RADI_MOUSE
ID RADI_MOUSE Reviewed; 583 AA.
AC P26043; Q3TS85; Q9QW27;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Radixin;
DE AltName: Full=ESP10;
GN Name=Rdx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-53 AND 263-277.
RC TISSUE=Liver;
RX PubMed=1955455; DOI=10.1083/jcb.115.4.1039;
RA Funayama N., Nagafuchi A., Sato N., Tsukita S., Tsukita S.;
RT "Radixin is a novel member of the band 4.1 family.";
RL J. Cell Biol. 115:1039-1048(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC STRAIN=BALB/cJ; TISSUE=Keratinocyte;
RX PubMed=8479753;
RA Fazioli F., Wong W.T., Ullrich S.J., Sakaguchi K., Appella E.,
RA Di Fiore P.P.;
RT "The ezrin-like family of tyrosine kinase substrates: receptor-specific
RT pattern of tyrosine phosphorylation and relationship to malignant
RT transformation.";
RL Oncogene 8:1335-1345(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PROTEIN SEQUENCE OF 84-100, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION AT THR-564, AND ACTIVITY REGULATION.
RX PubMed=9456324; DOI=10.1083/jcb.140.3.647;
RA Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K.,
RA Tsukita S., Tsukita S.;
RT "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin
RT (ERM) proteins and regulates their head-to-tail association.";
RL J. Cell Biol. 140:647-657(1998).
RN [6]
RP INTERACTION WITH SPN/CD43 CYTOPLASMIC TAIL; CD44 AND ICAM2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9472040; DOI=10.1083/jcb.140.4.885;
RA Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S.,
RA Tsukita S.;
RT "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino
RT acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and
RT ICAM-2.";
RL J. Cell Biol. 140:885-895(1998).
RN [7]
RP INTERACTION WITH CPNE1 AND CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [8]
RP INTERACTION WITH LAYN.
RX PubMed=15913605; DOI=10.1016/j.yexcr.2005.04.017;
RA Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T.,
RA Hynes R.O.;
RT "Layilin, a cell surface hyaluronan receptor, interacts with merlin and
RT radixin.";
RL Exp. Cell Res. 308:177-187(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-297 IN COMPLEX WITH
RP INOSITOL-1,4,5-TRISPHOSPHATE.
RX PubMed=10970839; DOI=10.1093/emboj/19.17.4449;
RA Hamada K., Shimizu T., Matsui T., Tsukita S., Hakoshima T.;
RT "Structural basis of the membrane-targeting and unmasking mechanisms of the
RT radixin FERM domain.";
RL EMBO J. 19:4449-4462(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-310 IN COMPLEX WITH ICAM2.
RX PubMed=12554651; DOI=10.1093/emboj/cdg039;
RA Hamada K., Shimizu T., Yonemura S., Tsukita S., Tsukita S., Hakoshima T.;
RT "Structural basis of adhesion-molecule recognition by ERM proteins revealed
RT by the crystal structure of the radixin-ICAM-2 complex.";
RL EMBO J. 22:502-514(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-310.
RX PubMed=16582480; DOI=10.1107/s1744309106010062;
RA Kitano K., Yusa F., Hakoshima T.;
RT "Structure of dimerized radixin FERM domain suggests a novel masking motif
RT in C-terminal residues 295-304.";
RL Acta Crystallogr. F 62:340-345(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-310 IN COMPLEXES WITH NHERF1 AND
RP NHERF2.
RX PubMed=16615918; DOI=10.1016/j.str.2006.01.015;
RA Terawaki S., Maesaki R., Hakoshima T.;
RT "Structural basis for NHERF recognition by ERM proteins.";
RL Structure 14:777-789(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH MME/NEP.
RX PubMed=17459884; DOI=10.1074/jbc.m609232200;
RA Terawaki S., Kitano K., Hakoshima T.;
RT "Structural basis for type II membrane protein binding by ERM proteins
RT revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex.";
RL J. Biol. Chem. 282:19854-19862(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-310 IN COMPLEX WITH SPN/CD43
RP CYTOPLASMIC TAIL.
RX PubMed=18614175; DOI=10.1016/j.jmb.2008.05.085;
RA Takai Y., Kitano K., Terawaki S., Maesaki R., Hakoshima T.;
RT "Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its
RT binding to ERM proteins.";
RL J. Mol. Biol. 381:634-644(2008).
CC -!- FUNCTION: Probably plays a crucial role in the binding of the barbed
CC end of actin filaments to the plasma membrane.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA
CC domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts
CC with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2
CC (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts
CC with ICAM2 (PubMed:12554651, PubMed:9472040). Interacts (via FERM
CC domain) with SPN/CD43 cytoplasmic tail (PubMed:9472040,
CC PubMed:18614175). Interacts with CD44 (PubMed:9472040).
CC {ECO:0000250|UniProtKB:P35241, ECO:0000269|PubMed:12522145,
CC ECO:0000269|PubMed:12554651, ECO:0000269|PubMed:15913605,
CC ECO:0000269|PubMed:16615918, ECO:0000269|PubMed:17459884,
CC ECO:0000269|PubMed:18614175, ECO:0000269|PubMed:9472040}.
CC -!- INTERACTION:
CC P26043; P35330: Icam2; NbExp=2; IntAct=EBI-647737, EBI-1035485;
CC P26043; O14745: SLC9A3R1; Xeno; NbExp=2; IntAct=EBI-647737, EBI-349787;
CC P26043; Q15599: SLC9A3R2; Xeno; NbExp=2; IntAct=EBI-647737, EBI-1149760;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell
CC projection, microvillus {ECO:0000269|PubMed:9472040}. Note=Highly
CC concentrated in the undercoat of the cell-to-cell adherens junction and
CC the cleavage furrow in the interphase and mitotic phase, respectively.
