(data stored in ACNUC9306 zone)

SWISSPROT: RADI_HUMAN

ID   RADI_HUMAN              Reviewed;         583 AA.
AC   P35241; A7YIJ8; A7YIK0; A7YIK3; B7Z9U6; F5H1A7; Q86Y61;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   11-DEC-2019, entry version 190.
DE   RecName: Full=Radixin;
GN   Name=RDX;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=8486357; DOI=10.1006/geno.1993.1159;
RA   Wilgenbus K.K., Milatovich A., Francke U., Furthmayr H.;
RT   "Molecular cloning, cDNA sequence, and chromosomal assignment of the human
RT   radixin gene and two dispersed pseudogenes.";
RL   Genomics 16:199-206(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT DFNB24
RP   ASN-578.
RC   TISSUE=Retina;
RX   PubMed=17226784; DOI=10.1002/humu.20469;
RA   Khan S.Y., Ahmed Z.M., Shabbir M.I., Kitajiri S., Kalsoom S., Tasneem S.,
RA   Shayiq S., Ramesh A., Srisailpathy S., Khan S.N., Smith R.J.H.,
RA   Riazuddin S., Friedman T.B., Riazuddin S.;
RT   "Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24
RT   locus.";
RL   Hum. Mutat. 28:417-423(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-328.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH SLC9A3R1.
RX   PubMed=9430655; DOI=10.1074/jbc.273.3.1273;
RA   Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C.,
RA   Solomon F., Gusella J., Ramesh V.;
RT   "NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common
RT   interactor for merlin and ERM (MERM) proteins.";
RL   J. Biol. Chem. 273:1273-1276(1998).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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: Binds SLC9A3R1 (PubMed:9430655). Interacts with NHERF1,
CC       NHERF2, LAYN, MME/NEP and ICAM2. Interacts with CPNE1 (via VWFA domain)
CC       and CPNE4 (via VWFA domain). Interacts with SPN and CD44 (By
CC       similarity). {ECO:0000250|UniProtKB:P26043,
CC       ECO:0000269|PubMed:9430655}.
CC   -!- INTERACTION:
CC       P15311:EZR; NbExp=6; IntAct=EBI-2514878, EBI-1056902;
CC       P05107:ITGB2; NbExp=2; IntAct=EBI-2514878, EBI-300173;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell
CC       projection, microvillus {ECO:0000250|UniProtKB:P26043}. 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P35241-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35241-2; Sequence=VSP_045315, VSP_045318;
CC       Name=3;
CC         IsoId=P35241-3; Sequence=VSP_045316, VSP_045317, VSP_045318;
CC       Name=4;
CC         IsoId=P35241-4; Sequence=VSP_047276;
CC       Name=5;
CC         IsoId=P35241-5; Sequence=VSP_045318;
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Deafness, autosomal recessive, 24 (DFNB24) [MIM:611022]: A
CC       form of non-syndromic sensorineural hearing loss. Sensorineural
CC       deafness results from damage to the neural receptors of the inner ear,
CC       the nerve pathways to the brain, or the area of the brain that receives
CC       sound information. {ECO:0000269|PubMed:17226784}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
DR   EMBL; L02320; AAA36541.1; -; mRNA.
DR   EMBL; AK316061; BAH14432.1; -; mRNA.
DR   EMBL; DQ916738; ABI34710.1; -; mRNA.
DR   EMBL; DQ916739; ABI34711.1; -; mRNA.
DR   EMBL; DQ916741; ABI34713.1; -; mRNA.
DR   EMBL; DQ916742; ABI34714.1; -; mRNA.
DR   EMBL; DQ916740; ABI34712.1; -; mRNA.
DR   EMBL; AP000901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67129.1; -; Genomic_DNA.
DR   EMBL; BC047109; AAH47109.1; -; mRNA.
