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Protein

Ezrin

Gene

Ezr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).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. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. actin filament bundle assembly Source: UniProtKB
  2. establishment of endothelial barrier Source: MGI
  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. positive regulation of gene expression Source: MGI
  8. receptor internalization Source: MGI
  9. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

ReactomeiREACT_229826. Netrin-1 signaling.
REACT_257923. Recycling pathway of L1.

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

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. actin filament Source: UniProtKB
  3. apical part of cell Source: MGI
  4. apical plasma membrane Source: MGI
  5. astrocyte projection Source: Ensembl
  6. basolateral plasma membrane Source: UniProtKB
  7. cell body Source: Ensembl
  8. cell cortex Source: UniProtKB-SubCell
  9. cell tip Source: Ensembl
  10. ciliary basal body Source: MGI
  11. cytosol Source: MGI
  12. extracellular space Source: MGI
  13. extracellular vesicular exosome Source: MGI
  14. extrinsic component of membrane Source: UniProtKB
  15. filopodium Source: MGI
  16. focal adhesion Source: MGI
  17. intracellular Source: MGI
  18. membrane Source: MGI
  19. membrane raft Source: Ensembl
  20. microspike Source: Ensembl
  21. microvillus Source: MGI
  22. microvillus membrane Source: UniProtKB-SubCell
  23. myelin sheath Source: UniProtKB
  24. nucleolus Source: MGI
  25. plasma membrane Source: MGI
  26. ruffle Source: MGI
  27. ruffle membrane Source: UniProtKB-SubCell
  28. Schwann cell microvillus Source: Ensembl
  29. T-tubule Source: Ensembl
  30. uropod Source: MGI
  31. vesicle 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 – 11RemovedBy similarity
Chaini2 – 586585EzrinPRO_0000219409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei146 – 1461Phosphotyrosine; by PDGFRBy similarity
Modified residuei354 – 3541Phosphotyrosine; by PDGFRBy similarity
Modified residuei535 – 5351PhosphoserineBy similarity
Modified residuei567 – 5671Phosphothreonine; by ROCK2 and PKC/PRKCI1 Publication

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

BgeeiP26040.
CleanExiMM_EZR.
ExpressionAtlasiP26040. baseline and differential.
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).By similarity

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP26040.
SMRiP26040. Positions 1-586.
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

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236035.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26040.
KOiK08007.
OMAiSEVEEWQ.
OrthoDBiEOG7BGHK6.
PhylomeDBiP26040.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV
60 70 80 90 100
DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK
110 120 130 140 150
LFFLQVKDGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE
160 170 180 190 200
RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR GMLKDSAMLE YLKIAQDLEM
210 220 230 240 250
YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR
360 370 380 390 400
LQDYEQKTKR AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK
410 420 430 440 450
EELERQAQDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK
460 470 480 490 500
EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VNYHVQEGLQ DEGAEPMGYS
510 520 530 540 550
AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ ARDENKRTHN
560 570 580
DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
Length:586
Mass (Da):69,407
Last modified:January 23, 2007 - v3
Checksum:i5B7728F575F6DE3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481Q → P in CAA43086. (PubMed:1955455)Curated
Sequence conflicti325 – 3251T → A in CAA43086. (PubMed:1955455)Curated
Sequence conflicti570 – 5701Q → R in BAB22341. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP26040.
SMRiP26040. Positions 1-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL3102687.

Protein family/group databases

TCDBi8.A.25.1.1. the ezrin/radixin/moesin (ezrin) family.

PTM databases

PhosphoSiteiP26040.

2D gel databases

REPRODUCTION-2DPAGEP26040.

Proteomic databases

MaxQBiP26040.
PaxDbiP26040.
PRIDEiP26040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
GeneIDi22350.
KEGGimmu:22350.
UCSCiuc008ahv.1. mouse.

Organism-specific databases

CTDi7430.
MGIiMGI:98931. Ezr.

Phylogenomic databases

eggNOGiNOG236035.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP26040.
KOiK08007.
OMAiSEVEEWQ.
OrthoDBiEOG7BGHK6.
PhylomeDBiP26040.
TreeFamiTF313935.

Enzyme and pathway databases

ReactomeiREACT_229826. Netrin-1 signaling.
REACT_257923. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiEzr. mouse.
NextBioi302635.
PROiP26040.
SOURCEiSearch...

Gene expression databases

BgeeiP26040.
CleanExiMM_EZR.
ExpressionAtlasiP26040. baseline and differential.
GenevestigatoriP26040.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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]
ProtoNetiSearch...

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: February 4, 2015
This is version 139 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.