ID A0A452J0U3_9SAUR Unreviewed; 586 AA.
AC A0A452J0U3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Radixin {ECO:0000256|ARBA:ARBA00040460};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000033982.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000033982.1}
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 STRING; 38772.ENSGAGP00000033987; -.
DR Ensembl; ENSGAGT00000038482.1; ENSGAGP00000033982.1; ENSGAGG00000024159.1.
DR Ensembl; ENSGAGT00000038487.1; ENSGAGP00000033987.1; ENSGAGG00000024159.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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 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; SSF101447; Formin homology 2 domain (FH2 domain); 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 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:UP000291020}.
FT DOMAIN 5..295
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 310..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..185
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 373..400
FT /note="Basic and acidic residues"
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..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
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 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 586 AA; 68858 MW; FEC0388CD268E8CD CRC64;
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK
LNKKVTQQDV RKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE
TAVLLASYAV QAKYGDYNKE IHKLGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR
GMLREDSVME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LRQIEEQTMK
AQKELEEQTR KALELDQERK RAKEEAERLE KDRRAAEEAK AALAKQAADQ MKNQEQLAAE
LAEFTAKIAL LEEAKKKKEE EASEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPPPP
VIPPTENEHD EHDENNAEAS AELSSDGVMN HRSEEERVTE TQKNERVKKQ LQTLSSELAQ
ARDETKKTQN DVLHAENVKA GRDKYKTLRQ IRQGNTKQRI DEFEAM
//
