Q32LP2
SS
Gene name |
RDX |
Protein name |
Radixin |
Names |
|
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:517111 |
EC number |
|
Protein Class |
|
Descriptions
MSN is a moesin protein and belongs to the ezrin-radixin-moesin (ERM) protein family, directly involved in the cytoskeleton-membrane crosslinking. Functional N-terminal FERM domain of ERM attaches to the membrane by binding specific membrane proteins while the last 34 residues of the C-terminal tail domain bind actin filaments. The autoinhibitory domain is positions at the C-terminal tail domain of ERM, where FERM domain of ERM is bound tightly via phosphotyrosine binding (PTB), pleckstrin homology (PH), and Enabled/VASP Homology 1 (EVH1) domains, thus masking the binding sites for other molecules. ERM is activated through phosphorylation at Thr558 weakening the FERM/tail binding and, unmasks the binding sites of membrane protein and actin filaments in the presence of phospholipids.
Autoinhibitory domains (AIDs)
Target domain |
5-295 (FERM domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Pearson MA et al. (2000) "Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain", Cell, 101, 259-70
- Austermann J et al. (2008) "Characterization of the Ca2+ -regulated ezrin-S100P interaction and its role in tumor cell migration", The Journal of biological chemistry, 283, 29331-40
- Liu J et al. (2014) "Conserved sequence repeats of IQGAP1 mediate binding to Ezrin", Journal of proteome research, 13, 1156-66
Autoinhibited structure
Activated structure
1 structures for Q32LP2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q32LP2-F1 | Predicted | AlphaFoldDB |
39 variants for Q32LP2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs465877433 | 40 | R>C | No | EVA | |
| rs447431182 | 46 | G>V | No | EVA | |
| rs452247408 | 65 | V>G | No | EVA | |
| rs466580409 | 68 | Q>K | No | EVA | |
| rs465357819 | 71 | K>R | No | EVA | |
| rs447980349 | 72 | K>T | No | EVA | |
| rs468831468 | 77 | Q>P | No | EVA | |
| rs450326850 | 78 | F>C | No | EVA | |
| rs450326850 | 78 | F>Y | No | EVA | |
| rs483281906 | 80 | F>I | No | EVA | |
| rs483281906 | 80 | F>V | No | EVA | |
| rs458128432 | 90 | S>A | No | EVA | |
| rs439671916 | 95 | Q>* | No | EVA | |
| rs460422366 | 95 | Q>H | No | EVA | |
| rs478903566 | 95 | Q>P | No | EVA | |
| rs441972248 | 96 | E>D | No | EVA | |
| rs474963495 | 97 | I>L | No | EVA | |
| rs456384818 | 122 | A>P | No | EVA | |
| rs446940751 | 148 | A>V | No | EVA | |
| rs444292114 | 154 | P>H | No | EVA | |
| rs452288085 | 155 | Q>K | No | EVA | |
| rs465820804 | 169 | E>* | No | EVA | |
| rs137647421 | 184 | R>K | No | EVA | |
| rs465403721 | 191 | Y>D | No | EVA | |
| rs437039332 | 235 | T>K | No | EVA | |
| rs461800852 | 312 | E>V | No | EVA | |
| rs444164511 | 326 | E>K | No | EVA | |
| rs452356665 | 344 | K>N | No | EVA | |
| rs432413445 | 355 | E>G | No | EVA | |
| rs457452412 | 355 | E>K | No | EVA | |
| rs463725051 | 366 | E>K | No | EVA | |
| rs450648820 | 413 | N>K | No | EVA | |
| rs477258654 | 414 | Q>K | No | EVA | |
| rs470077509 | 425 | T>A | No | EVA | |
| rs435203103 | 450 | F>L | No | EVA | |
| rs473503624 | 484 | N>K | No | EVA | |
| rs455093504 | 522 | E>K | No | EVA | |
| rs437471174 | 525 | K>R | No | EVA | |
| rs471886525 | 574 | K>M | No | EVA |
No associated diseases with Q32LP2
10 regional properties for Q32LP2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 5 - 295 | IPR000299 |
| domain | Ezrin/radixin/moesin, C-terminal | 508 - 583 | IPR011259 |
