UniProt:P26041 Msn

chain
  • chain:1-577
checksum 4E9B5521313EF5B5
comment
  • FUNCTION Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (By similarity). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (By similarity). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (By similarity). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:22875842). Modulates phagolysosomal biogenesis in macrophages (PubMed:28978692). Also participates in immunologic synapse formation (By similarity).SUBUNIT In resting T-cells, part of a PAG1-NHERF1-MSN complex which is disrupted upon TCR activation (PubMed:11777944). Interacts with NHERF1 (PubMed:11777944). Interacts with PPP1R16B (By similarity). Interacts with SELPLG and SYK; these interactions mediate the activation of SYK by SELPLG (By similarity). Interacts with PDPN (via cytoplasmic domain); this interaction activates RHOA and promotes epithelial-mesenchymal transition (By similarity). Interacts with SPN/CD43 cytoplasmic tail (PubMed:9472040). Interacts with CD44 (PubMed:9472040). Interacts with ICAM2 (PubMed:9472040). Interacts with ICAM3 (via C-terminus) (By similarity). Interacts with PDZD8 (By similarity). Interacts with F-actin (By similarity). Interacts with CD46 (By similarity). Interacts with PTPN6 (PubMed:29247647).SUBCELLULAR LOCATION Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts (By similarity).DOMAIN The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.PTM Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization (By similarity). Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding.PTM S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.DISRUPTION PHENOTYPE Moesin-deficient mice exhibit no obvious abnormalities in appearance or fertility, but display altered humoral immune responses.
crossReference
databaseName UniProt
dbId 95438
description
  • recommendedName: fullName evidence="14"Moesin alternativeName: Membrane-organizing extension spike protein
displayName UniProt:P26041 Msn
geneName
  • Msn
identifier P26041
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Cell membrane
  • Cell projection
  • Cytoplasm
  • Cytoskeleton
  • Membrane
  • Phosphoprotein
  • Reference proteome
  • S-nitrosylation
modified [InstanceEdit:9948485] Weiser, Joel, 2025-05-21
moleculeType Protein
name
  • Msn
otherIdentifier
  • 10600836
  • 1421814_at
  • 1450379_at
  • 160308_at
  • 17536364
  • 17698
  • 4484144
  • 4499247
  • 4627938
  • 4649837
  • 4717792
  • 4742760
  • 4893041
  • 4902456
  • 4961974
  • 5007337
  • 5017846
  • 5139071
  • 5161926
  • 5243076
  • 5301357
  • 5342277
  • 5473807
  • 5562409
  • A_51_P115197
  • A_52_P558411
  • A_52_P627177
  • A_55_P2072373
  • A_55_P2722075
  • A_55_P2729368
  • GE42647
  • GO:0001771
  • GO:0001931
  • GO:0002376
  • GO:0003723
  • GO:0003725
  • GO:0003779
  • GO:0005102
  • GO:0005515
  • GO:0005737
  • GO:0005829
  • GO:0005856
  • GO:0005886
  • GO:0005902
  • GO:0005912
  • GO:0005925
  • GO:0007159
  • GO:0007163
  • GO:0008092
  • GO:0008360
  • GO:0008361
  • GO:0009986
  • GO:0010628
  • GO:0016020
  • GO:0016323
  • GO:0016324
  • GO:0019899
  • GO:0019901
  • GO:0022612
  • GO:0022614
  • GO:0030154
  • GO:0030175
  • GO:0031143
  • GO:0031528
  • GO:0042098
  • GO:0042995
  • GO:0043209
  • GO:0045177
  • GO:0045198
  • GO:0045732
  • GO:0048471
  • GO:0048856
  • GO:0048870
  • GO:0050839
  • GO:0050900
  • GO:0061028
  • GO:0070489
  • GO:0071803
  • GO:0071944
  • GO:0072678
  • GO:1902115
  • GO:1902966
  • GO:2000401
  • GO:2000643
  • ILMN_1229193
  • ILMN_1236524
  • ILMN_1256966
  • ILMN_2583410
  • ILMN_2694960
  • Msa.978.0_at
  • c78546_rc_s_at
  • mMC003514
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • MOES_MOUSE
  • B1AX70
  • Q3UL28
  • Q8BSN4
sequenceLength 577
species [Species:48892] Mus musculus
stId uniprot:P26041
url http://purl.uniprot.org/uniprot/P26041
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