CC -!- DOMAIN: The N-terminal domain interacts with the C-terminal domain of
CC LAYN. An interdomain interaction between its N-terminal and C-terminal
CC domains inhibits its ability to bind LAYN. In the presence of acidic
CC phospholipids, the interdomain interaction is inhibited and this
CC enhances binding to LAYN.
CC -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by
CC ROCK2 suppresses the head-to-tail association of the N-terminal and C-
CC terminal halves resulting in an opened conformation which is capable of
CC actin and membrane-binding. {ECO:0000269|PubMed:8479753,
CC ECO:0000269|PubMed:9456324}.
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DR EMBL; X60672; CAA43087.1; -; mRNA.
DR EMBL; AK162204; BAE36790.1; -; mRNA.
DR CCDS; CCDS40634.1; -.
DR PIR; A41129; A41129.
DR RefSeq; NP_001098086.1; NM_001104616.1.
DR RefSeq; NP_033067.2; NM_009041.3.
DR PDB; 1GC6; X-ray; 2.90 A; A=1-297.
DR PDB; 1GC7; X-ray; 2.80 A; A=1-297.
DR PDB; 1J19; X-ray; 2.40 A; A=1-310.
DR PDB; 2D10; X-ray; 2.50 A; A/B/C/D=1-310.
DR PDB; 2D11; X-ray; 2.81 A; A/B/C/D=1-310.
DR PDB; 2D2Q; X-ray; 2.80 A; A/B=1-310.
DR PDB; 2EMS; X-ray; 2.90 A; A=1-310.
DR PDB; 2EMT; X-ray; 2.80 A; A/B=1-310.
DR PDB; 2YVC; X-ray; 3.20 A; A/B/C=1-310.
DR PDB; 2ZPY; X-ray; 2.10 A; A=1-310.
DR PDB; 3X23; X-ray; 2.40 A; A=1-310.
DR PDBsum; 1GC6; -.
DR PDBsum; 1GC7; -.
DR PDBsum; 1J19; -.
DR PDBsum; 2D10; -.
DR PDBsum; 2D11; -.
DR PDBsum; 2D2Q; -.
DR PDBsum; 2EMS; -.
DR PDBsum; 2EMT; -.
DR PDBsum; 2YVC; -.
DR PDBsum; 2ZPY; -.
DR PDBsum; 3X23; -.
DR AlphaFoldDB; P26043; -.
DR SMR; P26043; -.
DR BioGRID; 202845; 11.
DR DIP; DIP-29091N; -.
DR IntAct; P26043; 10.
DR MINT; P26043; -.
DR STRING; 10090.ENSMUSP00000000590; -.
DR iPTMnet; P26043; -.
DR PhosphoSitePlus; P26043; -.
DR SwissPalm; P26043; -.
DR REPRODUCTION-2DPAGE; P26043; -.
DR CPTAC; non-CPTAC-3858; -.
DR EPD; P26043; -.
DR jPOST; P26043; -.
DR MaxQB; P26043; -.
DR PaxDb; P26043; -.
DR PeptideAtlas; P26043; -.
DR PRIDE; P26043; -.
DR ProteomicsDB; 255030; -.
DR Antibodypedia; 633; 456 antibodies from 39 providers.
DR DNASU; 19684; -.
DR Ensembl; ENSMUST00000000590; ENSMUSP00000000590; ENSMUSG00000032050.
DR Ensembl; ENSMUST00000163153; ENSMUSP00000128249; ENSMUSG00000032050.
DR GeneID; 19684; -.
DR KEGG; mmu:19684; -.
DR UCSC; uc009plq.2; mouse.
DR CTD; 5962; -.
DR MGI; MGI:97887; Rdx.
DR VEuPathDB; HostDB:ENSMUSG00000032050; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; P26043; -.
DR OMA; SREDSMM; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P26043; -.
DR TreeFam; TF313935; -.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR BioGRID-ORCS; 19684; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rdx; mouse.
DR EvolutionaryTrace; P26043; -.
DR PRO; PR:P26043; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P26043; protein.
DR Bgee; ENSMUSG00000032050; Expressed in primary oocyte and 271 other tissues.
DR ExpressionAtlas; P26043; baseline and differential.
DR Genevisible; P26043; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IMP:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0030033; P:microvillus assembly; IMP:MGI.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; ISO:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032231; P:regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0008361; P:regulation of cell size; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:MGI.
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 IDEAL; IID50114; -.
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 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..583
FT /note="Radixin"
FT /id="PRO_0000219422"
FT DOMAIN 5..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Pro 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 COMPBIAS 537..555
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 BINDING 278
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 564
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:9456324"
FT CONFLICT 312..313
FT /note="EK -> VL (in Ref. 1; CAA43087)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="R -> W (in Ref. 1; CAA43087)"
FT /evidence="ECO:0000305"
FT CONFLICT 575..576
FT /note="QR -> HA (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:2ZPY"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2ZPY"
FT TURN 144..149
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:2ZPY"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:2ZPY"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:2ZPY"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 274..293
FT /evidence="ECO:0007829|PDB:2ZPY"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:1J19"
SQ SEQUENCE 583 AA; 68543 MW; 25752653017F0879 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 LRQIEEQTVK
AQKELEEQTR KALELEQERQ RAKEEAERLD RERRAAEEAK SAIAKQAADQ MKNQEQLAAE
LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP
PTENEHDEQD ENSAEASAEL SSEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD
ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
