(data stored in ACNUC9306 zone)

HOGENOM: HS6_PE4147

ID   HS6_PE4147                           STANDARD;      PRT;   586 AA.
AC   HS6_PE4147; P15311; E1P5A8; P23714; Q4VX75; Q96CU8; Q9NSJ4;
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; (HS6.PE4147).
GN   Name=EZR; Synonyms=VIL2;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS6.PE4147.
CC       Homo sapiens chromosome 6 GRCh37  sequence 1..171055067 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:EZRI_HUMAN
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.
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 MPP5 and SLC9A3R2. Found in a complex with
CC       EZR, PODXL and SLC9A3R2 (By similarity). Interacts with MCC,
CC       PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when
CC       phosphorylated) with FES/FPS.
CC   -!- INTERACTION:
CC       Q00987:MDM2; NbExp=3; IntAct=EBI-1056902, EBI-389668;
CC       Q8IZE3:SCYL3; NbExp=4; IntAct=EBI-1056902, EBI-1380680;
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       Microvillar peripheral membrane protein (cytoplasmic side).
CC   -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, basal ganglia,
CC       hippocampus, hypophysis, and optic nerve. Weakly expressed in
CC       brain stem and diencephalon. Stronger expression was detected in
CC       gray matter of frontal lobe compared to white matter (at protein
CC       level). Component of the microvilli of intestinal epithelial
CC       cells. Preferentially expressed in astrocytes of hippocampus,
CC       frontal cortex, thalamus, parahippocampal cortex, amygdala,
CC       insula, and corpus callosum. Not detected in neurons in most
CC       tissues studied.
CC   -!- DEVELOPMENTAL STAGE: Very strong staining is detected in the
CC       Purkinje cell layer and in part of the molecular layer of the
CC       infant brain compared to adult 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 (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA61278.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=CAB82418.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000092820;ENST00000337147;ENSP00000338934.
DR   EMBL; AF187552; - ;
DR   EMBL; AF188896; - ;
DR   EMBL; AF188897; - ;
DR   EMBL; AF189213; - ;
DR   EMBL; AF190059; - ;
DR   EMBL; AK296738; - ;
DR   EMBL; AK299456; - ;
DR   EMBL; AK312597; - ;
DR   EMBL; AK316031; - ;
DR   EMBL; AL162086; - ;
DR   EMBL; AL589931; - ;
DR   EMBL; BC013903; - ;
DR   EMBL; BC068458; - ;
DR   EMBL; J05021; - ;
DR   EMBL; X51521; - ;
DR   UniProtKB/Swiss-Prot; P15311; E1P5A8; P23714; Q4VX75; Q96CU8; Q9NSJ4; -.
DR   EMBL; X51521; CAA35893.1; -; mRNA.
DR   EMBL; J05021; AAA61278.1; ALT_INIT; mRNA.
DR   EMBL; AL162086; CAB82418.1; ALT_INIT; mRNA.
DR   EMBL; AL589931; CAI95307.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW47647.1; -; Genomic_DNA.
DR   EMBL; BC013903; AAH13903.1; -; mRNA.
DR   IPI; IPI00843975; -.
DR   PIR; A34400; A34400.
DR   RefSeq; NP_001104547.1; NM_001111077.1.
DR   RefSeq; NP_003370.2; NM_003379.4.
DR   UniGene; Hs.487027; -.
DR   PDB; 1NI2; X-ray; 2.30 A; A/B=2-297.
DR   PDBsum; 1NI2; -.
DR   ProteinModelPortal; P15311; -.
DR   SMR; P15311; 1-586.
DR   IntAct; P15311; 12.
DR   MINT; MINT-195721; -.
DR   STRING; P15311; -.
DR   PhosphoSite; P15311; -.
DR   SWISS-2DPAGE; P15311; -.
DR   DOSAC-COBS-2DPAGE; P15311; -.
DR   REPRODUCTION-2DPAGE; IPI00843975; -.
DR   PRIDE; P15311; -.
DR   Ensembl; ENST00000337147; ENSP00000338934; ENSG00000092820.
DR   Ensembl; ENST00000367075; ENSP00000356042; ENSG00000092820.
DR   GeneID; 7430; -.
DR   KEGG; hsa:7430; -.
DR   UCSC; uc003qrt.2; human.
DR   CTD; 7430; -.
DR   GeneCards; GC06M156657; -.
DR   H-InvDB; HIX0006334; -.
DR   HGNC; HGNC:12691; EZR.
DR   HPA; CAB004035; -.
DR   HPA; HPA021616; -.
DR   MIM; 123900; gene.
DR   neXtProt; NX_P15311; -.
DR   PharmGKB; PA162385512; -.
DR   eggNOG; prNOG04610; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   PhylomeDB; P15311; -.
DR   Pathway_Interaction_DB; syndecan_2_pathway; Syndecan-2-mediated signaling events.
DR   Reactome; REACT_18266; Axon guidance.
DR   NextBio; 29100; -.
DR   ArrayExpress; P15311; -.
DR   Bgee; P15311; -.
DR   CleanEx; HS_EZR; -.
DR   Genevestigator; P15311; -.
DR   GermOnline; ENSG00000092820; Homo sapiens.
DR   GO; GO:0005884; C:actin filament; IDA:HGNC.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030863; C:cortical cytoskeleton; TAS:HGNC.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0019898; C:extrinsic to membrane; IDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IEP:BHF-UCL.
DR   GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
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; HS6.PE4147; -.
KW   ENSG000000928201755old_1320000031; ENSP000003389347901old_1320000031;
KW   B2R6J2_HUMAN; B7Z437_HUMAN; B7Z5V2_HUMAN; B7Z9R6_HUMAN; Q6NUR7_HUMAN;
KW   Q9UJZ6_HUMAN; Q9UJZ7_HUMAN; Q9UJZ8_HUMAN; Q9UK20_HUMAN; AF187552;
KW   AF188897; AF189213; AF190059; AK296738; AK299456; AK312597; AK316031;
KW   AL589931; BC013903; BC068458; J05021; X51521;
KW   3D-structure; Acetylation; Cell membrane; Cell projection; Cell shape;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Membrane; Phosphoprotein; Polymorphism; Reference proteome.
SQ   SEQUENCE   586 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLHYV DNKGFPTWLK
     LDKKVSAQEV RKENPLQFKF RAKFYPEDVA EELIQDITQK LFFLQVKEGI LSDEIYCPPE
     TAVLLGSYAV QAKFGDYNKE VHKSGYLSSE RLIPQRVMDQ HKLTRDQWED RIQVWHAEHR
     GMLKDNAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM MREKEELMLR LQDYEEKTKK
     AERELSEQIQ RALQLEEERK RAQEEAERLE ADRMAALRAK EELERQAVDQ IKSQEQLAAE
     LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP
     VSYHVQESLQ DEGAEPTGYS AELSSEGIRD DRNEEKRITE AEKNERVQRQ LLTLSSELSQ
     ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAL
//

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