Q7PS12
PR
Gene name |
Moe |
Protein name |
Moesin/ezrin/radixin homolog 1 |
Names |
|
Species |
Anopheles gambiae (African malaria mosquito) |
KEGG Pathway |
aga:AgaP_AGAP000562 |
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 Q7PS12
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7PS12-F1 | Predicted | AlphaFoldDB |
No variants for Q7PS12
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7PS12 | |||||
No associated diseases with Q7PS12
10 regional properties for Q7PS12
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 8 - 298 | IPR000299 |
| domain | Ezrin/radixin/moesin, C-terminal | 506 - 581 | IPR011259 |
| domain | FERM, N-terminal | 12 - 73 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 213 - 302 | IPR018980 |
| conserved_site | FERM conserved site | 61 - 91 | IPR019747-1 |
| conserved_site | FERM conserved site | 179 - 208 | IPR019747-2 |
| domain | FERM central domain | 95 - 209 | IPR019748 |
| domain | Band 4.1 domain | 4 - 209 | IPR019749 |
| domain | ERM family, FERM domain C-lobe | 203 - 299 | IPR041789 |
| domain | Ezrin/radixin/moesin, alpha-helical domain | 333 - 452 | IPR046810 |
Functions
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| apical part of cell | The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| filopodium | Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| cell adhesion molecule binding | Binding to a cell adhesion molecule. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| animal organ morphogenesis | Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions. |
| establishment or maintenance of epithelial cell apical/basal polarity | Any cellular process that results in the specification, formation or maintenance of the apicobasal polarity of an epithelial cell. |
| neuron differentiation | The process in which a relatively unspecialized cell acquires specialized features of a neuron. |
| positive regulation of early endosome to late endosome transport | Any process that activates or increases the frequency, rate or extent of early endosome to late endosome transport. |
| positive regulation of protein localization to early endosome | Any process that activates or increases the frequency, rate or extent of protein localization to early endosome. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
| regulation of organelle assembly | Any process that modulates the frequency, rate or extent of organelle assembly. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVASSKMMNV | RVTTMDAELE | FAIQQGTTGK | QLFDQVVKTI | GLREVWFFGL | QYTDSKGDNT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WIKLYKKVMS | QDVQKGDPLL | FKFRAKFYPE | DVAEELIQDI | TLRLFYLQVK | NAILSDEIYC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PPETSVLLAS | YAVQARHGDY | NKGTHVPGFL | AKDRLLPQRV | IDQHKMSKDE | WENSITTWWQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EHRGLLREDA | MMEYLKIAQD | LEMYGVNYFE | IRNKKGTELW | LGVDALGLNI | YEKEDRLTPK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IGFPWSEIRN | ISFNDRKFII | KPIDKKAPDF | VFFAPRVRIN | KRILALCMGN | HELYMRRRKP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DTIDVQQMKA | QARDEKNAKQ | QEREKLQLAL | AARERAEKKQ | QEYEDRLRSM | QEEMERKQAN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSEAQDTIRR | LQEQLNQVQA | AKEELEQRQN | ELHEMMQRLE | ETKNMEATER | AKLEEEIRVK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLEMQKIQEE | VTLKDSETKR | LHEEVEEAIR | KQVAKGSRAA | AALQAATTTP | KHHHVEEEEE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NEEELINGEN | GTQDFSKDFD | TDEHIKDPVE | ERRTLAERNE | RLQDQLKALK | QDLALSRDDT |
| 550 | 560 | 570 | 580 | ||
| METPNDKIHR | ENVRQGRDKY | KTLREIRKGN | TKRRVDQFEN | M |