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 P31976

Entry ID Method Resolution Chain Position Source
AF-P31976-F1 Predicted AlphaFoldDB

202 variants for P31976

Variant ID(s) Position Change Description Diseaes Association Provenance
rs454889138 3 K>E No EVA
rs442968750 4 P>R No EVA
rs526880533 6 N>H No EVA
rs459308463 7 V>A No EVA
rs477779712 7 V>L No EVA
rs473858781 9 V>G No EVA
rs461968275 10 T>P No EVA
rs443388565 11 T>P No EVA
rs476361909 12 M>L No EVA
rs451475350 12 M>R No EVA
rs472424564 13 D>E No EVA
rs433182388 13 D>G No EVA
rs453996301 14 A>G No EVA
rs435694123 15 E>G No EVA
rs468637647 16 L>R No EVA
rs450308350 17 E>G No EVA
rs438183456 21 Q>H No EVA
rs456687559 65 V>G No EVA
rs438356735 66 S>A No EVA
rs444855692 69 E>A No EVA
rs477843459 70 V>D No EVA
rs477843459 70 V>G No EVA
rs465743799 76 L>P No EVA
rs447316525 78 F>L No EVA
rs447316525 78 F>V No EVA
rs136241981 121 T>P No EVA
rs443376857 122 A>G No EVA
rs461789939 122 A>T No EVA
rs439449531 123 V>A No EVA
rs457947604 123 V>L No EVA
rs472599074 125 L>M No EVA
rs454051221 126 G>R No EVA
rs442100784 127 S>Y No EVA
rs475091351 128 Y>D No EVA
rs456773635 134 F>V No EVA
rs438185292 137 Y>* No EVA
rs471328799 142 H>P No EVA
rs452741268 143 K>N No EVA
rs434246467 146 Y>S No EVA
rs447197996 150 E>K No EVA
rs435299639 154 P>L No EVA
rs468105357 155 Q>R No EVA
rs433644116 180 R>S No EVA
rs436318335 181 G>A No EVA
rs454684279 181 G>W No EVA
rs524682677 229 E>G No EVA
rs438659284 235 T>P No EVA
rs434879013 254 K>N No EVA
rs432873579 266 D>V No EVA
rs451182660 266 D>Y No EVA
rs876277991 268 V>G No EVA
rs465695505 270 Y>D No EVA
rs453818524 270 Y>S No EVA
rs435382226 271 A>P No EVA
rs468295294 272 P>S No EVA
rs449987011 277 N>I No EVA
rs449987011 277 N>T No EVA
rs464590178 280 I>S No EVA
rs464590178 280 I>T No EVA
rs446060451 281 L>R No EVA
rs876110423 282 Q>H No EVA
rs876217302 282 Q>R No EVA
rs876033788 283 L>H No EVA
rs876033788 283 L>R No EVA
rs876485854 283 L>V No EVA
rs479148440 286 G>V No EVA
rs460647560 287 N>Y No EVA
rs448439222 291 Y>F No EVA
rs448439222 291 Y>S No EVA
rs481689890 292 M>L No EVA
rs463078906 295 R>Q No EVA
rs444762204 300 I>M No EVA
rs471086532 302 V>G No EVA
rs457623409 307 A>S No EVA
rs435247786 318 L>R No EVA
rs456248810 319 E>Q No EVA
rs479900921 320 R>S No EVA
rs460202168 332 T>N No EVA
rs481013918 349 L>F No EVA
rs462629996 351 L>I No EVA
rs470798220 355 E>G No EVA
rs452310860 358 T>P No EVA
rs440361620 362 E>G No EVA
rs437477209 412 K>Q No EVA
rs462085649 418 A>P No EVA
rs443774517 421 L>P No EVA
rs483093413 423 E>D No EVA
rs439821217 430 L>R No EVA
rs472741763 447 L>V No EVA
rs442260073 448 R>P No EVA
rs456310655 451 E>Q No EVA
rs470875884 454 D>E No EVA
rs444396455 454 D>Y No EVA
rs452342130 455 D>A No EVA
rs433979339 456 L>R No EVA
rs466963524 458 K>Q No EVA
rs454959317 459 T>P No EVA
rs469433816 460 R>G No EVA
rs465507483 461 E>G No EVA
rs477546295 461 E>K No EVA
rs447091461 462 E>* No EVA
rs460138560 462 E>D No EVA
rs478668695 462 E>G No EVA
rs447091461 462 E>Q No EVA
rs481110413 463 L>R No EVA
rs441722394 463 L>V No EVA
rs444257738 464 H>D No EVA
rs470738589 464 H>L No EVA
rs470738589 464 H>P No EVA
rs473421498 465 L>R No EVA
rs440256956 465 L>V No EVA
rs454894634 466 V>A No EVA
rs454894634 466 V>G No EVA
rs457232779 467 M>I No EVA
rs475697246 467 M>L No EVA
rs475697246 467 M>V No EVA
rs432553566 468 T>A No EVA
rs432553566 468 T>P No EVA
rs465545411 469 A>P No EVA
rs435054898 470 P>A No EVA
rs480977277 472 P>T No EVA
rs450592190 473 P>Q No EVA
rs450592190 473 P>R No EVA
rs458731887 474 P>R No EVA
rs473324468 475 V>G No EVA
rs440321324 475 V>L No EVA
rs457294276 476 Y>* No EVA
rs475560158 476 Y>C No EVA
rs442788389 476 Y>D No EVA
rs475560158 476 Y>F No EVA
rs442788389 476 Y>H No EVA
rs475560158 476 Y>S No EVA
rs432414925 477 E>Q No EVA
rs472004429 478 P>A No EVA
rs453477338 479 V>G No EVA
rs468102614 481 Y>F No EVA
rs449560656 482 H>P No EVA
rs435999604 487 P>Q No EVA
rs450655236 491 G>D No EVA
rs468938324 491 G>R No EVA
rs477075599 495 S>G No EVA
rs458725918 495 S>N No EVA
rs458725918 495 S>T No EVA
rs446624384 497 E>G No EVA
rs461253656 498 L>P No EVA
rs479613704 498 L>V No EVA
rs482038976 499 S>A No EVA
rs463564786 500 S>R No EVA
rs471905285 501 E>G No EVA
rs438909078 501 E>Q No EVA
rs453296760 502 G>D No EVA
rs453296760 502 G>V No EVA
rs474383051 503 I>S No EVA
rs456046993 508 N>T No EVA
rs468997577 513 I>M No EVA
rs437478177 513 I>S No EVA
rs456922746 514 T>P No EVA
rs456922746 514 T>S No EVA
rs432102381 515 E>D No EVA
rs465073485 516 A>P No EVA
rs446458256 519 N>T No EVA
rs474458830 528 T>N No EVA
rs443989821 533 L>M No EVA
rs476887626 533 L>Q No EVA
rs451980401 536 A>D No EVA
rs451980401 536 A>G No EVA
rs431959078 538 D>H No EVA
rs452999394 539 E>A No EVA
rs434463641 539 E>D No EVA
rs464896167 539 E>K No EVA
rs467450118 541 K>R No EVA
rs448987599 542 R>P No EVA
rs436919977 543 T>A No EVA
rs469913493 545 N>K No EVA
rs445065265 547 I>T No EVA
rs459674806 548 I>M No EVA
rs478268602 548 I>N No EVA
rs447786895 554 R>S No EVA
rs480770930 555 Q>K No EVA
rs462382529 556 G>V No EVA
rs443849064 558 D>A No EVA
rs443849064 558 D>V No EVA
rs458450683 560 Y>* No EVA
rs476750736 560 Y>D No EVA
rs439856609 561 K>E No EVA
rs452807632 562 T>P No EVA
rs455226591 565 Q>K No EVA
rs436981683 565 Q>P No EVA
rs469776461 566 I>S No EVA
rs480571436 568 Q>H No EVA
rs447577339 568 Q>K No EVA
rs462243409 570 N>I No EVA
rs450181273 573 Q>R No EVA
rs458258041 574 R>P No EVA
rs483221173 574 R>S No EVA
rs439910139 576 D>H No EVA
rs460814389 578 F>V No EVA
rs440797519 579 E>K No EVA
rs440797519 579 E>Q No EVA
rs473574399 581 M>R No EVA
rs455291996 582 M>R No EVA
rs436846576 582 M>S No EVA

