ID A0A0D9S2M1_CHLSB Unreviewed; 605 AA.
AC A0A0D9S2M1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Radixin {ECO:0000256|ARBA:ARBA00040460};
GN Name=RDX {ECO:0000313|Ensembl:ENSCSAP00000015110.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000015110.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000015110.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000015110.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Probably plays a crucial role in the binding of the barbed
CC end of actin filaments to the plasma membrane.
CC {ECO:0000256|ARBA:ARBA00037725}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; AQIB01092653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01092654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01092655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01092656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9S2M1; -.
DR STRING; 60711.ENSCSAP00000015110; -.
DR Ensembl; ENSCSAT00000000956.1; ENSCSAP00000015110.1; ENSCSAG00000002938.1.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01090000260082; -.
DR OMA; WADHKNT; -.
DR Proteomes; UP000029965; Chromosome 1.
DR Bgee; ENSCSAG00000002938; Expressed in adrenal cortex and 7 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; IEA:Ensembl.
DR GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
DR GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0032231; P:regulation of actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:1902115; P:regulation of organelle assembly; IEA:Ensembl.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
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; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 5..296
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 377..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..525
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:0000256|PIRSR:PIRSR002305-1"
FT BINDING 279
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
SQ SEQUENCE 605 AA; 71142 MW; 00EF15D465719C06 CRC64;
FLLQINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK
LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE
TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR
GMLSREDSMM EYLKIAQDLE MYGVNYFEIK NKKGTELWLG VDALGLNIYE HDDKLTPKIG
FPWSEIRNIS FNDKKFVIKP IDKKAPDFVF YAPRLRINKG ILALYMGNYE LYMQRRKPDT
IKVQQMKAQA REEKHQKQLE RAQLENEKKK REIAEKEKER IEREKEELME RLKQIEEQTI
KAQKELEEQT RKALELDQER KRAKEEAERL EKERRAAEEA KSAIAKQAAD QMKNQEQLAA
ELAEFTAKIA LLEEAKKKKE EEATEWQHKA FAAQEDLEKT KEELKTVMSA PPPPPPPPVI
PPTENEHDEH DENNAEASAE LSNEGVMNHR SEEERVTETQ KNERVKKQLQ ALSSELAQAR
DETKKTQNDV LHAENVKAGR DKYKTLRQIR QGNTKQRIDE FEAMWGPKLY ALFQMRSCQS
SIKQM
//
