(data stored in ACNUC9306 zone)

HOGENOM: RABIT12_154_PE5

ID   RABIT12_154_PE5                      STANDARD;      PRT;   532 AA.
AC   RABIT12_154_PE5; Q8HZQ5;
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   Flags: Fragments;
DE   RecName: Full=Ezrin;AltName: Full=Cytovillin;AltName:
DE   Full=Villin-2;AltName: Full=p81; (RABIT12_154.PE5).
GN   Name=EZR; Synonyms=VIL2;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT12_154.PE5.
CC       Oryctolagus cuniculus chromosome 12 oryCun2 partial sequence
CC       148651370..149617632 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:EZRI_RABIT
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane (By similarity). In epithelial
CC       cells, required for the formation of microvilli and membrane
CC       ruffles on the apical pole. Along with PLEKHG6, required for
CC       normal macropinocytosis (By 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, 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). Interacts with MPP5.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Cell projection (By
CC       similarity). Cell projection, microvillus membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Cell
CC       projection, ruffle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cell cortex (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localizes to cell extensions and peripheral processes of
CC       astrocytes (By similarity). Microvillar peripheral membrane
CC       protein (cytoplasmic side). Localization to the apical membrane of
CC       parietal cells depends on the interaction with MPP5.
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:Oryctolagus_cuniculus;ENSOCUG00000003829;ENSOCUT00000003830;ENSOCUP00000003322.
DR   EMBL; AF537266; - ;
DR   UniProtKB/Swiss-Prot; Q8HZQ5; -.
DR   EMBL; AF537266; AAN06818.1; -; mRNA.
DR   RefSeq; NP_001075591.1; NM_001082122.1.
DR   UniGene; Ocu.2672; -.
DR   ProteinModelPortal; Q8HZQ5; -.
DR   SMR; Q8HZQ5; 1-378, 500-586.
DR   STRING; Q8HZQ5; -.
DR   Ensembl; ENSOCUT00000003830; ENSOCUP00000003322; ENSOCUG00000003829.
DR   GeneID; 100008846; -.
DR   CTD; 7430; -.
DR   eggNOG; maNOG15414; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   OrthoDB; EOG4C5CJJ; -.
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 to membrane; 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   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; RABIT12_154.PE5; -.
KW   ENSOCUG00000003829820036002503210000011;
KW   EZRI_RABIT; AF537266;
KW   Acetylation; Cell membrane; Cell projection; Cell shape; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein.
SQ   SEQUENCE   532 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKPINVRVT TMDAELEFAV QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
     LDKKVSAQEV RKENPVQFKF RAKFYPEDVS EELIQDITQK LFFLQVKEGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYSKE AHKAGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
     GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLESEKKRR EAVEQEKEQM LREKEELMVR LQDYEQKTKK
     AEKELSDQIQ RALQLEDERK RAQEESERLE ADRVAALRAK EELERQAADQ IKSQEQLAAE
     LAEYTAKIAL LEEARRRKES EVEEWQHRAR EAQDDLVKTK EELHLVMTAP PPPPPPMYEP
     VSYHVQEHLH EEGAESLGYS AELSSEGILD DRHEEKRITE AEKNERVQRQ LL
//

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