Q8HZQ5
Gene name |
EZR (VIL2) |
Protein name |
Ezrin |
Names |
Cytovillin, Villin-2, p81 |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100008846 |
EC number |
|
Protein Class |
|
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 Q8HZQ5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8HZQ5-F1 | Predicted | AlphaFoldDB |
No variants for Q8HZQ5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8HZQ5 | |||||
No associated diseases with Q8HZQ5
10 regional properties for Q8HZQ5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 5 - 295 | IPR000299 |
| domain | Ezrin/radixin/moesin, C-terminal | 511 - 586 | IPR011259 |
| domain | FERM, N-terminal | 9 - 68 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 210 - 299 | IPR018980 |
| conserved_site | FERM conserved site | 58 - 88 | IPR019747-1 |
| conserved_site | FERM conserved site | 176 - 205 | IPR019747-2 |
| domain | FERM central domain | 91 - 206 | IPR019748 |
| domain | Band 4.1 domain | 1 - 206 | IPR019749 |
| domain | ERM family, FERM domain C-lobe | 200 - 296 | IPR041789 |
| domain | Ezrin/radixin/moesin, alpha-helical domain | 337 - 456 | IPR046810 |
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. |
| actin filament | A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane. |
| apical plasma membrane | The region of the plasma membrane located at the apical end of the cell. |
| basolateral plasma membrane | The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis. |
| cell cortex | The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins. |
| extrinsic component of membrane | The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
| microvillus | Thin cylindrical membrane-covered projections on the surface of an animal cell containing a core bundle of actin filaments. Present in especially large numbers on the absorptive surface of intestinal cells. |
| microvillus membrane | The portion of the plasma membrane surrounding a microvillus. |
| ruffle membrane | The portion of the plasma membrane surrounding a ruffle. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| cell adhesion molecule binding | Binding to a cell adhesion molecule. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament bundle assembly | The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPKPINVRVT | TMDAELEFAV | QPNTTGKQLF | DQVVKTIGLR | EVWYFGLQYV | DNKGFPTWLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDKKVSAQEV | RKENPVQFKF | RAKFYPEDVS | EELIQDITQK | LFFLQVKEGI | LSDEIYCPPE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TAVLLGSYAV | QAKFGDYSKE | AHKAGYLSSE | RLIPQRVMDQ | HKLSRDQWED | RIQVWHAEHR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GMLKDSAMLE | YLKIAQDLEM | YGINYFEIKN | KKGTDLWLGV | DALGLNIYEK | NDKLTPKIGF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PWSEIRNISF | NDKKFVIKPI | DKKAPDFVFY | APRLRINKRI | LQLCMGNHEL | YMRRRKPDTI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EVQQMKAQAR | EEKHQKQLER | QQLESEKKRR | EAVEQEKEQM | LREKEELMMR | LQDYEQKTKK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AEKELSDQIQ | RALQLEDERK | RAQEESERLE | ADRVAALRAK | EELERQAADQ | IKSQEQLAAE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAEYTAKIAL | LEEARRRKES | EVEEWQHRAR | EAQDDLVKTK | EELHLVMTAP | PPPPPPMYEP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VSYHVQEHLH | EEGAESLGYS | AELSSEGILD | DRHEEKRITE | AEKNERVQRQ | LLTLSNELSQ |
| 550 | 560 | 570 | 580 | ||
| ARDENKRTHN | DIIHNENLRQ | GRDKYKTLRQ | IRQGNTKQRI | DEFEAM |