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P31977

- EZRI_RAT

UniProt

P31977 - EZRI_RAT

Protein

Ezrin

Gene

Ezr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (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.By similarity

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. cell adhesion molecule binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. protein complex binding Source: RGD
    5. protein domain specific binding Source: RGD
    6. structural molecule activity Source: RGD

    GO - Biological processi

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

    Keywords - Biological processi

    Cell shape

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ezrin
    Alternative name(s):
    Cytovillin
    Villin-2
    p81
    Gene namesi
    Name:Ezr
    Synonyms:Vil2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi621161. 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) By similarity. Localizes to cell extensions and peripheral processes of astrocytes. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells.By similarity2 Publications

    GO - Cellular componenti

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

    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_0000219411Add
    BLAST

    Amino acid modifications

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

    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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP31977.
    PRIDEiP31977.

    2D gel databases

    World-2DPAGE0004:P31977.

    PTM databases

    PhosphoSiteiP31977.

    Expressioni

    Tissue specificityi

    Glomerular epithelium cell (podocyte). Expressed in cerebrum, cerebellum and hippocampus (at protein level). Expressed in the small intestine, lung, kidney and ovaries.3 Publications

    Developmental stagei

    Levels increase in the fetal gut epithelium between day 15 and day 20 of gestation and during the first week after birth.1 Publication

    Gene expression databases

    GenevestigatoriP31977.

    Interactioni

    Subunit structurei

    Interacts with MCC, MPP5, PLEKHG6, SCYL3/PACE1, SLC9A3R1, SCYL3/PACE1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS By similarity. Found in a complex with EZR, PODXL and SLC9A3R2. Interacts with PODXL and SLC9A3R2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi248535. 1 interaction.
    IntActiP31977. 2 interactions.
    MINTiMINT-4570080.

    Structurei

    3D structure databases

    ProteinModelPortaliP31977.
    SMRiP31977. Positions 1-385, 500-586.
    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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili300 – 466167Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG236035.
    GeneTreeiENSGT00650000092953.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    InParanoidiP31977.
    KOiK08007.
    OMAiLQDEGTE.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP31977.
    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.

    P31977-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV    50
    DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK 100
    LFFLQVKEGI 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
    LQDFEQKTKR 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):69,391
    Last modified:January 23, 2007 - v3
    Checksum:i3A5287052E74CCC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti455 – 4551D → E in AAL47844. 1 PublicationCurated
    Sequence conflicti531 – 5311L → P in CAA48004. (PubMed:7640303)Curated
    Sequence conflicti532 – 5321L → Q in AAR91694. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY428869 mRNA. Translation: AAR91694.1.
    BC081958 mRNA. Translation: AAH81958.1.
    AF450298 mRNA. Translation: AAL47844.1.
    X67788 mRNA. Translation: CAA48004.1.
    PIRiS58759.
    RefSeqiNP_062230.1. NM_019357.1.
    UniGeneiRn.773.

    Genome annotation databases

    EnsembliENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
    GeneIDi54319.
    KEGGirno:54319.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY428869 mRNA. Translation: AAR91694.1 .
    BC081958 mRNA. Translation: AAH81958.1 .
    AF450298 mRNA. Translation: AAL47844.1 .
    X67788 mRNA. Translation: CAA48004.1 .
    PIRi S58759.
    RefSeqi NP_062230.1. NM_019357.1.
    UniGenei Rn.773.

    3D structure databases

    ProteinModelPortali P31977.
    SMRi P31977. Positions 1-385, 500-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248535. 1 interaction.
    IntActi P31977. 2 interactions.
    MINTi MINT-4570080.

    PTM databases

    PhosphoSitei P31977.

    2D gel databases

    World-2DPAGE 0004:P31977.

    Proteomic databases

    PaxDbi P31977.
    PRIDEi P31977.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000046746 ; ENSRNOP00000046593 ; ENSRNOG00000018524 .
    GeneIDi 54319.
    KEGGi rno:54319.

    Organism-specific databases

    CTDi 7430.
    RGDi 621161. Ezr.

    Phylogenomic databases

    eggNOGi NOG236035.
    GeneTreei ENSGT00650000092953.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi P31977.
    KOi K08007.
    OMAi LQDEGTE.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P31977.
    TreeFami TF313935.

    Miscellaneous databases

    NextBioi 611002.
    PROi P31977.

    Gene expression databases

    Genevestigatori P31977.

    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. "Rattus norvegicus ezrin."
      Harita Y., Koike H., Han G., Miyauchi N., Karasawa T., Suzuki K., Shimizu F., Kawachi H.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
    2. "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].
      Tissue: Lung.
    3. Gunn-Moore F.J., Tait S., Brophy P.J.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-455.
      Strain: Sprague-Dawley.
    4. "Transcriptional regulation of the ezrin gene during rat intestinal development and epithelial differentiation."
      Barila D., Murgia C., Nobili F., Perozzi G.
      Biochim. Biophys. Acta 1263:133-140(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 427-586, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Wistar.
      Tissue: Intestine.
    5. Lubec G., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 28-35; 101-107; 263-273; 372-379; 428-435 AND 530-542, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    6. "Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton."
      Takeda T., McQuistan T., Orlando R.A., Farquhar M.G.
      J. Clin. Invest. 108:289-301(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PODXL AND SLC9A3R2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "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, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiEZRI_RAT
    AccessioniPrimary (citable) accession number: P31977
    Secondary accession number(s): Q5WQV4, Q66H97, Q8VHK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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