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P26040

- EZRI_MOUSE

UniProt

P26040 - EZRI_MOUSE

Protein

Ezrin

Gene

Ezr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (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. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis By similarity.By similarity

    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. actin filament binding Source: UniProtKB
    2. cell adhesion molecule binding Source: BHF-UCL
    3. protein binding Source: MGI

    GO - Biological processi

    1. actin filament bundle assembly Source: UniProtKB
    2. epithelial cell differentiation Source: Ensembl
    3. establishment or maintenance of apical/basal cell polarity Source: MGI
    4. filopodium assembly Source: Ensembl
    5. leukocyte cell-cell adhesion Source: Ensembl
    6. membrane to membrane docking Source: Ensembl
    7. receptor internalization Source: MGI
    8. regulation of cell shape Source: UniProtKB-KW

    Keywords - Biological processi

    Cell shape

    Protein family/group databases

    TCDBi8.A.25.1.1. the ezrin/radixin/moesin (ezrin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ezrin
    Alternative name(s):
    Cytovillin
    Villin-2
    p81
    Gene namesi
    Name:Ezr
    Synonyms:Vil2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:98931. Ezr.

    Subcellular locationi

    Apical cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cell projectionmicrovillus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton By similarity
    Note: Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Microvillar peripheral membrane protein (cytoplasmic side). Localizes to cell extensions and peripheral processes of astrocytes By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. actin filament Source: UniProtKB
    3. apical part of cell Source: MGI
    4. apical plasma membrane Source: MGI
    5. astrocyte projection Source: Ensembl
    6. basolateral plasma membrane Source: UniProtKB
    7. cell body Source: Ensembl
    8. cell cortex Source: UniProtKB-SubCell
    9. cell tip Source: Ensembl
    10. ciliary basal body Source: MGI
    11. cytosol Source: Ensembl
    12. extrinsic component of membrane Source: UniProtKB
    13. filopodium Source: Ensembl
    14. focal adhesion Source: Ensembl
    15. intracellular Source: MGI
    16. membrane raft Source: Ensembl
    17. microspike Source: Ensembl
    18. microvillus Source: MGI
    19. microvillus membrane Source: UniProtKB-SubCell
    20. nucleolus Source: Ensembl
    21. plasma membrane Source: MGI
    22. ruffle membrane Source: UniProtKB-SubCell
    23. Schwann cell microvillus Source: Ensembl
    24. T-tubule Source: Ensembl
    25. uropod Source: MGI

    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 – 586585EzrinPRO_0000219409Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601N6-acetyllysineBy similarity
    Modified residuei146 – 1461Phosphotyrosine; by PDGFRBy similarity
    Modified residuei354 – 3541Phosphotyrosine; by PDGFRBy similarity
    Modified residuei535 – 5351PhosphoserineBy similarity
    Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI1 Publication

    Post-translational modificationi

    Phosphorylated by tyrosine-protein kinases. 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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26040.
    PaxDbiP26040.
    PRIDEiP26040.

    2D gel databases

    REPRODUCTION-2DPAGEP26040.

    PTM databases

    PhosphoSiteiP26040.

    Expressioni

    Tissue specificityi

    Expressed in cerebrum and cerebellum (at protein level). Component of the microvilli of intestinal epithelial cells.1 Publication

    Developmental stagei

    Detected in whole embryo from E5 with highest expression at E8, E11, E12, and E18. Expressed at E18 in brain, a clear reduction occurs after birth followed by a transient increase around 2 weeks to 1 month. Hardly detected in adult brain.1 Publication

    Gene expression databases

    ArrayExpressiP26040.
    BgeeiP26040.
    CleanExiMM_EZR.
    GenevestigatoriP26040.

    Interactioni

    Subunit structurei

    Interacts with MCC, MPP5, PLEKHG6, SCYL3/PACE1, SLC9A3R1, SLC9A3R2 and TMEM8B. Found in a complex with EZR, PODXL and SLC9A3R2. Interacts with PODXL and SLC9A3R2. Interacts (when phosphorylated) with FES/FPS By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204522. 2 interactions.
    IntActiP26040. 7 interactions.
    MINTiMINT-1708640.