DR   CCDS; CCDS58171.1; -. [P35241-2]
DR   CCDS; CCDS58172.1; -. [P35241-4]
DR   CCDS; CCDS58173.1; -. [P35241-3]
DR   CCDS; CCDS58174.1; -. [P35241-5]
DR   CCDS; CCDS8343.1; -. [P35241-1]
DR   PIR; A46127; A46127.
DR   RefSeq; NP_001247421.1; NM_001260492.1. [P35241-5]
DR   RefSeq; NP_001247422.1; NM_001260493.1. [P35241-5]
DR   RefSeq; NP_001247423.1; NM_001260494.1. [P35241-4]
DR   RefSeq; NP_001247424.1; NM_001260495.1. [P35241-2]
DR   RefSeq; NP_001247425.1; NM_001260496.1. [P35241-3]
DR   RefSeq; NP_002897.1; NM_002906.3. [P35241-1]
DR   SMR; P35241; -.
DR   BioGrid; 111894; 83.
DR   IntAct; P35241; 18.
DR   MINT; P35241; -.
DR   STRING; 9606.ENSP00000384136; -.
DR   DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate.
DR   iPTMnet; P35241; -.
DR   PhosphoSitePlus; P35241; -.
DR   SwissPalm; P35241; -.
DR   BioMuta; RDX; -.
DR   DMDM; 464541; -.
DR   EPD; P35241; -.
DR   jPOST; P35241; -.
DR   MassIVE; P35241; -.
DR   MaxQB; P35241; -.
DR   PaxDb; P35241; -.
DR   PeptideAtlas; P35241; -.
DR   PRIDE; P35241; -.
DR   ProteomicsDB; 1819; -.
DR   ProteomicsDB; 1820; -.
DR   ProteomicsDB; 1821; -.
DR   ProteomicsDB; 25595; -.
DR   ProteomicsDB; 55009; -. [P35241-1]
DR   Ensembl; ENST00000528498; ENSP00000432112; ENSG00000137710. [P35241-5]
DR   Ensembl; ENST00000528900; ENSP00000433580; ENSG00000137710. [P35241-2]
DR   Ensembl; ENST00000530301; ENSP00000436277; ENSG00000137710. [P35241-3]
DR   Ensembl; ENST00000530749; ENSP00000437301; ENSG00000137710. [P35241-5]
DR   Ensembl; ENST00000544551; ENSP00000445826; ENSG00000137710. [P35241-4]
DR   Ensembl; ENST00000645495; ENSP00000496503; ENSG00000137710. [P35241-1]
DR   Ensembl; ENST00000647231; ENSP00000496414; ENSG00000137710. [P35241-5]
DR   GeneID; 5962; -.
DR   KEGG; hsa:5962; -.
DR   UCSC; uc001pku.4; human. [P35241-1]
DR   CTD; 5962; -.
DR   DisGeNET; 5962; -.
DR   EuPathDB; HostDB:ENSG00000137710.14; -.
DR   GeneCards; RDX; -.
DR   GeneReviews; RDX; -.
DR   HGNC; HGNC:9944; RDX.
DR   HPA; CAB037312; -.
DR   HPA; HPA000263; -.
DR   HPA; HPA000763; -.
DR   MalaCards; RDX; -.
DR   MIM; 179410; gene.
DR   MIM; 611022; phenotype.
DR   neXtProt; NX_P35241; -.
DR   OpenTargets; ENSG00000137710; -.
DR   Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR   PharmGKB; PA34311; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   eggNOG; ENOG410XQFP; LUCA.
DR   GeneTree; ENSGT00960000186596; -.
DR   HOGENOM; HOG000007113; -.
DR   InParanoid; P35241; -.
DR   KO; K05762; -.
DR   OMA; EWERRIM; -.
DR   OrthoDB; 627741at2759; -.
DR   PhylomeDB; P35241; -.
DR   TreeFam; TF313935; -.
DR   Reactome; R-HSA-437239; Recycling pathway of L1.
