SOX4_HUMAN
ID SOX4_HUMAN Reviewed; 474 AA.
AC Q06945;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription factor SOX-4 {ECO:0000305};
GN Name=SOX4 {ECO:0000303|PubMed:8268656, ECO:0000312|HGNC:HGNC:11200};
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], AND TISSUE SPECIFICITY.
RX PubMed=8268656; DOI=10.1007/bf00361388;
RA Farr C.J., Easty D.J., Ragoussis J., Collignon J., Lovell-Badge R.,
RA Goodfellow P.N.;
RT "Characterization and mapping of the human SOX4 gene.";
RL Mamm. Genome 4:577-584(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-123.
RX PubMed=1614875; DOI=10.1093/nar/20.11.2887;
RA Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.;
RT "A conserved family of genes related to the testis determining gene, SRY.";
RL Nucleic Acids Res. 20:2887-2887(1992).
RN [5]
RP INTERACTION WITH UBE2I, AND SUBCELLULAR LOCATION.
RX PubMed=16631117; DOI=10.1016/j.bbrc.2006.03.194;
RA Pan X., Li H., Zhang P., Jin B., Man J., Tian L., Su G., Zhao J., Li W.,
RA Liu H., Gong W., Zhou T., Zhang X.;
RT "Ubc9 interacts with SOX4 and represses its transcriptional activity.";
RL Biochem. Biophys. Res. Commun. 344:727-734(2006).
RN [6]
RP FUNCTION, INTERACTION WITH HDAC1, ACETYLATION AT LYS-95, AND MUTAGENESIS OF
RP LYS-45 AND LYS-95.
RX PubMed=26291311; DOI=10.1038/cddis.2015.190;
RA Jang S.M., Kim J.W., Kim C.H., An J.H., Johnson A., Song P.I., Rhee S.,
RA Choi K.H.;
RT "KAT5-mediated SOX4 acetylation orchestrates chromatin remodeling during
RT myoblast differentiation.";
RL Cell Death Dis. 6:e1857-e1857(2015).
RN [7]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
RN [8]
RP INVOLVEMENT IN CSS10, VARIANTS CSS10 SER-59; LEU-66; ASN-105 AND PRO-112,
RP CHARACTERIZATION OF VARIANTS CSS10 SER-59; LEU-66; ASN-105 AND PRO-112, AND
RP FUNCTION.
RX PubMed=30661772; DOI=10.1016/j.ajhg.2018.12.014;
RG Deciphering Developmental Disorders Study;
RG University of Washington Center for Mendelian Genomics;
RA Zawerton A., Yao B., Yeager J.P., Pippucci T., Haseeb A., Smith J.D.,
RA Wischmann L., Kuehl S.J., Dean J.C.S., Pilz D.T., Holder S.E., McNeill A.,
RA Graziano C., Lefebvre V.;
RT "De Novo SOX4 Variants Cause a Neurodevelopmental Disease Associated with
RT Mild Dysmorphism.";
RL Am. J. Hum. Genet. 104:246-259(2019).
CC -!- FUNCTION: Transcriptional activator that binds with high affinity to
CC the T-cell enhancer motif 5'-AACAAAG-3' motif (PubMed:30661772).
CC Required for IL17A-producing Vgamma2-positive gamma-delta T-cell
CC maturation and development, via binding to regulator loci of RORC to
CC modulate expression (By similarity). Involved in skeletal myoblast
CC differentiation by promoting gene expression of CALD1
CC (PubMed:26291311). {ECO:0000250|UniProtKB:Q06831,
CC ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:30661772}.
CC -!- SUBUNIT: Interacts with UBE2I (PubMed:16631117). Interacts with HDAC1;
CC interaction inhibits the transcriptional activator activity
CC (PubMed:16631117). {ECO:0000269|PubMed:16631117}.
CC -!- INTERACTION:
CC Q06945; P04637: TP53; NbExp=4; IntAct=EBI-6672525, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:16631117}.
CC -!- TISSUE SPECIFICITY: Testis, brain, and heart.
