RADI_CHICK
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 03-AUG-2022, entry version 120.
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}.
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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; Q9PU45; -.
DR PRIDE; Q9PU45; -.
DR GeneID; 395511; -.
DR KEGG; gga:395511; -.
DR CTD; 5962; -.
DR VEuPathDB; HostDB:geneid_395511; -.
DR eggNOG; KOG3529; Eukaryota.
DR InParanoid; Q9PU45; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; Q9PU45; -.
DR PRO; PR:Q9PU45; -.
DR Proteomes; UP000000539; Unplaced.
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 Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
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; PTHR23281; 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 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
