(data stored in ACNUC9306 zone)

SWISSPROT: EZRI_RABIT

ID   EZRI_RABIT              Reviewed;         586 AA.
AC   Q8HZQ5;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=Ezrin;
DE   AltName: Full=Cytovillin;
DE   AltName: Full=Villin-2;
DE   AltName: Full=p81;
GN   Name=EZR; Synonyms=VIL2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RA   Goldenring J.R.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH MPP5, AND SUBCELLULAR LOCATION.
RX   PubMed=15677456; DOI=10.1074/jbc.m411941200;
RA   Cao X., Ding X., Guo Z., Zhou R., Wang F., Long F., Wu F., Bi F., Wang Q.,
RA   Fan D., Forte J.G., Teng M., Yao X.;
RT   "PALS1 specifies the localization of Ezrin to the apical membrane of
RT   gastric parietal cells.";
RL   J. Biol. Chem. 280:13584-13592(2005).
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane (By similarity). In epithelial cells,
CC       required for the formation of microvilli and membrane ruffles on the
CC       apical pole. Along with PLEKHG6, required for normal macropinocytosis
CC       (By similarity). {ECO:0000250}.
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 MPP5 (PubMed:15677456). Found in a complex with
CC       EZR, PODXL and SLC9A3R2. Interacts with MCC, PLEKHG6, PODXL,
CC       SCYL3/PACE1, SLC9A3R1, SLC9A3R2 and TMEM8B. Interacts (when
CC       phosphorylated) with FES/FPS. Interacts with dimeric S100P, the
CC       interaction may be activating through unmasking of F-actin binding
CC       sites. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1,
CC       BFSP2, ANK2, PLEC, PRX and spectrin. Detected in a complex composed of
CC       at least EZR, AHNAK, PPL and PRX. Interacts with PDPN (via cytoplasmic
CC       domain); activates RHOA and promotes epithelial-mesenchymal transition.
CC       Interacts with SPN, 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:0000269|PubMed:15677456}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P15311}. Cell projection
CC       {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus membrane
CC       {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P15311}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus
CC       {ECO:0000250|UniProtKB:P26040}. Note=Localizes to cell extensions and
CC       peripheral processes of astrocytes (By similarity). Microvillar
CC       peripheral membrane protein (cytoplasmic side). Localization to the
CC       apical membrane of parietal cells depends on the interaction with MPP5.
CC       {ECO:0000250|UniProtKB:P15311, ECO:0000250|UniProtKB:P31977,
CC       ECO:0000269|PubMed:15677456}.
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}.
DR   EMBL; AF537266; AAN06818.1; -; mRNA.
DR   RefSeq; NP_001075591.1; NM_001082122.1.
DR   SMR; Q8HZQ5; -.
DR   STRING; 9986.ENSOCUP00000003322; -.
DR   iPTMnet; Q8HZQ5; -.
DR   PRIDE; Q8HZQ5; -.
DR   GeneID; 100008846; -.
DR   KEGG; ocu:100008846; -.
DR   CTD; 7430; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   eggNOG; ENOG410XQFP; LUCA.
DR   HOGENOM; HOG000007113; -.
DR   InParanoid; Q8HZQ5; -.
DR   KO; K08007; -.
DR   OrthoDB; 627741at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
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:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:0071437; C:invadopodium; ISS:UniProtKB.
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:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.1020; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C_dom.
DR   InterPro; IPR041789; ERM_FERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR008954; Moesin_tail_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF00769; ERM; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PIRSF; PIRSF002305; ERM; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF48678; SSF48678; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8HZQ5.
DR   SWISS-2DPAGE; Q8HZQ5.
KW   Acetylation; Cell membrane; Cell projection; Cell shape; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW   S-nitrosylation.
FT   CHAIN           1..586
FT                   /note="Ezrin"
FT                   /id="PRO_0000219410"
FT   DOMAIN          2..295
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          244..586
FT                   /note="Interaction with SCYL3"
FT                   /evidence="ECO:0000250"
FT   MOTIF           115..120
FT                   /note="[IL]-x-C-x-x-[DE] motif"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         146
FT                   /note="Phosphotyrosine; by PDGFR"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         354
FT                   /note="Phosphotyrosine; by PDGFR"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         478
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26040"
FT   MOD_RES         567
FT                   /note="Phosphothreonine; by ROCK2 and PKC/PRKCI"
FT                   /evidence="ECO:0000250|UniProtKB:P15311"
SQ   SEQUENCE   586 AA;  69220 MW;  FA2467B72E4B365E CRC64;
     MPKPINVRVT TMDAELEFAV QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
     LDKKVSAQEV RKENPVQFKF RAKFYPEDVS EELIQDITQK LFFLQVKEGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYSKE AHKAGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
     GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK NDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLESEKKRR EAVEQEKEQM LREKEELMMR LQDYEQKTKK
     AEKELSDQIQ RALQLEDERK RAQEESERLE ADRVAALRAK EELERQAADQ IKSQEQLAAE
     LAEYTAKIAL LEEARRRKES EVEEWQHRAR EAQDDLVKTK EELHLVMTAP PPPPPPMYEP
     VSYHVQEHLH EEGAESLGYS AELSSEGILD DRHEEKRITE AEKNERVQRQ LLTLSNELSQ
     ARDENKRTHN DIIHNENLRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
//

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