MGP Database

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MGP001966

UniProt Annotations

Entry Information
Gene Namemoesin
Protein EntryMOES_HUMAN
UniProt IDP26038
SpeciesHuman
Comments
Comment typeDescription
Enzyme RegulationA head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. {ECO:0000250}.
FunctionProbably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. {ECO:0000269|PubMed:21549406}.
InteractionP16070:CD44; NbExp=6; IntAct=EBI-528768, EBI-490245; Q5S007:LRRK2; NbExp=15; IntAct=EBI-528768, EBI-5323863; Q5S006:Lrrk2 (xeno); NbExp=2; IntAct=EBI-528768, EBI-2693710; O14745:SLC9A3R1; NbExp=5; IntAct=EBI-528768, EBI-349787;
PtmPhosphorylation 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 (By similarity). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization. {ECO:0000250, ECO:0000269|PubMed:19255442, ECO:0000269|PubMed:19690332}.
SimilarityContains 1 FERM domain. {ECO:0000255|PROSITE- ProRule:PRU00084}.
Subcellular LocationCell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Apical cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment. {ECO:0000250, ECO:0000269|PubMed:18586956}.
SubunitIn resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation (By similarity). Binds SLC9A3R1. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG. {ECO:0000250, ECO:0000269|PubMed:12387735, ECO:0000269|PubMed:15020681, ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:21549406, ECO:0000269|PubMed:9314537}.
Tissue SpecificityIn all tissues and cultured cells studied.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MSNID363.html";
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