Q2HJ49
Gene name |
MSN |
Protein name |
Moesin |
Names |
Membrane-organizing extension spike protein |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:540426 |
EC number |
|
Protein Class |
|

Descriptions
(Annotation based on sequence homology with P26038)
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 |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for Q2HJ49
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q2HJ49-F1 | Predicted | AlphaFoldDB |
96 variants for Q2HJ49
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs455610087 | 4 | T>R | No | EVA | |
rs444779670 | 33 | V>G | No | EVA | |
rs479349030 | 35 | K>Q | No | EVA | |
rs459464625 | 43 | W>C | No | EVA | |
rs474429777 | 56 | F>V | No | EVA | |
rs434728106 | 66 | T>P | No | EVA | |
rs455356557 | 67 | A>P | No | EVA | |
rs435190689 | 68 | Q>R | No | EVA | |
rs449804238 | 94 | I>S | No | EVA | |
rs477855485 | 98 | T>S | No | EVA | |
rs464800728 | 106 | V>A | No | EVA | |
rs447883372 | 122 | A>D | No | EVA | |
rs462439817 | 133 | K>N | No | EVA | |
rs442280090 | 136 | D>E | No | EVA | |
rs483097534 | 140 | E>V | No | EVA | |
rs462745131 | 141 | V>L | No | EVA | |
rs470907706 | 143 | K>T | No | EVA | |
rs451428043 | 152 | L>V | No | EVA | |
rs469378247 | 157 | V>G | No | EVA | |
rs474266319 | 185 | E>G | No | EVA | |
rs437323078 | 194 | I>L | No | EVA | |
rs445325977 | 200 | M>I | No | EVA | |
rs466677517 | 201 | Y>F | No | EVA | |
rs432180996 | 201 | Y>N | No | EVA | |
rs446741554 | 204 | N>T | No | EVA | |
rs481363848 | 213 | G>R | No | EVA | |
rs460825359 | 218 | L>M | No | EVA | |
rs450374369 | 220 | V>G | No | EVA | |
rs481758952 | 222 | A>V | No | EVA | |
rs458490287 | 223 | L>Q | No | EVA | |
rs438455763 | 224 | G>D | No | EVA | |
rs473638979 | 228 | Y>S | No | EVA | |
rs469861418 | 271 | A>D | No | EVA | |
rs449771337 | 276 | I>V | No | EVA | |
rs433380915 | 278 | K>Q | No | EVA | |
rs464719636 | 286 | G>R | No | EVA | |
rs447896528 | 292 | M>R | No | EVA | |
rs462148707 | 294 | R>S | No | EVA | |
rs448376195 | 295 | R>S | No | EVA | |
rs482789814 | 303 | Q>H | No | EVA | |
rs462908115 | 304 | Q>P | No | EVA | |
rs439614528 | 305 | M>V | No | EVA | |
rs471580453 | 312 | E>A | No | EVA | |
rs457931303 | 317 | Q>H | No | EVA | |
rs462580683 | 361 | A>G | No | EVA | |
rs482912757 | 361 | A>T | No | EVA | |
rs438284642 | 384 | S>R | No | EVA | |
rs475899874 | 385 | E>* | No | EVA | |
rs452692120 | 386 | A>D | No | EVA | |
rs432381490 | 389 | L>V | No | EVA | |
rs466884315 | 390 | A>S | No | EVA | |
rs446950381 | 391 | K>E | No | EVA | |
rs436471515 | 392 | E>D | No | EVA | |
rs468418748 | 395 | E>G | No | EVA | |
rs482780003 | 403 | L>F | No | EVA | |
rs462878243 | 407 | S>P | No | EVA | |
rs445846170 | 408 | Q>* | No | EVA | |
rs445846170 | 408 | Q>K | No | EVA | |
rs477047843 | 409 | D>A | No | EVA | |
rs474288579 | 414 | Q>R | No | EVA | |
rs440134163 | 416 | Q>H | No | EVA | |
rs474484891 | 417 | L>Q | No | EVA | |
rs480080152 | 422 | A>S | No | EVA | |
rs797289810 | 433 | M>T | No | EVA | |
rs459924602 | 440 | S>R | No | EVA | |
rs443189727 | 442 | A>G | No | EVA | |
rs480891349 | 443 | V>A | No | EVA | |
rs480891349 | 443 | V>G | No | EVA | |
rs463785234 | 444 | E>G | No | EVA | |
rs443610768 | 447 | Q>E | No | EVA | |
rs458044072 | 450 | Q>R | No | EVA | |
rs441100771 | 462 | E>Q | No | EVA | |
rs472229932 | 464 | K>N | No | EVA | |
