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IID00344
 UniprotP26038
ProteinMoesin
GeneMSN
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
577
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-297 Hetero dimer : IID00134Complex
 Evidence X-RAY 1sgh A Reference
       Region 1sgh A 1-3 disorder
       Region 1sgh A 4-297 order
Seq 2-346 Monomer :
 Evidence X-RAY 1e5w A Reference
       Region 1e5w A 2-346 order
Seq 4-297,488-577 Hetero tetramer :
 Evidence X-RAY 1ef1 D This complex is hetero tetramer in the automatic decision, but is actually homo dimer. Reference
       Region 1ef1 D 488-577 order
 Evidence X-RAY 1ef1 C This complex is hetero tetramer in the automatic decision, but is actually homo dimer. Reference
       Region 1ef1 C 488-577 order
 Evidence X-RAY 1ef1 B This complex is hetero tetramer in the automatic decision, but is actually homo dimer. Reference
       Region 1ef1 B 4-297 order
 Evidence X-RAY 1ef1 A This complex is hetero tetramer in the automatic decision, but is actually homo dimer. Reference
       Region 1ef1 A 4-297 order
Seqphosphorylation
    116-116 Phosphotyrosine
    74-74 Phosphoserine
    407-407 Phosphoserine
    527-527 Phosphoserine
    558-558 Phosphothreonine; by ROCK2 and STK10
Seqacetylation
    79-79 N6-acetyllysine
    139-139 N6-acetyllysine
    165-165 N6-acetyllysine
 
Prediction
NeProc
Disorder 470-500,550-577
Order 1-469,501-549
ProS 489-500,550-577
AlphaFold
Disorder 1-2,404-418,452-490,495-501
Order 3-403,419-451,491-494,502-577
Pfam Hmmer
PF00373 7-206 3.5e-137
PF00769 210-577 9.7e-239
SEG 324-352 ,385-406 ,505-517
Function
Function in SwissProt
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 (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). 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:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (PubMed:27405666).