ID A0A2K5YXP6_MANLE Unreviewed; 395 AA.
AC A0A2K5YXP6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Radixin {ECO:0000256|ARBA:ARBA00040460};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000020328.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000020328.1}
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 AlphaFoldDB; A0A2K5YXP6; -.
DR Ensembl; ENSMLET00000043825.1; ENSMLEP00000020328.1; ENSMLEG00000034238.1.
DR GeneTree; ENSGT01090000260082; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0042995; C:cell projection; 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 CDD; cd17187; FERM_F1_ERM; 1.
DR Gene3D; 1.20.5.450; -; 1.
DR Gene3D; 1.20.80.10; -; 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; 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; 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; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 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 4: Predicted;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 10..300
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT COILED 163..190
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 307..369
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 395 AA; 47392 MW; 5CEB51E7E694B9A7 CRC64;
MIRLPQPPKI NVRVTTMDAE LEFAIQPNTT GKQLFDQVVK TVGLREVWFF GLQYVDSKGY
STWLKLNKKV TQQDVKKENP LQFKFRAKFF PEDVSEELIQ EITQRLFFLQ VKEAILNDEI
YCPPETAVLL ASYAVQAKYG DYNKEIHKPG YLANDRLLPQ RVLEQHKLTK EQWEERIQNW
HEEHRGMLRE DSMMEYLKIA QDLEMYGVNY FEIKNKKGTE LWLGVDALGL NIYEHDDKLT
PKIGFPWSEI RNISFNDKKF VIKPIDKKAP DFVFYAPRLR INKRILALCM GNHELYMRRR
KPDTIEVQQM KAQAREEKHQ KQLERAQLEN EKKKREIAEK EKERIEREKE ELMERLKQIE
EQTIKAQKGY IIKMLMIYKL RSTREYKEER VEERI
//