PFRK |