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P31977 (EZRI_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ezrin
Alternative name(s):
Cytovillin
Villin-2
p81
Gene names
Name:Ezr
Synonyms:Vil2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 regulation

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.

Subunit structure

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. Ref.6

Subcellular location

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. Ref.6 Ref.7

Tissue specificity

Glomerular epithelium cell (podocyte). Expressed in cerebrum, cerebellum and hippocampus (at protein level). Expressed in the small intestine, lung, kidney and ovaries. Ref.4 Ref.6 Ref.7

Developmental stage

Levels increase in the fetal gut epithelium between day 15 and day 20 of gestation and during the first week after birth. Ref.4

Post-translational modification

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.

Sequence similarities

Contains 1 FERM domain.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial cell differentiation

Inferred from expression pattern Ref.4. Source: RGD

establishment or maintenance of apical/basal cell polarity

Inferred from electronic annotation. Source: Ensembl

filopodium assembly

Inferred from mutant phenotype PubMed 21753079. Source: RGD

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

membrane to membrane docking

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSchwann cell microvillus

Inferred from direct assay PubMed 17045809. Source: RGD

T-tubule

Inferred from direct assay PubMed 19028724. Source: RGD

actin cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from direct assay Ref.6. Source: UniProtKB

astrocyte projection

Inferred from direct assay PubMed 21753079. Source: RGD

basolateral plasma membrane

Inferred from direct assay PubMed 11726633. Source: UniProtKB

cell body

Inferred from direct assay PubMed 11461930. Source: RGD

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell tip

Inferred from direct assay PubMed 17061246. Source: RGD

cytosol

Traceable author statement. Source: Reactome

extrinsic component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from direct assay PubMed 21753079. Source: RGD

focal adhesion

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from direct assay PubMed 21372499. Source: RGD

microspike

Inferred from direct assay PubMed 21753079. Source: RGD

microvillus membrane

Inferred from direct assay PubMed 11726633. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 21753079. Source: RGD

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

uropod

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion molecule binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6PubMed 11726633. Source: UniProtKB

protein complex binding

Inferred from physical interaction PubMed 21372499. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 17045809. Source: RGD

structural molecule activity

Traceable author statement Ref.4. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 586585Ezrin
PRO_0000219411

Regions

Domain2 – 295294FERM
Region244 – 586343Interaction with SCYL3 By similarity
Coiled coil300 – 466167 Potential

Amino acid modifications

Modified residue601N6-acetyllysine By similarity
Modified residue1461Phosphotyrosine; by PDGFR By similarity
Modified residue5351Phosphoserine By similarity
Modified residue5671Phosphothreonine; by ROCK2 and PKC/PRKCI By similarity

Experimental info

Sequence conflict4551D → E in AAL47844. Ref.3
Sequence conflict5311L → P in CAA48004. Ref.4
Sequence conflict5321L → Q in AAR91694. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31977 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3A5287052E74CCC9

FASTA58669,391
        10         20         30         40         50         60 
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK 

        70         80         90        100        110        120 
LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK LFFLQVKEGI LSDEIYCPPE 

       130        140        150        160        170        180 
TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR 

       190        200        210        220        230        240 
GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF 

       250        260        270        280        290        300 
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 

       310        320        330        340        350        360 
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDFEQKTKR 

       370        380        390        400        410        420 
AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE 

       430        440        450        460        470        480 
LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP 

       490        500        510        520        530        540 
VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ 

       550        560        570        580 
ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY428869 mRNA. Translation: AAR91694.1.
BC081958 mRNA. Translation: AAH81958.1.
AF450298 mRNA. Translation: AAL47844.1.
X67788 mRNA. Translation: CAA48004.1.
PIRS58759.
RefSeqNP_062230.1. NM_019357.1.
UniGeneRn.773.

3D structure databases

ProteinModelPortalP31977.
SMRP31977. Positions 1-385, 500-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248535. 1 interaction.
IntActP31977. 2 interactions.
MINTMINT-4570080.

PTM databases

PhosphoSiteP31977.

2D gel databases

World-2DPAGE0004:P31977.

Proteomic databases

PaxDbP31977.
PRIDEP31977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
GeneID54319.
KEGGrno:54319.

Organism-specific databases

CTD7430.
RGD621161. Ezr.

Phylogenomic databases

eggNOGNOG236035.
GeneTreeENSGT00650000092953.
HOGENOMHOG000007113.
HOVERGENHBG002185.
InParanoidP31977.
KOK08007.
OMALQDEGTE.
OrthoDBEOG7BGHK6.
PhylomeDBP31977.
TreeFamTF313935.

Enzyme and pathway databases

ReactomeREACT_195021. Developmental Biology.

Gene expression databases

GenevestigatorP31977.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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]
PfamPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFPIRSF002305. ERM. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio611002.
PROP31977.

Entry information

Entry nameEZRI_RAT
AccessionPrimary (citable) accession number: P31977
Secondary accession number(s): Q5WQV4, Q66H97, Q8VHK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families