rs455327244 | 468 | S>R | No | EVA | |
rs456134145 | 473 | A>T | No | EVA | |
rs433392641 | 476 | A>D | No | EVA | |
rs464679137 | 477 | E>A | No | EVA | |
rs454316739 | 479 | E>* | No | EVA | |
rs468434857 | 490 | A>G | No | EVA | |
rs448376190 | 500 | A>S | No | EVA | |
rs469521402 | 502 | D>E | No | EVA | |
rs446049118 | 509 | T>P | No | EVA | |
rs446049118 | 509 | T>S | No | EVA | |
rs478054460 | 520 | K>* | No | EVA | |
rs457859243 | 523 | K>N | No | EVA | |
rs481460570 | 528 | E>A | No | EVA | |
rs461375145 | 528 | E>D | No | EVA | |
rs444758045 | 529 | L>V | No | EVA | |
rs476091637 | 535 | E>Q | No | EVA | |
rs452743873 | 538 | K>R | No | EVA | |
rs438807552 | 548 | N>K | No | EVA | |
rs453440035 | 558 | T>P | No | EVA | |
rs469531367 | 564 | Q>* | No | EVA | |
rs468398268 | 575 | E>* | No | EVA | |
rs454627668 | 575 | E>D | No | EVA | |
rs437757729 | 576 | S>A | No | EVA |
No associated diseases with Q2HJ49
No regional properties for Q2HJ49
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for Q2HJ49 |
Functions
14 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. |
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 surface | The external part of the cell wall and/or plasma membrane. |
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. |
focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
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. |
perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
pseudopodium | A temporary protrusion or retractile process of a cell, associated with flowing movements of the protoplasm, and serving for locomotion and feeding. |
uropod | A membrane projection with related cytoskeletal components at the trailing edge of a cell in the process of migrating or being activated, found on the opposite side of the cell from the leading edge or immunological synapse, respectively. |
5 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. |
double-stranded RNA binding | Binding to double-stranded RNA. |
protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
signaling receptor binding | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
18 GO annotations of biological process
Name | Definition |
---|---|
cellular response to testosterone stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a testosterone stimulus. |
establishment of endothelial barrier | The establishment of a barrier between endothelial cell layers, such as those in the brain, lung or intestine, to exert specific and selective control over the passage of water and solutes, thus allowing formation and maintenance of compartments that differ in fluid and solute composition. |
establishment of epithelial cell apical/basal polarity | The specification and formation of the apicobasal polarity of an epithelial cell. |
gland morphogenesis | The process in which the anatomical structures of a gland are generated and organized. |
immunological synapse formation | The formation of an area of close contact between a lymphocyte (T-, B-, or natural killer cell) and a target cell through the clustering of particular signaling and adhesion molecules and their associated membrane rafts on both the lymphocyte and target cell, which facilitates activation of the lymphocyte, transfer of membrane from the target cell to the lymphocyte, and in some situations killing of the target cell through release of secretory granules and/or death-pathway ligand-receptor interaction. |
