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Protein

Ezrin

Gene

Ezr

Organism
Rattus norvegicus (Rat)
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

  • actin filament binding Source: UniProtKB
  • cell adhesion molecule binding Source: BHF-UCL
  • poly(A) RNA binding Source: Ensembl
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • structural molecule activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

ReactomeiREACT_286488. Recycling pathway of L1.
REACT_311439. Netrin-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ezrin
Alternative name(s):
Cytovillin
Villin-2
p81
Gene namesi
Name:Ezr
Synonyms:Vil2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621161. Ezr.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actin filament Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • astrocyte projection Source: RGD
  • basolateral plasma membrane Source: UniProtKB
  • brush border Source: Ensembl
  • cell body Source: RGD
  • cell cortex Source: UniProtKB-SubCell
  • cell tip Source: RGD
  • ciliary basal body Source: Ensembl
  • cytosol Source: Reactome
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • extrinsic component of membrane Source: UniProtKB
  • filopodium Source: RGD
  • focal adhesion Source: Ensembl
  • membrane raft Source: RGD
  • microspike Source: RGD
  • microvillus membrane Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleolus Source: Ensembl
  • plasma membrane Source: RGD
  • ruffle membrane Source: UniProtKB-SubCell
  • Schwann cell microvillus Source: RGD
  • T-tubule Source: RGD
  • uropod Source: Ensembl
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_0000219411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei83 – 831N6-succinyllysineBy similarity
Modified residuei116 – 1161PhosphotyrosineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei146 – 1461Phosphotyrosine; by PDGFRBy similarity
Modified residuei478 – 4781PhosphotyrosineBy similarity
Modified residuei567 – 5671Phosphothreonine; 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

PaxDbiP31977.
PRIDEiP31977.

2D gel databases

World-2DPAGE0004:P31977.

PTM databases

PhosphoSiteiP31977.

Expressioni

Tissue specificityi

Glomerular epithelium cell (podocyte). Expressed in cerebrum, cerebellum and hippocampus (at protein level). Expressed in the small intestine, lung, kidney and ovaries.3 Publications

Developmental stagei

Levels increase in the fetal gut epithelium between day 15 and day 20 of gestation and during the first week after birth.1 Publication

Gene expression databases

GenevisibleiP31977. RN.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi248535. 1 interaction.
IntActiP31977. 2 interactions.
MINTiMINT-4570080.
STRINGi10116.ENSRNOP00000046593.

Structurei

3D structure databases

ProteinModelPortaliP31977.
SMRiP31977. Positions 1-385, 500-586.
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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili300 – 466167Sequence AnalysisAdd
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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG236035.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP31977.
KOiK08007.
OMAiDEGSEYS.
OrthoDBiEOG7BGHK6.
PhylomeDBiP31977.
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.

P31977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV
60 70 80 90 100
DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK
110 120 130 140 150
LFFLQVKEGI 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
LQDFEQKTKR 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):69,391
Last modified:January 23, 2007 - v3
Checksum:i3A5287052E74CCC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551D → E in AAL47844 (Ref. 3) Curated
Sequence conflicti531 – 5311L → P in CAA48004 (PubMed:7640303).Curated
Sequence conflicti532 – 5321L → Q in AAR91694 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY428869 mRNA. Translation: AAR91694.1.
BC081958 mRNA. Translation: AAH81958.1.
AF450298 mRNA. Translation: AAL47844.1.
X67788 mRNA. Translation: CAA48004.1.
PIRiS58759.
RefSeqiNP_062230.1. NM_019357.1.
UniGeneiRn.773.

Genome annotation databases

EnsembliENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
GeneIDi54319.
KEGGirno:54319.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY428869 mRNA. Translation: AAR91694.1.
BC081958 mRNA. Translation: AAH81958.1.
AF450298 mRNA. Translation: AAL47844.1.
X67788 mRNA. Translation: CAA48004.1.
PIRiS58759.
RefSeqiNP_062230.1. NM_019357.1.
UniGeneiRn.773.

3D structure databases

ProteinModelPortaliP31977.
SMRiP31977. Positions 1-385, 500-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248535. 1 interaction.
IntActiP31977. 2 interactions.
MINTiMINT-4570080.
STRINGi10116.ENSRNOP00000046593.

PTM databases

PhosphoSiteiP31977.

2D gel databases

World-2DPAGE0004:P31977.

Proteomic databases

PaxDbiP31977.
PRIDEiP31977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
GeneIDi54319.
KEGGirno:54319.

Organism-specific databases

CTDi7430.
RGDi621161. Ezr.

Phylogenomic databases

eggNOGiNOG236035.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP31977.
KOiK08007.
OMAiDEGSEYS.
OrthoDBiEOG7BGHK6.
PhylomeDBiP31977.
TreeFamiTF313935.

Enzyme and pathway databases

ReactomeiREACT_286488. Recycling pathway of L1.
REACT_311439. Netrin-1 signaling.

Miscellaneous databases

NextBioi611002.
PROiP31977.

Gene expression databases

GenevisibleiP31977. RN.

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. "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.

Entry informationi

Entry nameiEZRI_RAT
AccessioniPrimary (citable) accession number: P31977
Secondary accession number(s): Q5WQV4, Q66H97, Q8VHK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 131 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. 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.