(data stored in ACNUC9306 zone)

HOGENOM: RAT1_PE371

ID   RAT1_PE371                           STANDARD;      PRT;   586 AA.
AC   RAT1_PE371; P31977; Q5WQV4; Q66H97; Q8VHK3;
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; (RAT1.PE371).
GN   Name=Ezr; Synonyms=Vil2;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT1.PE371.
CC       Rattus norvegicus chromosome 1 RGSC3.4  sequence 1..267910886
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:EZRI_RAT
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       SCYL3/PACE1 and TMEM8B. Interacts (when phosphorylated) with
CC       FES/FPS (By similarity). Found in a complex with EZR, PODXL and
CC       SLC9A3R2. Interacts with PODXL and SLC9A3R2.
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=Localization to the apical membrane of parietal cells depends
CC       on the interaction with MPP5. Microvillar peripheral membrane
CC       protein (cytoplasmic side) (By similarity). Localizes to cell
CC       extensions and peripheral processes of astrocytes. Colocalizes
CC       with EZR and SLC9A3R2 at the apical cell membrane of glomerular
CC       epithelium cells.
CC   -!- TISSUE SPECIFICITY: Glomerular epithelium cell (podocyte).
CC       Expressed in cerebrum, cerebellum and hippocampus (at protein
CC       level). Expressed in the small intestine, lung, kidney and
CC       ovaries.
CC   -!- DEVELOPMENTAL STAGE: Levels increase in the fetal gut epithelium
CC       between day 15 and day 20 of gestation and during the first week
CC       after birth.
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:Rattus_norvegicus;ENSRNOG00000018524;ENSRNOT00000046746;ENSRNOP00000046593.
DR   EMBL; AF450298; - ;
DR   EMBL; AY428869; - ;
DR   EMBL; BC081958; - ;
DR   EMBL; X67788; - ;
DR   UniProtKB/Swiss-Prot; P31977; Q5WQV4; Q66H97; Q8VHK3; -.
DR   EMBL; AY428869; AAR91694.1; -; mRNA.
DR   EMBL; BC081958; AAH81958.1; -; mRNA.
DR   EMBL; AF450298; AAL47844.1; -; mRNA.
DR   EMBL; X67788; CAA48004.1; -; mRNA.
DR   IPI; IPI00470254; -.
DR   PIR; S58759; S58759.
DR   RefSeq; NP_062230.1; NM_019357.1.
DR   UniGene; Rn.773; -.
DR   ProteinModelPortal; P31977; -.
DR   SMR; P31977; 1-385, 500-586.
DR   IntAct; P31977; 1.
DR   STRING; P31977; -.
DR   PhosphoSite; P31977; -.
DR   World-2DPAGE; 0004:P31977; -.
DR   PRIDE; P31977; -.
DR   Ensembl; ENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524.
DR   GeneID; 54319; -.
DR   KEGG; rno:54319; -.
DR   UCSC; AY428869; rat.
DR   CTD; 7430; -.
DR   RGD; 621161; Ezr.
DR   eggNOG; roNOG13879; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   InParanoid; P31977; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   Reactome; REACT_94408; Axon guidance.
DR   NextBio; 611002; -.
DR   ArrayExpress; P31977; -.
DR   Genevestigator; P31977; -.
DR   GermOnline; ENSRNOG00000018524; Rattus norvegicus.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0019898; C:extrinsic to membrane; ISS:UniProtKB.
DR   GO; GO:0031528; C:microvillus membrane; IDA: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:0005198; F:structural molecule activity; TAS:RGD.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:RGD.
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; RAT1.PE371; -.
KW   ENSRNOG00000018524820036002503210000011;
KW   Ezr; EZRI_RAT; AF450298; AY428869; BC081958; X67788;
KW   Acetylation; Cell membrane; Cell projection; Cell shape; Coiled coil;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Membrane; Phosphoprotein; Reference proteome.
SQ   SEQUENCE   586 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK
     LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK LFFLQVKEGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
     GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDFEQKTKR
     AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE
     LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP
     VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ
     ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
//

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