membrane to membrane docking | The initial attachment of a membrane to a target membrane, mediated by proteins protruding from the two membranes. Docking requires only that the membranes come close enough for the proteins to interact and adhere. |
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 gene expression | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
positive regulation of podosome assembly | Any process that activates or increases the rate or extent of podosome assembly. |
positive regulation of protein catabolic process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
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 cell size | Any process that modulates the size of a cell. |
regulation of lymphocyte migration | Any process that modulates the frequency, rate or extent of lymphocyte migration. |
regulation of organelle assembly | Any process that modulates the frequency, rate or extent of organelle assembly. |
T cell aggregation | The adhesion of one T cell to one or more other T cells via adhesion molecules. |
T cell migration | The movement of a T cell within or between different tissues and organs of the body. |
T cell proliferation | The expansion of a T cell population by cell division. Follows T cell activation. |
21 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P31976 | EZR | Ezrin | Bos taurus (Bovine) | PR |
Q32LP2 | RDX | Radixin | Bos taurus (Bovine) | SS |
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 |
P35241 | RDX | Radixin | Homo sapiens (Human) | SS |
P26038 | MSN | Moesin | Homo sapiens (Human) | EV |
A2AD83 | Frmd7 | FERM domain-containing protein 7 | Mus musculus (Mouse) | PR |
P26043 | Rdx | Radixin | Mus musculus (Mouse) | SS |
P46662 | Nf2 | Merlin | Mus musculus (Mouse) | SS |
P26040 | Ezr | Ezrin | Mus musculus (Mouse) | SS |
P26041 | Msn | Moesin | Mus musculus (Mouse) | SS |
P26044 | RDX | Radixin | Sus scrofa (Pig) | SS |
P26042 | MSN | Moesin | Sus scrofa (Pig) | PR |
Q63648 | Nf2 | Merlin | Rattus norvegicus (Rat) | SS |
P31977 | Ezr | Ezrin | Rattus norvegicus (Rat) | SS |
O35763 | Msn | Moesin | Rattus norvegicus (Rat) | SS |
Q6Q413 | nf2b | NF2, moesin-ezrin-radixin-like | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MPKTINVRVT | TMDAELEFAI | QPNTTGKQLF | DQVVKTIGLR | EIWFFGLQYQ | DTKGFFTWLK |
70 | 80 | 90 | 100 | 110 | 120 |
LNKKVTAQDV | RKESPLLFKF | RAKFYPEDVS | EELIQDITQR | LFFLQVKEDI | LNDDIYCPPE |
130 | 140 | 150 | 160 | 170 | 180 |
TAVLLASYAV | QSKYGDFNKE | VHKSGYLAGD | RLLPQRVLEQ | HKLNKDQWEE | RIQVWHEEHR |
190 | 200 | 210 | 220 | 230 | 240 |
GMLREDAVLE | YLKIAQDLEM | YGVNYFSIKN | KKGSELWLGV | DALGLNIYEQ | NDRLTPKIGF |
250 | 260 | 270 | 280 | 290 | 300 |
PWSEIRNISF | NDKKFVIKPI | DKKAPDFVFY | APRLRINKRI | LALCMGNHEL | YMRRRKPDTI |
310 | 320 | 330 | 340 | 350 | 360 |
EVQQMKAQAR | EEKHQKQMER | ALLENEKKKR | EMAEKEKEKI | EREKEELMER | LKQIEEQTKK |
370 | 380 | 390 | 400 | 410 | 420 |
AQQELEEQTR | RALELEQERK | RAQSEAEKLA | KERQEAEEAK | EALLQASQDQ | KKTQEQLALE |
430 | 440 | 450 | 460 | 470 | 480 |
MAELTARISQ | LEMARQKKES | EAVEWQQKAQ | MVQEDLEKTR | AELKTAMSTP | HVAEPAENEQ |
490 | 500 | 510 | 520 | 530 | 540 |
DEQDENGAEA | SAELRADAMA | KDRSEEERTT | EAEKNERVQK | HLKALTSELA | NARDESKKTA |
550 | 560 | 570 | |||
NDMIHAENMR | LGRDKYKTLR | QIRQGNTKQR | IDEFESM |