(data stored in ACNUC9306 zone)

HOGENOM: MOUSE17_PE65

ID   MOUSE17_PE65                         STANDARD;      PRT;   586 AA.
AC   MOUSE17_PE65; P26040; Q80ZT8; Q9DCI1;
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; (MOUSE17.PE65).
GN   Name=Ezr; Synonyms=Vil2;
OS   MUS MUSCULUS.
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; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE17.PE65.
CC       Mus musculus chromosome 17 NCBIM37  sequence 1..95272651 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:EZRI_MOUSE
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.
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 (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). Localizes to cell extensions and
CC       peripheral processes of astrocytes (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in cerebrum and cerebellum (at
CC       protein level). Component of the microvilli of intestinal
CC       epithelial cells.
CC   -!- DEVELOPMENTAL STAGE: Detected in whole embryo from E5 with highest
CC       expression at E8, E11, E12, and E18. Expressed at E18 in brain, a
CC       clear reduction occurs after birth followed by a transient
CC       increase around 2 weeks to 1 month. Hardly detected in adult
CC       brain.
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.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000052397;ENSMUST00000064234;ENSMUSP00000063734.
DR   EMBL; AK002766; - ;
DR   EMBL; AK035271; - ;
DR   EMBL; AK135194; - ;
DR   EMBL; AK135353; - ;
DR   EMBL; AK145707; - ;
DR   EMBL; AK159717; - ;
DR   EMBL; AK159824; - ;
DR   EMBL; AK166191; - ;
DR   EMBL; AK168840; - ;
DR   EMBL; AK170610; - ;
DR   EMBL; AK172336; - ;
DR   EMBL; BC048181; - ;
DR   EMBL; BC098502; - ;
DR   EMBL; CH466692; - ;
DR   EMBL; X60671; - ;
DR   UniProtKB/Swiss-Prot; P26040; Q80ZT8; Q9DCI1; -.
DR   EMBL; X60671; CAA43086.1; -; mRNA.
DR   EMBL; AK002766; BAB22341.1; -; mRNA.
DR   EMBL; BC048181; AAH48181.2; -; mRNA.
DR   IPI; IPI00330862; -.
DR   PIR; B41129; B41129.
DR   RefSeq; NP_033536.2; NM_009510.2.
DR   UniGene; Mm.277812; -.
DR   ProteinModelPortal; P26040; -.
DR   SMR; P26040; 1-586.
DR   IntAct; P26040; 3.
DR   MINT; MINT-1708640; -.
DR   STRING; P26040; -.
DR   TCDB; 8.A.25.1.1; ezrin/radixin/moesin (Ezrin) family.
DR   PhosphoSite; P26040; -.
DR   REPRODUCTION-2DPAGE; P26040; -.
DR   PRIDE; P26040; -.
DR   Ensembl; ENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
DR   GeneID; 22350; -.
DR   KEGG; mmu:22350; -.
DR   CTD; 7430; -.
DR   MGI; MGI:98931; Ezr.
DR   eggNOG; roNOG13879; -.
DR   InParanoid; P26040; -.
DR   OMA; SEGIRDD; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   PhylomeDB; P26040; -.
DR   NextBio; 457682; -.
DR   ArrayExpress; P26040; -.
DR   Bgee; P26040; -.
DR   CleanEx; MM_EZR; -.
DR   Genevestigator; P26040; -.
DR   GermOnline; ENSMUSG00000052397; Mus musculus.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001931; C:uropod; IDA:MGI.
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; IMP:MGI.
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; MOUSE17.PE65; -.
KW   ENSMUSG000000523975old_1320000031; ENSMUSP000000637341old_1320000031;
KW   Q3TCP5_MOUSE; Q3UL48_MOUSE; Q3UXR4_MOUSE; Q4KML7_MOUSE; Q8CBU4_MOUSE;
KW   AK035271; AK135194; AK135353; AK145707; AK159717; AK159824; AK166191;
KW   AK170610; AK172336; BC048181; BC098502; CH466692; X60671;
KW   Acetylation; Cell membrane; Cell projection; Cell shape;
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 EELIQDITQK LFFLQVKDGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR
     GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDYEQKTKR
     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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