| domain | FERM, N-terminal | 9 - 70 | 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 | 90 - 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 |
|---|---|
| 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. |
| cleavage furrow | The cleavage furrow is a plasma membrane invagination at the cell division site. The cleavage furrow begins as a shallow groove and eventually deepens to divide the cytoplasm. |
| 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. |
| stereocilium base | The tapered base of the stereocilium adjacent to where it joins the hair cell body. This region contains a rootlet comprised of bundled actin filaments which spans the joint and stabilizes the stereocilium. |
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. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament capping | The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits. |
| 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. |
21 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P31976 | EZR | Ezrin | Bos taurus (Bovine) | PR |
| Q2HJ49 | MSN | Moesin | Bos taurus (Bovine) | PR |
| Q9PU45 | RDX | Radixin | Gallus gallus (Chicken) | PR |
| Q24564 | Mer | Moesin/ezrin/radixin homolog 2 | Drosophila melanogaster (Fruit fly) | SS |
| P46150 | Moe | Moesin/ezrin/radixin homolog 1 | Drosophila melanogaster (Fruit fly) | SS |
| Q3KP66 | INAVA | Innate immunity activator protein | Homo sapiens (Human) | PR |
| P15311 | EZR | Ezrin | Homo sapiens (Human) | EV |
| P35240 | NF2 | Merlin | Homo sapiens (Human) | EV |
| P26038 | MSN | Moesin | Homo sapiens (Human) | EV |
| P35241 | RDX | Radixin | Homo sapiens (Human) | SS |
| A2AD83 | Frmd7 | FERM domain-containing protein 7 | Mus musculus (Mouse) | PR |
| P46662 | Nf2 | Merlin | Mus musculus (Mouse) | SS |
| P26040 | Ezr | Ezrin | Mus musculus (Mouse) | SS |
| P26041 | Msn | Moesin | Mus musculus (Mouse) | SS |
| P26043 | Rdx | Radixin | Mus musculus (Mouse) | SS |
| P26042 | MSN | Moesin | Sus scrofa (Pig) | PR |
| P26044 | RDX | Radixin | Sus scrofa (Pig) | SS |
| Q63648 | Nf2 | Merlin | Rattus norvegicus (Rat) | SS |
| O35763 | Msn | Moesin | Rattus norvegicus (Rat) | SS |
| P31977 | Ezr | Ezrin | Rattus norvegicus (Rat) | SS |
| Q6Q413 | nf2b | NF2, moesin-ezrin-radixin-like | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPKPINVRVT | TMDAELEFAI | QPNTTGKQLF | DQVVKTVGLR | EVWFFGLQYV | DSKGYSTWLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LNKKVTQQDV | KKENPLQFKF | RAKFFPEDVS | EELIQEITQR | LFFLQVKEAI | LNDEIYCPPE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TAVLLASYAV | QAKYGDYNKE | IHKPGYLAND | RLLPQRVLEQ | HKLTKEQWEE | RIQNWHEEHR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GMLREDSMME | YLKIAQDLEM | YGVNYFEIKN | KKGTELWLGV | DALGLNIYEH | DDKLTPKIGF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PWSEIRNISF | NDKKFVIKPI | DKKAPDFVFY | APRLRINKRI | LALCMGNHEL | YMRRRKPDTI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EVQQMKAQAR | EEKHQKQLER | AQLENEKKKR | EIAEKEKERI | EREKEELMER | LRQIEEQTMK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AQKELEEQTR | KALELDQERK | RAKEEAERLE | KERQAAEEAK | SALAKQAADQ | MKNQEQLAAE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAEFTAKIAL | LEEAKKKKEE | EATEWQHKAF | AAQEDLEKTK | EELKTVMSAP | PPPPPPPVIP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PTENEHDEHD | ENNAEASAEL | SNDGVMNHRS | EEERVTETQK | NERVKKQLQA | LSSELAQARD |
| 550 | 560 | 570 | 580 | ||
| ETKKTQNDVL | HAENVKAGRD | KYKTLRQIRQ | GNTKQRIDEF | EAM |