CC {ECO:0000269|PubMed:8268656}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- PTM: Acetylation at Lys-95 by KAT5 promotes the transcription activator
CC activity and is required during myoblast differentiation
CC (PubMed:26291311). Acetylation by KAT5 abolishes the interaction
CC between SOX4 and HDAC1 and switches SOX4 into a transcriptional
CC activator (PubMed:26291311). {ECO:0000269|PubMed:26291311}.
CC -!- DISEASE: Coffin-Siris syndrome 10 (CSS10) [MIM:618506]: A form of
CC Coffin-Siris syndrome, a congenital multiple malformation syndrome with
CC broad phenotypic and genetic variability. Cardinal features are
CC intellectual disability, coarse facial features, hypertrichosis, and
CC hypoplastic or absent fifth digit nails or phalanges. Additional
CC features include malformations of the cardiac, gastrointestinal,
CC genitourinary, and/or central nervous systems. Sucking/feeding
CC difficulties, poor growth, ophthalmologic abnormalities, hearing
CC impairment, and spinal anomalies are common findings. CSS10 is
CC characterized by mild to severe intellectual disability, global
CC developmental delay, mild but distinct facial dysmorphism, fifth finger
CC clinodactyly, and small stature. Hypotonia, ventricular septal defect,
CC and spastic quadriparesis may also be present. CSS10 inheritance is
CC autosomal dominant. {ECO:0000269|PubMed:30661772}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SOX4ID42358ch6p22.html";
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DR EMBL; X70683; CAA50018.1; -; mRNA.
DR EMBL; AL136179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072668; AAH72668.1; -; mRNA.
DR EMBL; X65661; CAA46612.1; -; mRNA.
DR CCDS; CCDS4547.1; -.
DR PIR; I38240; I38240.
DR RefSeq; NP_003098.1; NM_003107.2.
DR AlphaFoldDB; Q06945; -.
DR SMR; Q06945; -.
DR BioGRID; 112542; 74.
DR CORUM; Q06945; -.
DR DIP; DIP-58650N; -.
DR IntAct; Q06945; 26.
DR STRING; 9606.ENSP00000244745; -.
DR iPTMnet; Q06945; -.
DR PhosphoSitePlus; Q06945; -.
DR BioMuta; SOX4; -.
DR DMDM; 548952; -.
DR EPD; Q06945; -.
DR MassIVE; Q06945; -.
DR MaxQB; Q06945; -.
DR PaxDb; Q06945; -.
DR PeptideAtlas; Q06945; -.
DR PRIDE; Q06945; -.
DR ProteomicsDB; 58488; -.
DR Antibodypedia; 25243; 297 antibodies from 35 providers.
DR DNASU; 6659; -.
DR Ensembl; ENST00000244745.4; ENSP00000244745.1; ENSG00000124766.7.
DR GeneID; 6659; -.
DR KEGG; hsa:6659; -.
DR MANE-Select; ENST00000244745.4; ENSP00000244745.1; NM_003107.3; NP_003098.1.
DR UCSC; uc003ndi.4; human.
DR CTD; 6659; -.
DR DisGeNET; 6659; -.
DR GeneCards; SOX4; -.
DR GeneReviews; SOX4; -.
DR HGNC; HGNC:11200; SOX4.
DR HPA; ENSG00000124766; Tissue enhanced (lymphoid).
DR MalaCards; SOX4; -.
DR MIM; 184430; gene.
DR MIM; 618506; phenotype.
DR neXtProt; NX_Q06945; -.
DR OpenTargets; ENSG00000124766; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR PharmGKB; PA36037; -.
DR VEuPathDB; HostDB:ENSG00000124766; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000161470; -.
DR HOGENOM; CLU_043342_0_0_1; -.
DR InParanoid; Q06945; -.
DR OMA; PAEHHHN; -.
DR OrthoDB; 1186233at2759; -.
DR PhylomeDB; Q06945; -.
DR PathwayCommons; Q06945; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q06945; -.
DR SIGNOR; Q06945; -.