DR   SIGNOR; P35241; -.
DR   ChiTaRS; RDX; human.
DR   GeneWiki; Radixin; -.
DR   GenomeRNAi; 5962; -.
DR   Pharos; P35241; Tbio.
DR   PRO; PR:P35241; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P35241; protein.
DR   Bgee; ENSG00000137710; Expressed in 239 organ(s), highest expression level in metanephros.
DR   ExpressionAtlas; P35241; baseline and differential.
DR   Genevisible; P35241; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR   GO; GO:0051286; C:cell tip; IEA:Ensembl.
DR   GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR   GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0051018; F:protein kinase A binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IGI:UniProtKB.
DR   GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR   GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR   GO; GO:1903392; P:negative regulation of adherens junction organization; IMP:UniProtKB.
DR   GO; GO:0045792; P:negative regulation of cell size; IMP:UniProtKB.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IGI:UniProtKB.
DR   GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IGI:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR   GO; GO:1902966; P:positive regulation of protein localization to early endosome; IGI:UniProtKB.
DR   GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR   GO; GO:0032231; P:regulation of actin filament bundle assembly; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; IGI:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IGI:UniProtKB.
DR   GO; GO:1902115; P:regulation of organelle assembly; IGI:UniProtKB.
DR   GO; GO:0032487; P:regulation of Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:1900027; P:regulation of ruffle assembly; IMP:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.1020; -; 1.
DR   Gene3D; 2.30.29.30; -; 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; 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   Pfam; PF00769; ERM; 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;
DR   PRODOM; P35241.
DR   SWISS-2DPAGE; P35241.
KW   Actin capping; Actin-binding; Alternative splicing; Cell membrane;
KW   Cell projection; Cytoplasm; Cytoskeleton; Deafness; Disease mutation;
KW   Membrane; Non-syndromic deafness; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN           1..583
FT                   /note="Radixin"
FT                   /id="PRO_0000219421"
FT   DOMAIN          5..295
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          60..63
FT                   /note="Phosphatidylinositol binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        311..522
FT                   /note="Glu-rich"
FT   COMPBIAS        470..477
FT                   /note="Poly-Pro"
FT   BINDING         278
FT                   /note="Phosphatidylinositol"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26043"
FT   MOD_RES         564
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000250|UniProtKB:P26043"
FT   VAR_SEQ         1..347
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17226784"
FT                   /id="VSP_045315"
FT   VAR_SEQ         1..156
FT                   /note="MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDS
FT                   KGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAIL
FT                   NDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQR -> MLSWNLPFSP
FT                   IQLANNFLTS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047276"
FT   VAR_SEQ         33..64
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17226784"
FT                   /id="VSP_045316"
FT   VAR_SEQ         168..539
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17226784"
FT                   /id="VSP_045317"
FT   VAR_SEQ         583
FT                   /note="M -> MWGPKLYALFQMRSCQSSIKQM (in isoform 2, isoform 3
FT                   and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17226784"
FT                   /id="VSP_045318"
FT   VARIANT         328
FT                   /note="K -> E (in dbSNP:rs17854427)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_036857"
FT   VARIANT         490
FT                   /note="D -> N (in dbSNP:rs34471100)"
FT                   /id="VAR_036858"
FT   VARIANT         578
FT                   /note="D -> N (in DFNB24; dbSNP:rs121918379)"
FT                   /evidence="ECO:0000269|PubMed:17226784"
FT                   /id="VAR_036859"
FT   CONFLICT        435
FT                   /note="K -> R (in Ref. 2; BAH14432)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   583 AA;  68564 MW;  889687E1D675FFE7 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 LKQIEEQTIK
     AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SAIAKQAADQ MKNQEQLAAE
     LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP
     PTENEHDEHD ENNAEASAEL SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD
     ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
//

If you have problems or comments...

PBIL Back to PBIL home page