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O35763

- MOES_RAT

UniProt

O35763 - MOES_RAT

Protein

Moesin

Gene

Msn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (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.By similarity

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. protein binding, bridging Source: RGD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Moesin
    Alternative name(s):
    Membrane-organizing extension spike protein
    Gene namesi
    Name:Msn
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621260. Msn.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Apical cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionmicrovillus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    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 plasma membrane Source: UniProtKB-SubCell
    2. cell surface Source: RGD
    3. cell tip Source: RGD
    4. cytoplasmic side of plasma membrane Source: RGD
    5. cytoskeleton Source: UniProtKB-SubCell
    6. extrinsic component of membrane Source: InterPro
    7. filopodium membrane Source: RGD
    8. microvillus membrane Source: UniProtKB-SubCell
    9. secretory granule membrane Source: RGD
    10. T-tubule Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 577576MoesinPRO_0000219419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysineBy similarity
    Modified residuei116 – 1161PhosphotyrosineBy similarity
    Modified residuei139 – 1391N6-acetyllysineBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei558 – 5581Phosphothreonine; by ROCK2 and STK10By similarity

    Post-translational modificationi

    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. Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO35763.
    PRIDEiO35763.

    2D gel databases

    World-2DPAGE0004:O35763.

    PTM databases

    PhosphoSiteiO35763.

    Expressioni

    Gene expression databases

    GenevestigatoriO35763.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi249518. 2 interactions.
    IntActiO35763. 4 interactions.
    MINTiMINT-4571444.
    STRINGi10116.ENSRNOP00000043519.

    Structurei

    3D structure databases

    ProteinModelPortaliO35763.
    SMRiO35763. Positions 1-396, 488-577.
    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.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    InParanoidiO35763.
    KOiK05763.
    PhylomeDBiO35763.

    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.

    O35763-1 [UniParc]FASTAAdd to Basket

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    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 MAELTARVSQ LEMARKKKES EAEECHQKAQ 450
    MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA 500
    KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTT NDMIHAENMR 550
    LGRDKYKTLR QIRQGNTKQR IDEFESM 577
    Length:577
    Mass (Da):67,739
    Last modified:January 23, 2007 - v3
    Checksum:i49F47973D6C8FDC8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004811 mRNA. Translation: AAB61666.1.
    RefSeqiNP_110490.1. NM_030863.1.
    UniGeneiRn.2762.

    Genome annotation databases

    GeneIDi81521.
    KEGGirno:81521.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004811 mRNA. Translation: AAB61666.1 .
    RefSeqi NP_110490.1. NM_030863.1.
    UniGenei Rn.2762.

    3D structure databases

    ProteinModelPortali O35763.
    SMRi O35763. Positions 1-396, 488-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249518. 2 interactions.
    IntActi O35763. 4 interactions.
    MINTi MINT-4571444.
    STRINGi 10116.ENSRNOP00000043519.

    PTM databases

    PhosphoSitei O35763.

    2D gel databases

    World-2DPAGE 0004:O35763.

    Proteomic databases

    PaxDbi O35763.
    PRIDEi O35763.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81521.
    KEGGi rno:81521.

    Organism-specific databases

    CTDi 4478.
    RGDi 621260. Msn.

    Phylogenomic databases

    eggNOGi NOG236035.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi O35763.
    KOi K05763.
    PhylomeDBi O35763.

    Miscellaneous databases

    NextBioi 615037.

    Gene expression databases

    Genevestigatori O35763.

    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. "Cloning and cellular localization of the rat mast cell 78-kDa protein phosphorylated in response to the mast cell 'stabilizer' cromolyn."
      Theoharides T.C., Wang L., Pang X., Letourneau R., Culm K.E., Basu S., Wang Y., Correia I.
      J. Pharmacol. Exp. Ther. 294:810-821(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
    2. Lubec G., Afjehi-Sadat L.
      Submitted (DEC-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 262-272, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.

    Entry informationi

    Entry nameiMOES_RAT
    AccessioniPrimary (citable) accession number: O35763
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3