    Structurei

    3D structure databases

    ProteinModelPortaliP26040.
    SMRiP26040. Positions 1-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni244 – 586343Interaction with SCYL3By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236035.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    InParanoidiP26040.
    KOiK08007.
    OMAiLQDEGTE.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP26040.
    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.

    P26040-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV    50
    DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK 100
    LFFLQVKDGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE 150
    RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR GMLKDSAMLE YLKIAQDLEM 200
    YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF 250
    NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 300
    EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR 350
    LQDYEQKTKR AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK 400
    EELERQAQDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK 450
    EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VNYHVQEGLQ DEGAEPMGYS 500
    AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ ARDENKRTHN 550
    DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM 586
    Length:586
    Mass (Da):69,407
    Last modified:January 23, 2007 - v3
    Checksum:i5B7728F575F6DE3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481Q → P in CAA43086. (PubMed:1955455)Curated
    Sequence conflicti325 – 3251T → A in CAA43086. (PubMed:1955455)Curated
    Sequence conflicti570 – 5701Q → R in BAB22341. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60671 mRNA. Translation: CAA43086.1.
    AK002766 mRNA. Translation: BAB22341.1.
    BC048181 mRNA. Translation: AAH48181.2.
    CCDSiCCDS37428.1.
    PIRiB41129.
    RefSeqiNP_033536.2. NM_009510.2.
    UniGeneiMm.277812.

    Genome annotation databases

    EnsembliENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
    GeneIDi22350.
    KEGGimmu:22350.
    UCSCiuc008ahv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60671 mRNA. Translation: CAA43086.1 .
    AK002766 mRNA. Translation: BAB22341.1 .
    BC048181 mRNA. Translation: AAH48181.2 .
    CCDSi CCDS37428.1.
    PIRi B41129.
    RefSeqi NP_033536.2. NM_009510.2.
    UniGenei Mm.277812.

    3D structure databases

    ProteinModelPortali P26040.
    SMRi P26040. Positions 1-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204522. 2 interactions.
    IntActi P26040. 7 interactions.
    MINTi MINT-1708640.

    Protein family/group databases

    TCDBi 8.A.25.1.1. the ezrin/radixin/moesin (ezrin) family.

    PTM databases

    PhosphoSitei P26040.

    2D gel databases

    REPRODUCTION-2DPAGE P26040.

    Proteomic databases

    MaxQBi P26040.
    PaxDbi P26040.
    PRIDEi P26040.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064234 ; ENSMUSP00000063734 ; ENSMUSG00000052397 .
    GeneIDi 22350.
    KEGGi mmu:22350.
    UCSCi uc008ahv.1. mouse.

    Organism-specific databases

    CTDi 7430.
    MGIi MGI:98931. Ezr.

    Phylogenomic databases

    eggNOGi NOG236035.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi P26040.
    KOi K08007.
    OMAi LQDEGTE.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P26040.
    TreeFami TF313935.

    Miscellaneous databases

    ChiTaRSi EZR. mouse.
    NextBioi 302635.
    PROi P26040.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26040.
    Bgeei P26040.
    CleanExi MM_EZR.
    Genevestigatori P26040.

    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. 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.
      Tissue: Kidney.
    3. "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: C57BL/6.
      Tissue: Brain.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 264-273, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "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-567, ENZYME REGULATION.
    6. "Characterization of the NF2 protein merlin and the ERM protein ezrin in human, rat, and mouse central nervous system."
      Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T., Wartiovaara K., Vaheri A., Carpen O.
      Mol. Cell. Neurosci. 28:683-693(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiEZRI_MOUSE
    AccessioniPrimary (citable) accession number: P26040
    Secondary accession number(s): Q80ZT8, Q9DCI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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. 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