RFX3_HUMAN
ID RFX3_HUMAN Reviewed; 749 AA.
AC P48380; A8K0H5; D3DRH8; D3DRH9; Q5JTL7; Q5JTL8; Q6NW13; Q8WTU4; Q95HL5;
AC Q95HL6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcription factor RFX3;
DE AltName: Full=Regulatory factor X 3;
GN Name=RFX3;
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 2).
RX PubMed=8289803; DOI=10.1128/mcb.14.2.1230-1244.1994;
RA Reith W., Ucla C., Barras E., Gaud A., Durand B., Herrero-Sanchez C.,
RA Kobr M., Mach B.;
RT "RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel
RT family of homodimeric and heterodimeric DNA-binding proteins.";
RL Mol. Cell. Biol. 14:1230-1244(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Muscle, and Testis;
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 [6]
RP SUBUNIT.
RX PubMed=10330134; DOI=10.1128/mcb.19.6.3940;
RA Iwama A., Pan J., Zhang P., Reith W., Mach B., Tenen D.G., Sun Z.;
RT "Dimeric RFX proteins contribute to the activity and lineage specificity of
RT the interleukin-5 receptor alpha promoter through activation and repression
RT domains.";
RL Mol. Cell. Biol. 19:3940-3950(1999).
RN [7]
RP FUNCTION.
RX PubMed=12411430; DOI=10.1074/jbc.m209574200;
RA Nakayama A., Murakami H., Maeyama N., Yamashiro N., Sakakibara A., Mori N.,
RA Takahashi M.;
RT "Role for RFX transcription factors in non-neuronal cell-specific
RT inactivation of the microtubule-associated protein MAP1A promoter.";
RL J. Biol. Chem. 278:233-240(2003).
RN [8]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH RFX6.
RX PubMed=20148032; DOI=10.1038/nature08748;
RA Smith S.B., Qu H.Q., Taleb N., Kishimoto N.Y., Scheel D.W., Lu Y.,
RA Patch A.M., Grabs R., Wang J., Lynn F.C., Miyatsuka T., Mitchell J.,
RA Seerke R., Desir J., Eijnden S.V., Abramowicz M., Kacet N., Weill J.,
RA Renard M.E., Gentile M., Hansen I., Dewar K., Hattersley A.T., Wang R.,
RA Wilson M.E., Johnson J.D., Polychronakos C., German M.S.;
RT "Rfx6 directs islet formation and insulin production in mice and humans.";
RL Nature 463:775-780(2010).
CC -!- FUNCTION: Transcription factor required for ciliogenesis and islet cell
CC differentiation during endocrine pancreas development. Essential for
CC the differentiation of nodal monocilia and left-right asymmetry
CC specification during embryogenesis. Required for the biogenesis of
CC motile cilia by governing growth and beating efficiency of motile
CC cells. Also required for ciliated ependymal cell differentiation.
CC Regulates the expression of genes involved in ciliary assembly
CC (DYNC2LI1, FOXJ1 and BBS4) and genes involved in ciliary motility
CC (DNAH11, DNAH9 and DNAH5) (By similarity). Together with RFX6,
CC participates in the differentiation of 4 of the 5 islet cell types
CC during endocrine pancreas development, with the exception of pancreatic
CC PP (polypeptide-producing) cells. Regulates transcription by forming a
CC heterodimer with another RFX protein and binding to the X-box in the
CC promoter of target genes (PubMed:20148032). Represses transcription of
CC MAP1A in non-neuronal cells but not in neuronal cells
CC (PubMed:12411430). {ECO:0000250|UniProtKB:P48381,
CC ECO:0000269|PubMed:12411430, ECO:0000269|PubMed:20148032}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with RFX1 and RFX2, and RFX6.
CC {ECO:0000269|PubMed:10330134, ECO:0000269|PubMed:20148032}.
