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 03-AUG-2022, entry version 203.
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 (via FERM domain) with SPN/CD43
CC cytoplasmic tail (By similarity). Interacts with CD44 (By similarity).
CC {ECO:0000250|UniProtKB:P26043, ECO:0000269|PubMed:9430655}.
CC -!- INTERACTION:
CC P35241; P15311: EZR; NbExp=6; IntAct=EBI-2514878, EBI-1056902;
CC P35241; P05107: ITGB2; NbExp=2; IntAct=EBI-2514878, EBI-300173;
CC P35241; Q8IZU9: KIRREL3; NbExp=5; IntAct=EBI-2514878, EBI-16427312;
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 variants affecting the gene represented in this entry.
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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 AlphaFoldDB; P35241; -.
DR SMR; P35241; -.
DR BioGRID; 111894; 199.
DR IntAct; P35241; 31.
DR MINT; P35241; -.
DR STRING; 9606.ENSP00000384136; -.
DR DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate.
DR iPTMnet; P35241; -.
DR MetOSite; 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 Antibodypedia; 633; 456 antibodies from 39 providers.
DR DNASU; 5962; -.
DR Ensembl; ENST00000528498.5; ENSP00000432112.1; ENSG00000137710.17. [P35241-5]
DR Ensembl; ENST00000528900.5; ENSP00000433580.1; ENSG00000137710.17. [P35241-2]
DR Ensembl; ENST00000530301.5; ENSP00000436277.1; ENSG00000137710.17. [P35241-3]
DR Ensembl; ENST00000530749.5; ENSP00000437301.1; ENSG00000137710.17. [P35241-5]
DR Ensembl; ENST00000544551.5; ENSP00000445826.1; ENSG00000137710.17. [P35241-4]
DR Ensembl; ENST00000645495.2; ENSP00000496503.2; ENSG00000137710.17. [P35241-1]
DR Ensembl; ENST00000647231.1; ENSP00000496414.1; ENSG00000137710.17. [P35241-5]
DR GeneID; 5962; -.
DR KEGG; hsa:5962; -.
DR MANE-Select; ENST00000645495.2; ENSP00000496503.2; NM_002906.4; NP_002897.1.
DR UCSC; uc001pku.4; human. [P35241-1]
DR CTD; 5962; -.
DR DisGeNET; 5962; -.
DR GeneCards; RDX; -.
DR GeneReviews; RDX; -.
DR HGNC; HGNC:9944; RDX.
DR HPA; ENSG00000137710; Tissue enhanced (adrenal).
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 VEuPathDB; HostDB:ENSG00000137710; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_1081673_0_0_1; -.
DR InParanoid; P35241; -.
DR OMA; SREDSMM; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P35241; -.
DR TreeFam; TF313935; -.
DR PathwayCommons; P35241; -.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; P35241; -.
DR SIGNOR; P35241; -.
DR BioGRID-ORCS; 5962; 8 hits in 1074 CRISPR screens.
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 adrenal tissue and 212 other tissues.
DR ExpressionAtlas; P35241; baseline and differential.
DR Genevisible; P35241; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
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: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: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:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
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:0061951; P:establishment of protein localization to plasma membrane; ISS:UniProtKB.
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: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:0045732; P:positive regulation of protein catabolic process; 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; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 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; 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 Actin capping; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Deafness; Disease variant;
KW Membrane; Non-syndromic deafness; Phosphoprotein; 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 310..330
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 462..526
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 467..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Basic and acidic 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 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:0000250"
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: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
