(data stored in ACNUC9306 zone)

HOGENOM: BOVIN9_102_PE5

ID   BOVIN9_102_PE5                       STANDARD;      PRT;   581 AA.
AC   BOVIN9_102_PE5; P31976; Q3ZCB9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Ezrin;AltName: Full=Cytovillin;AltName:
DE   Full=Villin-2;AltName: Full=p81; (BOVIN9_102.PE5).
GN   Name=EZR; Synonyms=VIL2;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN9_102.PE5.
CC       Bos taurus chromosome 9 Btau_4.0 partial sequence 98578118..99578117
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:EZRI_BOVIN
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane. In epithelial cells, required
CC       for the formation of microvilli and membrane ruffles on the apical
CC       pole. Along with PLEKHG6, required for normal macropinocytosis (By
CC       similarity).
CC   -!- ENZYME REGULATION: A head-to-tail association, of the N-terminal
CC       and C-terminal halves results in a closed conformation (inactive
CC       form) which is incapable of actin or membrane-binding (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with MCC, MPP5, PLEKHG6, SCYL3/PACE1, SLC9A3R1,
CC       SLC9A3R2 and TMEM8B. Found in a complex with EZR, PODXL and
CC       SLC9A3R2. Interacts with PODXL and SLC9A3R2. Interacts (when
CC       phosphorylated) with FES/FPS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cell projection. Cell projection,
CC       microvillus membrane; Peripheral membrane protein; Cytoplasmic
CC       side. Cell projection, ruffle membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm,
CC       cytoskeleton. Note=Localization to the apical membrane of parietal
CC       cells depends on the interaction with MPP5. Localizes to cell
CC       extensions and peripheral processes of astrocytes (By similarity).
CC   -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation
CC       by ROCK2 suppresses the head-to-tail association of the N-terminal
CC       and C-terminal halves resulting in an opened conformation which is
CC       capable of actin and membrane-binding (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000010347;ENSBTAT00000013663;ENSBTAP00000013663.
DR   EMBL; BC102573; - ;
DR   EMBL; M98498; - ;
DR   UniProtKB/Swiss-Prot; P31976; Q3ZCB9; -.
DR   EMBL; M98498; AAA30510.1; -; mRNA.
DR   EMBL; BC102573; AAI02574.1; -; mRNA.
DR   IPI; IPI00694641; -.
DR   PIR; I45889; I45889.
DR   RefSeq; NP_776642.1; NM_174217.2.
DR   UniGene; Bt.3583; -.
DR   ProteinModelPortal; P31976; -.
DR   SMR; P31976; 1-324, 493-581.
DR   STRING; P31976; -.
DR   PRIDE; P31976; -.
DR   Ensembl; ENSBTAT00000013663; ENSBTAP00000013663; ENSBTAG00000010347.
DR   GeneID; 281574; -.
DR   KEGG; bta:281574; -.
DR   CTD; 7430; -.
DR   eggNOG; maNOG15414; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   InParanoid; P31976; -.
DR   OMA; SEGIRDD; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   PhylomeDB; P31976; -.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:AgBase.
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 to membrane; ISS:UniProtKB.
DR   GO; GO:0005932; C:microtubule basal body; ISS:AgBase.
DR   GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001931; C:uropod; ISS:AgBase.
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:0035088; P:establishment or maintenance of apical/basal cell polarity; ISS:AgBase.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
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   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF48678; Moesin; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   HOGENOMDNA; BOVIN9_102.PE5; -.
KW   ENSBTAG00000010347fold_1320000031; ENSBTAP00000013663fold_1320000031;
KW   BC102573; M98498;
KW   Acetylation; Cell membrane; Cell projection; Cell shape;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Membrane; Phosphoprotein; Reference proteome.
SQ   SEQUENCE   581 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
     LDKKVSAQEV RKESPLQFKF RAKFYPEDVA EELIQDITQK LFFLQVKEGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYNKE LHKAGYLGSE RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR
     GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR LQDYEEKTRK
     AEKELSDQIQ RALKLEEERK RAQEEAGRLE ADRLAALRAK EELERQAADQ IKSQEQLATE
     LAEYTAKIAL LEEARRRKEN EVEEWQLRAK EAQDDLVKTR EELHLVMTAP PPPPVYEPVN
     YHVHEGPQEE GTELSAELSS EGILDDRNEE KRITEAEKNE RVQRQLMTLT SELSQARDEN
     KRTHNDIIHN ENMRQGRDKY KTLRQIRQGN TKQRIDEFEA M
//

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