A4FUD6
Gene name |
ELMO2 |
Protein name |
Engulfment and cell motility protein 2 |
Names |
|
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:508361 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
1-113 (Ras-binding domain) |
Relief mechanism |
Partner binding |
Assay |
|
Target domain |
1-113 (Ras-binding domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Patel M et al. (2011) "The Arf family GTPase Arl4A complexes with ELMO proteins to promote actin cytoskeleton remodeling and reveals a versatile Ras-binding domain in the ELMO proteins family", The Journal of biological chemistry, 286, 38969-79
- Patel M et al. (2010) "An evolutionarily conserved autoinhibitory molecular switch in ELMO proteins regulates Rac signaling", Current biology : CB, 20, 2021-7
- Patel M et al. (2011) "Opening up on ELMO regulation: New insights into the control of Rac signaling by the DOCK180/ELMO complex", Small GTPases, 2, 268-275
Autoinhibited structure

Activated structure

1 structures for A4FUD6
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-A4FUD6-F1 | Predicted | AlphaFoldDB |
No variants for A4FUD6
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for A4FUD6 |
No associated diseases with A4FUD6
4 regional properties for A4FUD6
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Homeobox domain | 505 - 569 | IPR001356 |
conserved_site | Homeobox, conserved site | 540 - 563 | IPR017970 |
domain | Homeobox domain, metazoa | 529 - 540 | IPR020479-1 |
domain | Homeobox domain, metazoa | 544 - 563 | IPR020479-2 |
2 GO annotations of cellular component
1 GO annotations of molecular function
Name | Definition |
---|---|
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. |
5 GO annotations of biological process
Name | Definition |
---|---|
actin filament organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
cell chemotaxis | The directed movement of a motile cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). |
cell motility | Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another. |
phagocytosis | A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles. |
8 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q08DZ3 | ELMOD2 | ELMO domain-containing protein 2 | Bos taurus (Bovine) | PR |
Q92556 | ELMO1 | Engulfment and cell motility protein 1 | Homo sapiens (Human) | EV |
Q96BJ8 | ELMO3 | Engulfment and cell motility protein 3 | Homo sapiens (Human) | SS |
Q96JJ3 | ELMO2 | Engulfment and cell motility protein 2 | Homo sapiens (Human) | SS |
Q8BPU7 | Elmo1 | Engulfment and cell motility protein 1 | Mus musculus (Mouse) | SS |
Q8BYZ7 | Elmo3 | Engulfment and cell motility protein 3 | Mus musculus (Mouse) | SS |
Q8BHL5 | Elmo2 | Engulfment and cell motility protein 2 | Mus musculus (Mouse) | SS |
Q499U2 | Elmo3 | Engulfment and cell motility protein 3 | Rattus norvegicus (Rat) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MPPPSDIVKV | AIEWPGANAQ | LLEIDQKRPL | ASIIKEVCDG | WSLPNPEYYT | LRYADGPQLY |
70 | 80 | 90 | 100 | 110 | 120 |
ITEQTRSDIK | NGTILQLAIS | PSRAARQLME | RTQSSSMETR | LDAMKELAKL | SADVTFATEF |
130 | 140 | 150 | 160 | 170 | 180 |
INMDGIVVLT | RLVESGTKLL | SHYSEMLAFT | LTAFLELMDH | GIVSWDMVSI | TFIKQIAGYV |
190 | 200 | 210 | 220 | 230 | 240 |
SQPMVDVSIL | QRSLAILESM | VLNSQSLYQK | IAEEITVGQL | ISHLQVSNQE | IQTYAIALIN |
250 | 260 | 270 | 280 | 290 | 300 |
ALFLKAPEDK | RQDMANAFAQ | KHLRSIILNH | VIRGNRPIKT | EMAHQLYVLQ | VLTFNLLEER |
310 | 320 | 330 | 340 | 350 | 360 |
MMTKMDPNDQ | AQRDIIFELR | RIAFDADSDP | SNAPGSGTEK | RKAMYTKDYK | MLGFTNHINP |
370 | 380 | 390 | 400 | 410 | 420 |
AMDFTQTPPG | MLALDNMLYL | AKVHQDTYIR | IVLENSSRED | KHECPFGRSA | IELTKMLCEI |
430 | 440 | 450 | 460 | 470 | 480 |
LQVGELPNEG | RNDYHPMFFT | HDRAFEELFG | ICIQLLNKTW | KEMRATAEDF | NKVMQVVREQ |
490 | 500 | 510 | 520 | 530 | 540 |
ITRALPSKPN | SLDQFKSKLR | SLSYSEILRL | RQSERMSQDD | FQSPPIVELR | EKIQPEILEL |
550 | 560 | 570 | 580 | 590 | 600 |
IKQQRLNRLC | EGSSFRKIGN | RRRQERFWYC | RLALNHKVLH | YGDLDDNPQG | EVTFESLQEK |
610 | 620 | 630 | 640 | 650 | 660 |
IPVADIKAIV | TGKDCPHMKE | KSALKQNKEV | LELAFSILYD | PDETLNFIAP | NKYEYCIWID |
670 | 680 | 690 | 700 | 710 | |
GLSALLGKDM | SSELTKSDRD | TLLSMEMKLR | LLDLENIQIP | EAPPPVPKEP | SSYDFVYHYG |