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P26041

- MOES_MOUSE

UniProt

P26041 - MOES_MOUSE

Protein

Moesin

Gene

Msn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Enzyme regulationi

    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.1 Publication

    GO - Molecular functioni

    1. double-stranded RNA binding Source: MGI

    GO - Biological processi

    1. leukocyte cell-cell adhesion Source: Ensembl
    2. leukocyte migration Source: Ensembl
    3. membrane to membrane docking Source: Ensembl
    4. regulation of lymphocyte migration Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Moesin
    Alternative name(s):
    Membrane-organizing extension spike protein
    Gene namesi
    Name:Msn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:97167. Msn.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication. Apical cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionmicrovillus membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    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.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. apical plasma membrane Source: MGI
    3. basolateral plasma membrane Source: MGI
    4. cytoplasm Source: UniProtKB-KW
    5. cytoskeleton Source: UniProtKB-SubCell
    6. extracellular vesicular exosome Source: Ensembl
    7. extrinsic component of membrane Source: InterPro
    8. filopodium Source: Ensembl
    9. focal adhesion Source: Ensembl
    10. microvillus membrane Source: UniProtKB-SubCell
    11. nucleolus Source: Ensembl
    12. uropod Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi558 – 5581T → A: Diminishes the number of microvilli-like structures. 1 Publication
    Mutagenesisi558 – 5581T → D: No effect on microvilli-like structures. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 577576MoesinPRO_0000219417Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysineBy similarity
    Modified residuei116 – 1161Phosphotyrosine1 Publication
    Modified residuei139 – 1391N6-acetyllysineBy similarity
    Modified residuei165 – 1651N6-acetyllysine1 Publication
    Modified residuei558 – 5581Phosphothreonine; by ROCK2 and STK102 Publications

    Post-translational modificationi

    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.By similarity3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26041.
    PaxDbiP26041.
    PRIDEiP26041.

    PTM databases

    PhosphoSiteiP26041.

    Expressioni

    Gene expression databases

    ArrayExpressiP26041.
    BgeeiP26041.
    CleanExiMM_MSN.
    GenevestigatoriP26041.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi201534. 2 interactions.
    IntActiP26041. 5 interactions.
    MINTiMINT-4996580.

    Structurei

    3D structure databases

    ProteinModelPortaliP26041.
    SMRiP26041. Positions 3-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 295294FERMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236035.
    GeneTreeiENSGT00650000092953.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    InParanoidiB1AX70.
    KOiK05763.
    OMAiPHVTEPM.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP26041.
    TreeFamiTF313935.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. 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]
    PfamiPF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002305. ERM. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26041-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ    50
    DTKAFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR 100
    LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD 150
    KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM 200
    YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF 250
    NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 300
    EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK 350
    LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK 400
    EALLQASRDQ KKTQEQLASE MAELTARISQ LEMARKKKES EAVEWQQKAQ 450
    MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA 500
    KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR 550
    LGRDKYKTLR QIRQGNTKQR IDEFESM 577
    Length:577
    Mass (Da):67,767
    Last modified:January 23, 2007 - v3
    Checksum:i4E9B5521313EF5B5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti331 – 3322EL → DV in AAA39728. (PubMed:1573844)Curated
    Sequence conflicti371 – 3722RA → SP in AAA39728. (PubMed:1573844)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS53139.1.
    RefSeqiNP_034963.2. NM_010833.2.
    UniGeneiMm.138876.

    Genome annotation databases

    EnsembliENSMUST00000117399; ENSMUSP00000113071; ENSMUSG00000031207.
    GeneIDi17698.
    KEGGimmu:17698.
    UCSCiuc009tug.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS53139.1.
    RefSeqi NP_034963.2. NM_010833.2.
    UniGenei Mm.138876.

    3D structure databases

    ProteinModelPortali P26041.
    SMRi P26041. Positions 3-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201534. 2 interactions.
    IntActi P26041. 5 interactions.
    MINTi MINT-4996580.

    PTM databases

    PhosphoSitei P26041.

    Proteomic databases

    MaxQBi P26041.
    PaxDbi P26041.
    PRIDEi P26041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000117399 ; ENSMUSP00000113071 ; ENSMUSG00000031207 .
    GeneIDi 17698.
    KEGGi mmu:17698.
    UCSCi uc009tug.1. mouse.

    Organism-specific databases

    CTDi 4478.
    MGIi MGI:97167. Msn.

    Phylogenomic databases

    eggNOGi NOG236035.
    GeneTreei ENSGT00650000092953.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi B1AX70.
    KOi K05763.
    OMAi PHVTEPM.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P26041.
    TreeFami TF313935.

    Miscellaneous databases

    ChiTaRSi MSN. mouse.
    NextBioi 292286.
    PROi P26041.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26041.
    Bgeei P26041.
    CleanExi MM_MSN.
    Genevestigatori P26041.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. 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 ]
    Pfami PF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002305. ERM. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiMOES_MOUSE
    AccessioniPrimary (citable) accession number: P26041
    Secondary accession number(s): B1AX70, Q3UL28, Q8BSN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3