DR BioGRID-ORCS; 6659; 38 hits in 1111 CRISPR screens.
DR ChiTaRS; SOX4; human.
DR GeneWiki; SOX4; -.
DR GenomeRNAi; 6659; -.
DR Pharos; Q06945; Tbio.
DR PRO; PR:Q06945; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q06945; protein.
DR Bgee; ENSG00000124766; Expressed in cortical plate and 205 other tissues.
DR Genevisible; Q06945; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0035910; P:ascending aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003211; P:cardiac ventricle formation; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0021782; P:glial cell development; ISS:UniProtKB.
DR GO; GO:0014009; P:glial cell proliferation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:BHF-UCL.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0060993; P:kidney morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060174; P:limb bud formation; ISS:UniProtKB.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0001841; P:neural tube formation; ISS:UniProtKB.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0003357; P:noradrenergic neuron differentiation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
DR GO; GO:2000761; P:positive regulation of N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0002328; P:pro-B cell differentiation; ISS:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IMP:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; ISS:UniProtKB.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017386; SOX-12/11/4.
DR Pfam; PF00505; HMG_box; 1.
DR PIRSF; PIRSF038098; SOX-12/11/4a; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Disease variant; DNA-binding;
KW Intellectual disability; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..474
FT /note="Transcription factor SOX-4"
FT /id="PRO_0000048724"
FT DNA_BIND 59..127
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 426..434
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:34342803"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26291311"
FT VARIANT 59
FT /note="I -> S (in CSS10; loss of DNA-binding transcription
FT factor activity; dbSNP:rs1582601669)"
FT /evidence="ECO:0000269|PubMed:30661772"
FT /id="VAR_083360"
FT VARIANT 66
FT /note="F -> L (in CSS10; loss of DNA-binding transcription
FT factor activity; dbSNP:rs1334099693)"
FT /evidence="ECO:0000269|PubMed:30661772"
FT /id="VAR_083361"
FT VARIANT 105
FT /note="K -> N (in CSS10; loss of DNA-binding transcription
FT factor activity; dbSNP:rs1582601747)"
FT /evidence="ECO:0000269|PubMed:30661772"
FT /id="VAR_083362"
FT VARIANT 112
FT /note="A -> P (in CSS10; loss DNA-binding transcription
FT factor activity; dbSNP:rs1464282327)"
FT /evidence="ECO:0000269|PubMed:30661772"
FT /id="VAR_083363"
FT MUTAGEN 45
FT /note="K->R: Does not affect acetylation by KAT5."
FT /evidence="ECO:0000269|PubMed:26291311"
FT MUTAGEN 95
FT /note="K->R: Abolished acetylation by KAT5."
FT /evidence="ECO:0000269|PubMed:26291311"
FT CONFLICT 71
FT /note="Q -> P (in Ref. 4; CAA46612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 47263 MW; CB75B76ABF507A07 CRC64;
MVQQTNNAEN TEALLAGESS DSGAGLELGI ASSPTPGSTA STGGKADDPS WCKTPSGHIK
RPMNAFMVWS QIERRKIMEQ SPDMHNAEIS KRLGKRWKLL KDSDKIPFIR EAERLRLKHM
ADYPDYKYRP RKKVKSGNAN SSSSAAASSK PGEKGDKVGG SGGGGHGGGG GGGSSNAGGG
GGGASGGGAN SKPAQKKSCG SKVAGGAGGG VSKPHAKLIL AGGGGGGKAA AAAAASFAAE
QAGAAALLPL GAAADHHSLY KARTPSASAS ASSAASASAA LAAPGKHLAE KKVKRVYLFG
GLGTSSSPVG GVGAGADPSD PLGLYEEEGA GCSPDAPSLS GRSSAASSPA AGRSPADHRG
YASLRAASPA PSSAPSHASS SASSHSSSSS SSGSSSSDDE FEDDLLDLNP SSNFESMSLG
SFSSSSALDR DLDFNFEPGS GSHFEFPDYC TPEVSEMISG DWLESSISNL VFTY
