ID A0A2K6DSN9_MACNE Unreviewed; 447 AA.
AC A0A2K6DSN9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Radixin {ECO:0000256|ARBA:ARBA00040460};
GN Name=RDX {ECO:0000313|Ensembl:ENSMNEP00000038887.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000038887.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000038887.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011759762.1; XM_011761460.1.
DR AlphaFoldDB; A0A2K6DSN9; -.
DR Ensembl; ENSMNET00000063370.1; ENSMNEP00000038887.1; ENSMNEG00000042245.1.
DR GeneID; 105493642; -.
DR CTD; 5962; -.
DR GeneTree; ENSGT01090000260082; -.
DR OrthoDB; 5476297at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000042245; Expressed in lung and 12 other cell types or tissues.
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:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_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; 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; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
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 PRINTS; PR00661; ERMFAMILY.
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 PROSITE; PS00661; FERM_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 1..159
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 174..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 240..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 52665 MW; 5CF1565C3C75AA27 CRC64;
MLSWNLPFSP IQLANNFLTS VLEQHKLTKE QWEERIQNWH EEHRGMLRED SMMEYLKIAQ
DLEMYGVNYF EIKNKKGTEL WLGVDALGLN IYEHDDKLTP KIGFPWSEIR NISFNDKKFV
IKPIDKKAPD FVFYAPRLRI NKRILALCMG NHELYMRRRK PDTIEVQQMK AQAREEKHQK
QLERAQLENE KKKREIAEKE KERIEREKEE LMERLKQIEE QTVKAQKELE EQTRKALELD
QERKRAKEEA ERLEKERRAA EEAKSAIAKQ AADQMKNQEQ LAAELAEFTA KIALLEEAKK
KKEEEATEWQ HKAFAAQEDL EKTKEELKTV MSAPPPPPPP PVIPPTENEH DEHDENNAEA
SAELSNEGVM NHRSEEERVT ETQKNERVKK QLQALSSELA QARDETKKTQ NDVLHAENVK
AGRDKYKTLR QIRQGNTKQR IDEFEAM
//
