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Database: UniProt
Entry: W5PUV9_SHEEP
LinkDB: W5PUV9_SHEEP
Original site: W5PUV9_SHEEP 
ID   W5PUV9_SHEEP            Unreviewed;       581 AA.
AC   W5PUV9; A0A6P3YQC6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Radixin {ECO:0000256|ARBA:ARBA00040460};
GN   Name=RDX {ECO:0000313|Ensembl:ENSOARP00000014241.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000014241.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000014241.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000014241.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000014241.1}
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: Cell projection, microvillus
CC       {ECO:0000256|ARBA:ARBA00004105}. 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; AMGL01031135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01031136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01031137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01031138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_011950811.1; XM_012095421.2.
DR   RefSeq; XP_014956389.1; XM_015100903.1.
DR   AlphaFoldDB; W5PUV9; -.
DR   Ensembl; ENSOART00000014448.1; ENSOARP00000014241.1; ENSOARG00000013286.1.
DR   GeneID; 101106875; -.
DR   KEGG; oas:101106875; -.
DR   CTD; 5962; -.
DR   HOGENOM; CLU_003623_6_2_1; -.
DR   OrthoDB; 5476297at2759; -.
DR   Proteomes; UP000002356; Chromosome 15.
DR   Bgee; ENSOARG00000013286; Expressed in skeletal muscle tissue of biceps brachii and 55 other cell types or tissues.
DR   ExpressionAtlas; W5PUV9; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005902; C:microvillus; 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; 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   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:UP000002356}.
FT   DOMAIN          5..295
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
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         278
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   581 AA;  68402 MW;  A700383280F6A387 CRC64;
     MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK
     LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE
     TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR
     GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LRQIEEQTMK
     AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SALAKQAADQ MKNQEQLAAE
     LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPVIPPT
     ENEHDEHDEN NAEASAELSN DGVMNHRSEE ERVTETQKNE RVKKQLQALS SELAQARDET
     KKTQNDVLHA ENVKAGRDKY KTLRQIRQGN TKQRIDEFEA M
//
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