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Protein

Ezrin

Gene

EZR

Organism
Bos taurus (Bovine)
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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

ReactomeiR-BTA-373752. Netrin-1 signaling.
R-BTA-437239. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Ezrin
Alternative name(s):
Cytovillin
Villin-2
p81
Gene namesi
Name:EZR
Synonyms:VIL2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 9

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 581580EzrinPRO_0000219407Add
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 residuei366 – 3661PhosphoserineBy similarity
Modified residuei476 – 4761PhosphotyrosineBy similarity
Modified residuei562 – 5621Phosphothreonine; by ROCK2 and PKC/PRKCIBy 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).By similarity
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP31976.
PeptideAtlasiP31976.
PRIDEiP31976.

Expressioni

Tissue specificityi

Detected in eye lens fiber cells (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with MPP5 and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2 (By similarity). Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (PubMed:14625392).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013663.

Structurei

3D structure databases

ProteinModelPortaliP31976.
SMRiP31976. Positions 1-324, 493-581.
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 – 581338Interaction with SCYL3By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi115 – 1206[IL]-x-C-x-x-[DE] motifBy similarity

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP31976.
KOiK08007.
OMAiPGYLNSE.
OrthoDBiEOG7BGHK6.
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_dom-like.
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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 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.

P31976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV
60 70 80 90 100
DNKGFPTWLK LDKKVSAQEV RKESPLQFKF RAKFYPEDVA EELIQDITQK
110 120 130 140 150
LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE LHKAGYLGSE
160 170 180 190 200
RLIPQRVMDQ HKLTRDQWED 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 MREKEELMLR
360 370 380 390 400
LQDYEEKTRK AEKELSDQIQ RALKLEEERK RAQEEAGRLE ADRLAALRAK
410 420 430 440 450
EELERQAADQ IKSQEQLATE LAEYTAKIAL LEEARRRKEN EVEEWQLRAK
460 470 480 490 500
EAQDDLVKTR EELHLVMTAP PPPPVYEPVN YHVHEGPQEE GTELSAELSS
510 520 530 540 550
EGILDDRNEE KRITEAEKNE RVQRQLMTLT SELSQARDEN KRTHNDIIHN
560 570 580
ENMRQGRDKY KTLRQIRQGN TKQRIDEFEA M
Length:581
Mass (Da):68,760
Last modified:January 23, 2007 - v2
Checksum:iB00D3FBCD294EAD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98498 mRNA. Translation: AAA30510.1.
BC102573 mRNA. Translation: AAI02574.1.
PIRiI45889.
RefSeqiNP_776642.1. NM_174217.2.
XP_010799028.1. XM_010800726.2.
UniGeneiBt.3583.

Genome annotation databases

EnsembliENSBTAT00000013663; ENSBTAP00000013663; ENSBTAG00000010347.
GeneIDi281574.
KEGGibta:281574.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98498 mRNA. Translation: AAA30510.1.
BC102573 mRNA. Translation: AAI02574.1.
PIRiI45889.
RefSeqiNP_776642.1. NM_174217.2.
XP_010799028.1. XM_010800726.2.
UniGeneiBt.3583.

3D structure databases

ProteinModelPortaliP31976.
SMRiP31976. Positions 1-324, 493-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013663.

Proteomic databases

PaxDbiP31976.
PeptideAtlasiP31976.
PRIDEiP31976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013663; ENSBTAP00000013663; ENSBTAG00000010347.
GeneIDi281574.
KEGGibta:281574.

Organism-specific databases

CTDi7430.

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00830000128251.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP31976.
KOiK08007.
OMAiPGYLNSE.
OrthoDBiEOG7BGHK6.
TreeFamiTF313935.

Enzyme and pathway databases

ReactomeiR-BTA-373752. Netrin-1 signaling.
R-BTA-437239. Recycling pathway of L1.

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_dom-like.
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.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 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. "Ezrin and osteonectin, two proteins associated with cell shape and growth, are enriched in the locus coeruleus."
    Bergson C.M., Zhao H., Saijoh K., Duman R.S., Nestler E.J.
    Mol. Cell. Neurosci. 4:64-73(1993)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Proteins and their amino acid compositions: uniqueness, variability, and applications."
    Galat A., Gerbod M.C., Bouet F., Riviere S.
    Arch. Biochem. Biophys. 330:229-237(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16 AND 127-141.
    Tissue: Kidney.
  4. "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells."
    Straub B.K., Boda J., Kuhn C., Schnoelzer M., Korf U., Kempf T., Spring H., Hatzfeld M., Franke W.W.
    J. Cell Sci. 116:4985-4995(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION IN A COMPLEX WITH PRX; AHNAK AND PPL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiEZRI_BOVIN
AccessioniPrimary (citable) accession number: P31976
Secondary accession number(s): Q3ZCB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 133 of the entry and version 2 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

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 one 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.