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P26040

- EZRI_MOUSE

UniProt

P26040 - EZRI_MOUSE

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Protein
Ezrin
Gene
Ezr, Vil2
Organism
Mus musculus (Mouse)
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.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
Complete GO annotation...

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; 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.

GO - Cellular componenti

  1. Schwann cell microvillus Source: Ensembl
  2. T-tubule Source: Ensembl
  3. actin cytoskeleton Source: UniProtKB
  4. actin filament Source: UniProtKB
  5. apical part of cell Source: MGI
  6. apical plasma membrane Source: MGI
  7. astrocyte projection Source: Ensembl
  8. basolateral plasma membrane Source: UniProtKB
  9. cell body Source: Ensembl
  10. cell cortex Source: UniProtKB-SubCell
  11. cell tip Source: Ensembl
  12. ciliary basal body Source: MGI
  13. cytosol Source: Ensembl
  14. extrinsic component of membrane Source: UniProtKB
  15. filopodium Source: Ensembl
  16. focal adhesion Source: Ensembl
  17. intracellular Source: MGI
  18. membrane raft Source: Ensembl
  19. microspike Source: Ensembl
  20. microvillus Source: MGI
  21. microvillus membrane Source: UniProtKB-SubCell
  22. nucleolus Source: Ensembl
  23. plasma membrane Source: MGI
  24. ruffle membrane Source: UniProtKB-SubCell
  25. uropod Source: MGI
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_0000219409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysine By similarity
Modified residuei146 – 1461Phosphotyrosine; by PDGFR By similarity
Modified residuei354 – 3541Phosphotyrosine; by PDGFR By similarity
Modified residuei535 – 5351Phosphoserine By similarity
Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI Inferred

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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP26040.
SMRiP26040. Positions 1-586.

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

Sequence similaritiesi

Contains 1 FERM domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481Q → P in CAA43086. 1 Publication
Sequence conflicti325 – 3251T → A in CAA43086. 1 Publication
Sequence conflicti570 – 5701Q → R in BAB22341. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 134 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

Similar proteinsi