CC -!- INTERACTION:
CC P48380; Q14192: FHL2; NbExp=10; IntAct=EBI-742557, EBI-701903;
CC P48380; Q13643: FHL3; NbExp=4; IntAct=EBI-742557, EBI-741101;
CC P48380; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-742557, EBI-16439278;
CC P48380; Q12933: TRAF2; NbExp=5; IntAct=EBI-742557, EBI-355744;
CC P48380; Q15654: TRIP6; NbExp=3; IntAct=EBI-742557, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P48380-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48380-2; Sequence=VSP_007626, VSP_007627;
CC Name=3;
CC IsoId=P48380-3; Sequence=VSP_015162, VSP_015163;
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
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DR EMBL; X76092; CAA53706.1; -; mRNA.
DR EMBL; AK289540; BAF82229.1; -; mRNA.
DR EMBL; AL365202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58795.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58796.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58798.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58799.1; -; Genomic_DNA.
DR EMBL; BC022191; AAH22191.1; -; mRNA.
DR EMBL; BC067778; AAH67778.1; -; mRNA.
DR CCDS; CCDS6449.1; -. [P48380-1]
DR CCDS; CCDS6450.1; -. [P48380-2]
DR CCDS; CCDS75809.1; -. [P48380-3]
DR PIR; D55926; D55926.
DR RefSeq; NP_001269045.1; NM_001282116.1. [P48380-1]
DR RefSeq; NP_001269046.1; NM_001282117.1. [P48380-3]
DR RefSeq; NP_002910.1; NM_002919.3. [P48380-2]
DR RefSeq; NP_602304.1; NM_134428.2. [P48380-1]
DR AlphaFoldDB; P48380; -.
DR SMR; P48380; -.
DR BioGRID; 111923; 44.
DR IntAct; P48380; 21.
DR MINT; P48380; -.
DR STRING; 9606.ENSP00000371434; -.
DR iPTMnet; P48380; -.
DR PhosphoSitePlus; P48380; -.
DR SwissPalm; P48380; -.
DR BioMuta; RFX3; -.
DR DMDM; 32172437; -.
DR EPD; P48380; -.
DR jPOST; P48380; -.
DR MassIVE; P48380; -.
DR MaxQB; P48380; -.
DR PaxDb; P48380; -.
DR PeptideAtlas; P48380; -.
DR PRIDE; P48380; -.
DR ProteomicsDB; 55883; -. [P48380-1]
DR ProteomicsDB; 55884; -. [P48380-2]
DR ProteomicsDB; 55885; -. [P48380-3]
DR Antibodypedia; 23939; 251 antibodies from 31 providers.
DR DNASU; 5991; -.
DR Ensembl; ENST00000302303.5; ENSP00000303847.2; ENSG00000080298.16. [P48380-3]
DR Ensembl; ENST00000358730.6; ENSP00000351574.2; ENSG00000080298.16. [P48380-2]
DR Ensembl; ENST00000382004.7; ENSP00000371434.3; ENSG00000080298.16. [P48380-1]
DR Ensembl; ENST00000617270.5; ENSP00000482598.1; ENSG00000080298.16. [P48380-1]
DR GeneID; 5991; -.
DR KEGG; hsa:5991; -.
DR MANE-Select; ENST00000617270.5; ENSP00000482598.1; NM_001282116.2; NP_001269045.1.
DR UCSC; uc003zhr.5; human. [P48380-1]
DR CTD; 5991; -.
DR DisGeNET; 5991; -.
DR GeneCards; RFX3; -.
DR HGNC; HGNC:9984; RFX3.
DR HPA; ENSG00000080298; Tissue enhanced (brain, choroid plexus).
DR MIM; 601337; gene.
DR neXtProt; NX_P48380; -.
DR OpenTargets; ENSG00000080298; -.
DR PharmGKB; PA34354; -.
DR VEuPathDB; HostDB:ENSG00000080298; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244879; -.
DR HOGENOM; CLU_010393_1_1_1; -.
DR InParanoid; P48380; -.
DR OMA; HATRVSQ; -.