No associated diseases with P31976

1 regional properties for P31976

Type Name Position InterPro Accession
domain Small GTP-binding protein domain 16 - 171 IPR005225

Functions

Description
EC Number
Subcellular Localization
  • Apical cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell projection
  • Cell projection, microvillus membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasm, cell cortex
  • Cytoplasm, cytoskeleton
  • Cell projection, microvillus
  • Localization to the apical membrane of parietal cells depends on the interaction with PALS1
  • Microvillar peripheral membrane protein (cytoplasmic side)
  • Localizes to cell extensions and peripheral processes of astrocytes (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

15 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.
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 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.
ciliary basal body A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
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.
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.
microvillus membrane The portion of the plasma membrane surrounding a microvillus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.
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.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
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.

6 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.
establishment or maintenance of apical/basal cell polarity Any cellular process that results in the specification, formation or maintenance polarization of a cell's architecture along its apical/basal axis so that the apical and basal regions of the cell have different membrane, extracellular matrix and sub-membrane cellular components.
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
Q2HJ49 MSN Moesin 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
P35240 NF2 Merlin Homo sapiens (Human) EV
P35241 RDX Radixin Homo sapiens (Human) SS
P15311 EZR Ezrin Homo sapiens (Human) EV
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
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 DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
70 80 90 100 110 120
LDKKVSAQEV RKESPLQFKF RAKFYPEDVA EELIQDITQK LFFLQVKEGI LSDEIYCPPE
130 140 150 160 170 180
TAVLLGSYAV QAKFGDYNKE LHKAGYLGSE RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR
190 200 210 220 230 240
GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
250 260 270 280 290 300
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
310 320 330 340 350 360
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR LQDYEEKTRK
370 380 390 400 410 420
AEKELSDQIQ RALKLEEERK RAQEEAGRLE ADRLAALRAK EELERQAADQ IKSQEQLATE
430 440 450 460 470 480
LAEYTAKIAL LEEARRRKEN EVEEWQLRAK EAQDDLVKTR EELHLVMTAP PPPPVYEPVN
490 500 510 520 530 540
YHVHEGPQEE GTELSAELSS EGILDDRNEE KRITEAEKNE RVQRQLMTLT SELSQARDEN
550 560 570 580
KRTHNDIIHN ENMRQGRDKY KTLRQIRQGN TKQRIDEFEA M