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P26040 (EZRI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.5

Subunit structure

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.

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). Localizes to cell extensions and peripheral processes of astrocytes By similarity.

Tissue specificity

Expressed in cerebrum and cerebellum (at protein level). Component of the microvilli of intestinal epithelial cells. Ref.6

Developmental stage

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. Ref.6

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. Ref.5

Sequence similarities

Contains 1 FERM domain.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   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 electronic annotation. Source: Ensembl

establishment or maintenance of apical/basal cell polarity

Inferred from mutant phenotype PubMed 15177033. Source: MGI

filopodium assembly

Inferred from electronic annotation. Source: Ensembl

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

membrane to membrane docking

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from mutant phenotype PubMed 16365167. Source: MGI

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSchwann cell microvillus

Inferred from electronic annotation. Source: Ensembl

T-tubule

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament

Inferred from sequence or structural similarity. Source: UniProtKB

apical part of cell

Inferred from direct assay PubMed 14996907PubMed 9890997. Source: MGI

apical plasma membrane

Inferred from direct assay PubMed 14625387. Source: MGI

astrocyte projection

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell body

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell tip

Inferred from electronic annotation. Source: Ensembl

ciliary basal body

Inferred from direct assay PubMed 14996907. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

extrinsic component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

intracellular

Inferred from direct assay PubMed 17122142. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

microspike

Inferred from electronic annotation. Source: Ensembl

microvillus

Inferred from direct assay PubMed 17138661PubMed 20551175PubMed 23284756. Source: MGI

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 21377456. Source: MGI

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

uropod

Inferred from direct assay PubMed 11728336. Source: MGI

   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 PubMed 12068294. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 586585Ezrin
PRO_0000219409

Regions

Domain2 – 295294FERM
Region244 – 586343Interaction with SCYL3 By similarity

Amino acid modifications

Modified residue601N6-acetyllysine By similarity
Modified residue1461Phosphotyrosine; by PDGFR By similarity
Modified residue3541Phosphotyrosine; by PDGFR By similarity
Modified residue5351Phosphoserine By similarity
Modified residue5671Phosphothreonine; by ROCK2 and PKC/PRKCI Probable

Experimental info

Sequence conflict481Q → P in CAA43086. Ref.1
Sequence conflict3251T → A in CAA43086. Ref.1
Sequence conflict5701Q → R in BAB22341. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26040 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5B7728F575F6DE3E

FASTA58669,407
        10         20         30         40         50         60 
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK 

        70         80         90        100        110        120 
LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK LFFLQVKDGI 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 LQDYEQKTKR 

       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]"Radixin is a novel member of the band 4.1 family."
Funayama N., Nagafuchi A., Sato N., Tsukita S., Tsukita S.
J. Cell Biol. 115:1039-1048(1991) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60671 mRNA. Translation: CAA43086.1.
AK002766 mRNA. Translation: BAB22341.1.
BC048181 mRNA. Translation: AAH48181.2.
CCDSCCDS37428.1.
PIRB41129.
RefSeqNP_033536.2. NM_009510.2.
UniGeneMm.277812.

3D structure databases

ProteinModelPortalP26040.
SMRP26040. Positions 1-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204522. 2 interactions.
IntActP26040. 7 interactions.
MINTMINT-1708640.

Protein family/group databases

TCDB8.A.25.1.1. the ezrin/radixin/moesin (ezrin) family.

PTM databases

PhosphoSiteP26040.

2D gel databases

REPRODUCTION-2DPAGEP26040.

Proteomic databases

MaxQBP26040.
PaxDbP26040.
PRIDEP26040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
GeneID22350.
KEGGmmu:22350.
UCSCuc008ahv.1. mouse.

Organism-specific databases

CTD7430.
MGIMGI:98931. Ezr.

Phylogenomic databases

eggNOGNOG236035.
HOGENOMHOG000007113.
HOVERGENHBG002185.
InParanoidP26040.
KOK08007.
OMALQDEGTE.
OrthoDBEOG7BGHK6.
PhylomeDBP26040.
TreeFamTF313935.

Gene expression databases

ArrayExpressP26040.
BgeeP26040.
CleanExMM_EZR.
GenevestigatorP26040.

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

ChiTaRSEZR. mouse.
NextBio302635.
PROP26040.
SOURCESearch...

Entry information

Entry nameEZRI_MOUSE
AccessionPrimary (citable) accession number: P26040
Secondary accession number(s): Q80ZT8, Q9DCI1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 134 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot