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0RADI_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRDX
DescriptionRadixin.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The ERM family consists of three closely-related proteins.zrin.adixin and moesin .Ezrin was first identified as a constituent of microvilli .adixin as a barbed.nd-capping actin-modulating protein from isolated junctional fractions .nd moesin as a heparinbinding protein . A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2)is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein).ERM molecules contain 3 domains.n N-terminal globular domain; an extended alpha-helical domain; and acharged C-terminal domain . Ezrin.adixin and merlin also contain a polyproline region betweenthe helical and C-terminal domains. The N-terminal domain is highly conserved.nd is also found in merlin.and 4.1 proteins and members of the band 4.1 superfamily. ERM proteins crosslink actin filaments withplasma membranes. They co-localise with CD44 at actin filament-plasma membrane interaction sites.ssociating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains.
  IPR011259:Ezrin/radixin/moesin, C-terminal
This domain is found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. It is a conserved N-terminal domain of about 150 residues .nvolved in the linkage of cytoplasmic proteins to the membrane.
  IPR000299:Band 4.1
The ERM family consists of three closely-related proteins.zrin.adixin and moesin .Ezrin was first identified as a constituent of microvilli .adixin as a barbed.nd-capping actin-modulating protein from isolated junctional fractions .nd moesin as a heparinbinding protein . A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2)is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein).ERM molecules contain 3 domains.n N-terminal globular domain; an extended alpha-helical domain; and acharged C-terminal domain . Ezrin.adixin and merlin also contain a polyproline region betweenthe helical and C-terminal domains. The N-terminal domain is highly conserved.nd is also found in merlin.and 4.1 proteins and members of the band 4.1 superfamily. ERM proteins crosslink actin filaments withplasma membranes. They co-localise with CD44 at actin filament-plasma membrane interaction sites.ssociating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains.
  IPR000798:Ezrin/radixin/moesin ERM
ERM proteins.ighly related members of the larger protein 4.1 superfamily.an exist in an active or inactive conformation. The sole Drosophila ERM protein.oesin.unctions to promote cortical actin assembly and apical-basal polarity. As a result.ells lacking Moesin lose epithelial characteristics and adopt invasive migratory behaviour. Moesin appears to facilitate epithelial morphology not by providing an essential structural function.ut rather by antagonizing activity of the small GTPase Rho. Thus.oesin functions in maintaining epithelial integrity by regulating cell-signalling events that affect actin organization and polarity .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008954:Moesin
FERM domains (band F ezrin-radixin-moesin homology domains) are a common membrane-binding module involved in localising proteins to the plasma membrane . Proteins containing a FERM domain include cytoskeletal proteins such as erythrocyte membrane protein 4.1R.alin.nd the ezrin-radixin-moesin protein family.s well as several protein tyrosine kinases and phosphatases.nd the neurofibromatosis 2 tumour suppressor protein merlin. The ezrin-radixin-moesin protein family function to crosslink the actin filaments of cytoskeletal structures to the plasma membrane.
  IPR009065:FERM
This group represents an ezrin/radixin/moesin. The ERM family consists of three closely-related proteins.zrin.adixin and moesin .Ezrin was first identified as a constituent of microvilli .adixin as a barbed.nd-capping actin-modulating protein from isolated junctional fractions .nd moesin as a heparinbinding protein . A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2)is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein).ERM molecules contain 3 domains.n N-terminal globular domain; an extended alpha-helical domain; and acharged C-terminal domain . Ezrin.adixin and merlin also contain a polyproline region betweenthe helical and C-terminal domains. The N-terminal domain is highly conserved.nd is also found in merlin.and 4.1 proteins and members of the band 4.1 superfamily. ERM proteins crosslink actin filaments withplasma membranes. They co-localise with CD44 at actin filament-plasma membrane interaction sites.ssociating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains.
  IPR011174:Ezrin/radixin/moesin
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR011259:ERM 
Evalue:-246.568634033203 
Location:210-583IPR000299:Band_41 
Evalue:-130.958602905273 
Location:7-206
SequencesProtein: RADI_HUMAN (583 aa)
mRNA: NM_002906
Local Annotation
Synapse Ontology
actin exists in two states within the cell: as polymerized two-stranded helical filaments (F-actin) or as monomers (Gactin), which provide the building blocks for filament assembly.
sdb:0283 G-actin  (Evidence:keywords)
KO assignmentK05762
  Level 3 annotation:
    radixin
  Level 2 annotation:
    Regulation of actin cytoskeleton
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 865 residues, 109605375-109607968Exon2: 83 residues, 109609171-109609414Exon3: 33 residues, 109612033-109612126Exon4: 55 residues, 109613426-109613587Exon5: 45 residues, 109623637-109623768Exon6: 56 residues, 109629880-109630044Exon7: 34 residues, 109631223-109631320Exon8: 51 residues, 109633701-109633848Exon9: 30 residues, 109634040-109634124Exon10: 93 residues, 109639894-109640169Exon11: 34 residues, 109640713-109640809Exon12: 30 residues, 109648470-109648554Exon13: 27 residues, 109655615-109655691Exon14: 84 residues, 109672401-109672647Exon15: 2 residues, -Jump to RADI_HUMAN  
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Loci Cluster (Details)Loci: 2702 109805803-109840814 ~-35K 7711(FDX1)(+)Loci: 3989 109605375-109672647 ~-67K 7709(RDX)(-)Link out to UCSC