EZRI_MESAU
ID EZRI_MESAU Reviewed; 92 AA.
AC P86232;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Ezrin {ECO:0000250|UniProtKB:P15311};
DE AltName: Full=Cytovillin {ECO:0000250|UniProtKB:P15311};
DE AltName: Full=Villin-2 {ECO:0000250|UniProtKB:P15311};
DE AltName: Full=p81 {ECO:0000250|UniProtKB:P15311};
DE Flags: Fragments;
GN Name=EZR {ECO:0000250|UniProtKB:P15311};
GN Synonyms=VIL2 {ECO:0000250|UniProtKB:P15311};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. In epithelial cells, required for
CC the formation of microvilli and membrane ruffles on the apical pole.
CC Along with PLEKHG6, required for normal macropinocytosis (By
CC similarity). {ECO:0000250|UniProtKB:P15311}.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PALS1 and SLC9A3R2. Found in a complex with
CC EZR, PODXL and SLC9A3R2. Interacts with MCC, PLEKHG6, PODXL,
CC SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with
CC FES/FPS. Interacts with dimeric S100P, the interaction may be
CC activating through unmasking of F-actin binding sites. Identified in
CC complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX
CC and spectrin. Detected in a complex composed of at least EZR, AHNAK,
CC PPL and PRX. Interacts with PDPN (via cytoplasmic domain); activates
CC RHOA and promotes epithelial-mesenchymal transition. Interacts with
CC SPN/CD43 cytoplasmic tail, CD44 and ICAM2 (By similarity).
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P26040,
CC ECO:0000250|UniProtKB:P31976, ECO:0000250|UniProtKB:P31977,
CC ECO:0000250|UniProtKB:Q8HZQ5}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977}. Cell
CC projection {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977};
CC Cytoplasmic side {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P26040}. Note=Localization to the apical
CC membrane of parietal cells depends on the interaction with PALS1.
CC Microvillar peripheral membrane protein (cytoplasmic side). Localizes
CC to cell extensions and peripheral processes of astrocytes (By
CC similarity). {ECO:0000250|UniProtKB:P15311,
CC ECO:0000250|UniProtKB:P31977}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
CC -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by
CC ROCK2 suppresses the head-to-tail association of the N-terminal and C-
CC terminal halves resulting in an opened conformation which is capable of
CC actin and membrane-binding (By similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P15311}.
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DR AlphaFoldDB; P86232; -.
DR SMR; P86232; -.
DR PRIDE; P86232; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cell shape; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW S-nitrosylation.
FT CHAIN <1..>92
FT /note="Ezrin"
FT /id="PRO_0000394739"
FT DOMAIN <1..72
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 42..>92
FT /note="Interaction with SCYL3"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15311"
FT NON_CONS 8..9
FT /evidence="ECO:0000305"
FT NON_CONS 18..19
FT /evidence="ECO:0000305"
FT NON_CONS 26..27
FT /evidence="ECO:0000305"
FT NON_CONS 35..36
FT /evidence="ECO:0000305"
FT NON_CONS 71..72
FT /evidence="ECO:0000305"
FT NON_CONS 83..84
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 92
SQ SEQUENCE 92 AA; 11131 MW; A569D42682F6F914 CRC64;
QLFDQVVKGF PTWLKLDKKE NPVQFKIQVW HAEHRIGFPW SEIRNISFND KKFVIKPIDK
KAPDFVFYAP RRKPDTIEVQ QMKLQDFEQK TK
