ID:RADI_HUMAN DESCRIPTION: RecName: Full=Radixin; FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. ENZYME REGULATION: A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding (By similarity). SUBUNIT: Binds SLC9A3R1. Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively. DOMAIN: The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C- terminal domains inhibits its ablilty to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN (By similarity). PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). DISEASE: Defects in RDX are the cause of deafness autosomal recessive type 24 (DFNB24) [MIM:611022]. DFNB24 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. SIMILARITY: Contains 1 FERM domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF00373 - FERM central domain PF00769 - Ezrin/radixin/moesin family PF09379 - FERM N-terminal domain PF09380 - FERM C-terminal PH-like domain
SCOP Domains: 47031 - Second domain of FERM 48678 - Moesin tail domain 101278 - N-terminal domain of adenylylcyclase associated protein, CAP 50729 - PH domain-like 54236 - Ubiquitin-like
ModBase Predicted Comparative 3D Structure on P35241
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0008360 regulation of cell shape GO:0008361 regulation of cell size GO:0010628 positive regulation of gene expression GO:0010737 protein kinase A signaling GO:0030033 microvillus assembly GO:0030335 positive regulation of cell migration GO:0032231 regulation of actin filament bundle assembly GO:0032487 regulation of Rap protein signal transduction GO:0034111 negative regulation of homotypic cell-cell adhesion GO:0034260 negative regulation of GTPase activity GO:0036120 cellular response to platelet-derived growth factor stimulus GO:0043087 regulation of GTPase activity GO:0045176 apical protein localization GO:0045184 establishment of protein localization GO:0045792 negative regulation of cell size GO:0051016 barbed-end actin filament capping GO:0051693 actin filament capping GO:0061028 establishment of endothelial barrier GO:0072659 protein localization to plasma membrane GO:0097067 cellular response to thyroid hormone stimulus GO:1900027 regulation of ruffle assembly GO:1900087 positive regulation of G1/S transition of mitotic cell cycle GO:1902115 regulation of organelle assembly GO:1902966 positive regulation of protein localization to early endosome GO:1903364 positive regulation of cellular protein catabolic process GO:1903392 negative regulation of adherens junction organization GO:2000643 positive regulation of early endosome to late endosome transport