DR OrthoDB; 346630at2759; -.
DR PhylomeDB; P48380; -.
DR TreeFam; TF321340; -.
DR PathwayCommons; P48380; -.
DR SignaLink; P48380; -.
DR SIGNOR; P48380; -.
DR BioGRID-ORCS; 5991; 15 hits in 1101 CRISPR screens.
DR ChiTaRS; RFX3; human.
DR GeneWiki; RFX3; -.
DR GenomeRNAi; 5991; -.
DR Pharos; P48380; Tbio.
DR PRO; PR:P48380; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P48380; protein.
DR Bgee; ENSG00000080298; Expressed in bronchial epithelial cell and 176 other tissues.
DR ExpressionAtlas; P48380; baseline and differential.
DR Genevisible; P48380; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0048469; P:cell maturation; ISS:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL.
DR GO; GO:0060285; P:cilium-dependent cell motility; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000078; P:positive regulation of type B pancreatic cell development; ISS:BHF-UCL.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0072560; P:type B pancreatic cell maturation; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR007668; RFX1_trans_act.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 1.
DR Pfam; PF04589; RFX1_trans_act; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; DNA-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..749
FT /note="Transcription factor RFX3"
FT /id="PRO_0000215290"
FT DNA_BIND 183..258
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 663..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 401..413
FT /note="SNLSEIESRLPKA -> RSESTSFPIHFHG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015162"
FT VAR_SEQ 414..749
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015163"
FT VAR_SEQ 657..707
FT /note="FGDLNAVSPGNLDKDEGSEVESEMDEELDDSSEPQAKREKTELSQAFPVGC
FT -> VREAERAVTHWVIKNKPELHFSLNTLLIKTMVPNQVSLRARRDCGVIARVP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:8289803"
FT /id="VSP_007626"
FT VAR_SEQ 708..749
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8289803"
FT /id="VSP_007627"
FT CONFLICT 150
FT /note="H -> P (in Ref. 2; BAF82229)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="E -> G (in Ref. 5; AAH67778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 83530 MW; 531F5CFCA7A707C7 CRC64;
MQTSETGSDT GSTVTLQTSV ASQAAVPTQV VQQVPVQQQV QQVQTVQQVQ HVYPAQVQYV
EGSDTVYTNG AIRTTTYPYT ETQMYSQNTG GNYFDTQGSS AQVTTVVSSH SMVGTGGIQM
GVTGGQLISS SGGTYLIGNS MENSGHSVTH TTRASPATIE MAIETLQKSD GLSTHRSSLL
NSHLQWLLDN YETAEGVSLP RSTLYNHYLR HCQEHKLDPV NAASFGKLIR SIFMGLRTRR
LGTRGNSKYH YYGIRVKPDS PLNRLQEDMQ YMAMRQQPMQ QKQRYKPMQK VDGVADGFTG
SGQQTGTSVE QTVIAQSQHH QQFLDASRAL PEFGEVEISS LPDGTTFEDI KSLQSLYREH
CEAILDVVVN LQFSLIEKLW QTFWRYSPST PTDGTTITES SNLSEIESRL PKAKLITLCK
HESILKWMCN CDHGMYQALV EILIPDVLRP IPSALTQAIR NFAKSLEGWL SNAMNNIPQR
MIQTKVAAVS AFAQTLRRYT SLNHLAQAAR AVLQNTSQIN QMLSDLNRVD FANVQEQASW
VCQCDDNMVQ RLETDFKMTL QQQSTLEQWA AWLDNVMMQA LKPYEGRPSF PKAARQFLLK
WSFYSSMVIR DLTLRSAASF GSFHLIRLLY DEYMFYLVEH RVAQATGETP IAVMGEFGDL
NAVSPGNLDK DEGSEVESEM DEELDDSSEP QAKREKTELS QAFPVGCMQP VLETGVQPSL
LNPIHSEHIV TSTQTIRQCS ATGNTYTAV
