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P31977

- EZRI_RAT

UniProt

P31977 - EZRI_RAT

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Protein
Ezrin
Gene
Ezr, Vil2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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
Complete GO annotation...

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
Complete GO annotation...

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; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection By similarity. Cell projectionmicrovillus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionruffle membrane; Peripheral membrane protein; 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.2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 586585Ezrin
PRO_0000219411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysine By similarity
Modified residuei146 – 1461Phosphotyrosine; by PDGFR By similarity
Modified residuei535 – 5351Phosphoserine By similarity
Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI By 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.

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 SLC9A3R2.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 295294FERM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 586343Interaction with SCYL3 By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili300 – 466167 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 1 FERM domain.

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

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 121 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

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