Msn
entrez
17698
canonical
uniprot
P26041
canonical
ensembl
ENSMUSG00000031207
resolver
ensp
ENSMUSP00000113071
resolver
enst
ENSMUST00000117399
resolver
genesymbol
Msn
resolver
uniprot
B1AX70
resolver
uniprot
Q3UL28
resolver
uniprot
Q8BSN4
resolver
uniprot_entry
MOES_MOUSE
resolver
uniprot_sec
B1AX70
resolver
uniprot_sec
Q3UL28
resolver
uniprot_sec
Q8BSN4
resolver
amino_acid_sequence
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARISQLEMARKKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P26038, ECO:0000269|PubMed:22875842, ECO:0000269|PubMed:28978692}.
uniprot
proteins
mass_dalton
67767
uniprot
proteins
mutagenesis
MUTAGEN 558; /note="T->A: Diminishes the number of microvilli-like structures."; /evidence="ECO:0000269|PubMed:9856983"; MUTAGEN 558; /note="T->D: No effect on microvilli-like structures."; /evidence="ECO:0000269|PubMed:9856983
uniprot
proteins
post_translational_modification
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. {ECO:0000250, ECO:0000269|PubMed:9456324, ECO:0000269|PubMed:9856983}.; 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. {ECO:0000250|UniProtKB:P26038}.
uniprot
proteins
pubmed
11777944
uniprot
proteins
pubmed
1429901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1573844
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22875842
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28978692
uniprot
proteins
pubmed
29247647
uniprot
proteins
pubmed
9456324
uniprot
proteins
pubmed
9472040
uniprot
proteins
pubmed
9856983
uniprot
proteins
pubmed
9890997
uniprot
proteins
sequence_length
577
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9856983}. Apical cell membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cell projection, microvillus membrane {ECO:0000269|PubMed:9856983}; Peripheral membrane protein {ECO:0000269|PubMed:9856983}; Cytoplasmic side {ECO:0000269|PubMed:9856983}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Note=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). {ECO:0000250|UniProtKB:P26038, ECO:0000269|PubMed:9856983}.
uniprot
proteins