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Protein

Ezrin

Gene

Ezr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processCell shape

Enzyme and pathway databases

ReactomeiR-RNO-373752 Netrin-1 signaling
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621161 Ezr

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194111 – 586EzrinAdd BLAST586

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei146Phosphotyrosine; by PDGFRBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei478PhosphotyrosineBy similarity1
Modified residuei535PhosphoserineCombined sources1
Modified residuei567Phosphothreonine; by ROCK2 and PKC/PRKCIBy similarity1

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-2DPAGEi0004:P31977

PTM databases

iPTMnetiP31977
PhosphoSitePlusiP31977

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

BgeeiENSRNOG00000018524
ExpressionAtlasiP31977 baseline and differential
GenevisibleiP31977 RN

Interactioni

Subunit structurei

Interacts with PODXL and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2 (PubMed:11457882). Interacts with MPP5. Interacts with MCC, PLEKHG6, 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. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin. Detected in a complex composed of at least EZR, AHNAK, PPL and PRX. Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition. Interacts with SPN, CD44 and ICAM2 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248535, 1 interactor
CORUMiP31977
IntActiP31977, 2 interactors
STRINGi10116.ENSRNOP00000046593

Structurei

3D structure databases

ProteinModelPortaliP31977
SMRiP31977
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 295FERMPROSITE-ProRule annotationAdd BLAST294

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni244 – 586Interaction with SCYL3By similarityAdd BLAST343

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili300 – 466Sequence analysisAdd BLAST167

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi115 – 120[IL]-x-C-x-x-[DE] motifBy similarity6

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3529 Eukaryota
ENOG410XQFP LUCA
GeneTreeiENSGT00920000148976
HOGENOMiHOG000007113
HOVERGENiHBG002185
InParanoidiP31977
KOiK08007
OMAiARDESKN
OrthoDBiEOG091G06UO
PhylomeDBiP31977
TreeFamiTF313935

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
Gene3Di1.20.80.10, 1 hit
1.25.40.1020, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR011174 ERM
IPR011259 ERM_C_dom
IPR000798 Ez/rad/moesin-like
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR019747 FERM_CS
IPR000299 FERM_domain
IPR018979 FERM_N
IPR018980 FERM_PH-like_C
IPR008954 Moesin_tail_sf
IPR011993 PH-like_dom_sf
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF00769 ERM, 1 hit
PF09380 FERM_C, 1 hit
PF00373 FERM_M, 1 hit
PF09379 FERM_N, 1 hit
PIRSFiPIRSF002305 ERM, 1 hit
PRINTSiPR00935 BAND41
PR00661 ERMFAMILY
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM01196 FERM_C, 1 hit
SUPFAMiSSF47031 SSF47031, 1 hit
SSF48678 SSF48678, 1 hit
SSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00660 FERM_1, 1 hit
PS00661 FERM_2, 1 hit
PS50057 FERM_3, 1 hit

Sequencei

Sequence statusi: Complete.

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)DescriptionActionsGraphical viewLength
Sequence conflicti455D → E in AAL47844 (Ref. 3) Curated1
Sequence conflicti531L → P in CAA48004 (PubMed:7640303).Curated1
Sequence conflicti532L → Q in AAR91694 (Ref. 1) Curated1

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

Similar proteinsi

Entry informationi

Entry nameiEZRI_RAT
AccessioniPrimary (citable) accession number: P31977
Secondary accession number(s): Q5WQV4, Q66H97, Q8VHK3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 159 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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