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P26041 (MOES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Moesin
Alternative name(s):
Membrane-organizing extension spike protein
Gene names
Name:Msn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in connections of major cytoskeletal structures to the plasma membrane.

Enzyme regulation

A 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. Ref.7

Subunit structure

Binds SLC9A3R1 By similarity. In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with PPP1R16B By similarity. Interacts with PDZD8 By similarity. Interacts with SELPLG and SYK; mediates the activation of SYK by SELPLG By similarity. Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionmicrovillus membrane; Peripheral membrane protein; Cytoplasmic side. 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. Ref.6

Post-translational modification

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.

Sequence similarities

Contains 1 FERM domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processleukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Inferred from electronic annotation. Source: Ensembl

membrane to membrane docking

Inferred from electronic annotation. Source: Ensembl

regulation of lymphocyte migration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 9890997. Source: MGI

apical plasma membrane

Inferred from direct assay PubMed 14625387. Source: MGI

basolateral plasma membrane

Inferred from direct assay PubMed 14625387. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

extrinsic component of membrane

Inferred from electronic annotation. Source: InterPro

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

uropod

Inferred from direct assay PubMed 11728336. Source: MGI

   Molecular_functiondouble-stranded RNA binding

Inferred from sequence orthology PubMed 21266579. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 577576Moesin
PRO_0000219417

Regions

Domain2 – 295294FERM

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue1161Phosphotyrosine Ref.9
Modified residue1391N6-acetyllysine By similarity
Modified residue1651N6-acetyllysine Ref.10
Modified residue5581Phosphothreonine; by ROCK2 and STK10 Ref.6 Ref.7

Experimental info

Mutagenesis5581T → A: Diminishes the number of microvilli-like structures. Ref.6
Mutagenesis5581T → D: No effect on microvilli-like structures. Ref.6
Sequence conflict331 – 3322EL → DV in AAA39728. Ref.5
Sequence conflict371 – 3722RA → SP in AAA39728. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P26041 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4E9B5521313EF5B5

FASTA57767,767
        10         20         30         40         50         60 
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK 

        70         80         90        100        110        120 
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE 

       130        140        150        160        170        180 
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR 

       190        200        210        220        230        240 
GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF 

       250        260        270        280        290        300 
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 

       310        320        330        340        350        360 
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK 

       370        380        390        400        410        420 
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE 

       430        440        450        460        470        480 
MAELTARISQ LEMARKKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH 

       490        500        510        520        530        540 
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA 

       550        560        570 
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM 

« Hide

References

« Hide 'large scale' references
[1]"A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites."
Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S.
J. Cell Sci. 103:131-143(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Forelimb and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions."
Furthmayr H., Lankes W.T., Amieva M.R.
Kidney Int. 41:665-670(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-577.
[6]"Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures."
Oshiro N., Fukata Y., Kaibuchi K.
J. Biol. Chem. 273:34663-34666(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-558, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-558.
[7]"Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association."
Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S.
J. Cell Biol. 140:647-657(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-558, ENZYME REGULATION.
[8]"Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly."
Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H., Miyazaki M., Nakajima N., Okada M., Saito T.
J. Immunol. 168:541-544(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SLC9A3R1 AND PAG1.
[9]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S47577 mRNA. Translation: AAA11762.1.
AK031171 mRNA. Translation: BAC27288.1.
AK088336 mRNA. Translation: BAC40290.1.
AK133819 mRNA. Translation: BAE21861.1.
AK145746 mRNA. Translation: BAE26623.1.
AK150869 mRNA. Translation: BAE29920.1.
AK153210 mRNA. Translation: BAE31809.1.
AL805963 Genomic DNA. Translation: CAM27501.1.
BC047366 mRNA. Translation: AAH47366.1.
M86390 mRNA. Translation: AAA39728.1.
CCDSCCDS53139.1.
RefSeqNP_034963.2. NM_010833.2.
UniGeneMm.138876.

3D structure databases

ProteinModelPortalP26041.
SMRP26041. Positions 3-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201534. 2 interactions.
IntActP26041. 5 interactions.
MINTMINT-4996580.

PTM databases

PhosphoSiteP26041.

Proteomic databases

MaxQBP26041.
PaxDbP26041.
PRIDEP26041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
GeneID17698.
KEGGmmu:17698.
UCSCuc009tug.1. mouse.

Organism-specific databases

CTD4478.
MGIMGI:97167. Msn.

Phylogenomic databases

eggNOGNOG236035.
GeneTreeENSGT00650000092953.
HOGENOMHOG000007113.
HOVERGENHBG002185.
InParanoidB1AX70.
KOK05763.
OMAPHVTEPM.
OrthoDBEOG7BGHK6.
PhylomeDBP26041.
TreeFamTF313935.

Gene expression databases

ArrayExpressP26041.
BgeeP26041.
CleanExMM_MSN.
GenevestigatorP26041.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin_like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFPIRSF002305. ERM. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSN. mouse.
NextBio292286.
PROP26041.
SOURCESearch...

Entry information

Entry nameMOES_MOUSE
AccessionPrimary (citable) accession number: P26041
Secondary accession number(s): B1AX70, Q3UL28, Q8BSN4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot