ID RADI_CHICK Reviewed; 583 AA. AC Q9PU45; DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 08-NOV-2023, entry version 124. DE RecName: Full=Radixin; GN Name=RDX; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10760599; DOI=10.1016/s0167-4781(00)00060-9; RA Li W., Crouch D.H.; RT "Cloning and expression profile of chicken radixin."; RL Biochim. Biophys. Acta 1491:327-332(2000). CC -!- FUNCTION: Probably plays a crucial role in the binding of the barbed CC end of actin filaments to the plasma membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ249838; CAB59977.1; -; mRNA. DR RefSeq; NP_990082.1; NM_204751.1. DR AlphaFoldDB; Q9PU45; -. DR SMR; Q9PU45; -. DR IntAct; Q9PU45; 1. DR STRING; 9031.ENSGALP00000021028; -. DR PaxDb; 9031-ENSGALP00000021028; -. DR GeneID; 395511; -. DR KEGG; gga:395511; -. DR CTD; 5962; -. DR VEuPathDB; HostDB:geneid_395511; -. DR eggNOG; KOG3529; Eukaryota. DR InParanoid; Q9PU45; -. DR PhylomeDB; Q9PU45; -. DR PRO; PR:Q9PU45; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0030175; C:filopodium; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0003779; F:actin binding; IBA:GO_Central. DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central. DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central. DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13194; FERM_C_ERM; 1. DR CDD; cd17187; FERM_F1_ERM; 1. DR Gene3D; 1.20.5.450; -; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 6.10.360.10; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR011174; ERM. DR InterPro; IPR011259; ERM_C_dom. DR InterPro; IPR041789; ERM_FERM_C. DR InterPro; IPR046810; ERM_helical. DR InterPro; IPR000798; Ez/rad/moesin-like. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. 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_tail_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 1. DR PANTHER; PTHR23281:SF14; RADIXIN; 1. DR Pfam; PF00769; ERM_C; 1. DR Pfam; PF20492; ERM_helical; 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 SMART; SM01196; FERM_C; 1. DR SUPFAM; SSF48678; Moesin tail domain; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. PE 2: Evidence at transcript level; KW Actin capping; Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; KW Membrane; Reference proteome. FT CHAIN 1..583 FT /note="Radixin" FT /id="PRO_0000219424" FT DOMAIN 5..295 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT REGION 310..336 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 436..527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..464 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 467..481 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..496 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..524 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 60..63 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000250" SQ SEQUENCE 583 AA; 68555 MW; BE25634F4798CBE0 CRC64; MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK LNKKVTQQDV RKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE TAVLLASYAV QSKYGDYNKE IHKLGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LRQIEEQTMK AQKELEEQTR RALELDQERK RAKEEAERLE KERRAAEEAK AALAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EASEWQHKAF AAQEDLEKTK EELKSVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL SSDGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL HAENVKAGRG KYKTLRQIRQ GNTKQRIDEF EAM //