MYB4_ARATH
ID MYB4_ARATH Reviewed; 282 AA.
AC Q9SZP1; O49774; Q7DLI1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcription repressor MYB4;
DE AltName: Full=Myb-related protein 4;
DE Short=AtMYB4;
GN Name=MYB4; OrderedLocusNames=At4g38620; ORFNames=F20M13.180;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9839469; DOI=10.1046/j.1365-313x.1998.00278.x;
RA Kranz H.D., Denekamp M., Greco R., Jin H.-L., Leyva A., Meissner R.C.,
RA Petroni K., Urzainqui A., Bevan M., Martin C., Smeekens S., Tonelli C.,
RA Paz-Ares J., Weisshaar B.;
RT "Towards functional characterisation of the members of the R2R3-MYB gene
RT family from Arabidopsis thaliana.";
RL Plant J. 16:263-276(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-99.
RX PubMed=9628022; DOI=10.1046/j.1365-313x.1998.00113.x;
RA Romero I., Fuertes A., Benito M.J., Malpica J.M., Leyva A., Paz-Ares J.;
RT "More than 80 R2R3-MYB regulatory genes in the genome of Arabidopsis
RT thaliana.";
RL Plant J. 14:273-284(1998).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11080161; DOI=10.1093/emboj/19.22.6150;
RA Jin H., Cominelli E., Bailey P., Parr A., Mehrtens F., Jones J.,
RA Tonelli C., Weisshaar B., Martin C.;
RT "Transcriptional repression by AtMYB4 controls production of UV-protecting
RT sunscreens in Arabidopsis.";
RL EMBO J. 19:6150-6161(2000).
RN [8]
RP INTERACTION WITH BHLH12 AND BHLH42.
RX PubMed=15361138; DOI=10.1111/j.1365-313x.2004.02183.x;
RA Zimmermann I.M., Heim M.A., Weisshaar B., Uhrig J.F.;
RT "Comprehensive identification of Arabidopsis thaliana MYB transcription
RT factors interacting with R/B-like BHLH proteins.";
RL Plant J. 40:22-34(2004).
RN [9]
RP GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [10]
RP INTERACTION WITH SAD2.
RX PubMed=17993626; DOI=10.1105/tpc.106.048900;
RA Zhao J., Zhang W., Zhao Y., Gong X., Guo L., Zhu G., Wang X., Gong Z.,
RA Schumaker K.S., Guo Y.;
RT "SAD2, an importin -like protein, is required for UV-B response in
RT Arabidopsis by mediating MYB4 nuclear trafficking.";
RL Plant Cell 19:3805-3818(2007).
CC -!- FUNCTION: Transcription repressor involved in regulation of protection
CC against UV. Mediates transcriptional repression of CYP73A5, the gene
CC encoding trans-cinnamate 4-monooxygenase, thereby regulating the
CC accumulation of the UV-protectant compound sinapoylmalate.
CC {ECO:0000269|PubMed:11080161}.
CC -!- SUBUNIT: Interacts with BHLH12/MYC1 and BHLH42/TT8 (PubMed:15361138).
CC Interacts with SAD2 (PubMed:17993626). {ECO:0000269|PubMed:15361138,
CC ECO:0000269|PubMed:17993626}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Highly expressed in
CC siliques. Weakly expressed in seedlings, young and mature leaves,
CC cauline leaves, stems, flower buds and roots.
CC {ECO:0000269|PubMed:9839469}.
CC -!- INDUCTION: Down-regulated by exposure to UV-B light.
CC {ECO:0000269|PubMed:11080161}.
CC -!- DISRUPTION PHENOTYPE: Defects lead to a better tolerance of UV-B
CC irradiation due to the increase in sinapate ester accumulation.
CC {ECO:0000269|PubMed:11080161}.
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DR EMBL; AF062860; AAC83582.1; -; mRNA.
DR EMBL; AL035540; CAB37518.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80526.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86955.1; -; Genomic_DNA.
DR EMBL; AY519615; AAS10085.1; -; mRNA.
DR EMBL; AY070100; AAL49837.1; -; mRNA.
DR EMBL; AY123004; AAM67537.1; -; mRNA.
DR EMBL; AY140037; AAM98178.1; -; mRNA.
DR EMBL; BT006302; AAP13410.1; -; mRNA.
DR EMBL; Z95763; CAB09195.1; -; mRNA.
DR PIR; T05690; T05690.
DR PIR; T51632; T51632.
DR RefSeq; NP_195574.1; NM_120023.3.
DR AlphaFoldDB; Q9SZP1; -.
DR SMR; Q9SZP1; -.
DR BioGRID; 15298; 6.
DR IntAct; Q9SZP1; 4.
DR STRING; 3702.AT4G38620.1; -.
DR PaxDb; Q9SZP1; -.
DR PRIDE; Q9SZP1; -.
DR ProteomicsDB; 251002; -.
DR EnsemblPlants; AT4G38620.1; AT4G38620.1; AT4G38620.
DR GeneID; 830018; -.
DR Gramene; AT4G38620.1; AT4G38620.1; AT4G38620.
DR KEGG; ath:AT4G38620; -.
DR Araport; AT4G38620; -.
DR TAIR; locus:2121259; AT4G38620.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_23_0_1; -.
DR InParanoid; Q9SZP1; -.
DR OMA; ETFHESI; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9SZP1; -.
DR PRO; PR:Q9SZP1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZP1; baseline and differential.
DR Genevisible; Q9SZP1; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:1903086; P:negative regulation of sinapate ester biosynthetic process; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:2000762; P:regulation of phenylpropanoid metabolic process; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..282
FT /note="Transcription repressor MYB4"
FT /id="PRO_0000197075"
FT DOMAIN 9..61
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 62..116
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 37..61
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 89..112
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 119..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 141
FT /note="T -> I (in Ref. 1; AAC83582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31808 MW; CEFB4F1E9D8A8687 CRC64;
MGRSPCCEKA HTNKGAWTKE EDERLVAYIK AHGEGCWRSL PKAAGLLRCG KSCRLRWINY
LRPDLKRGNF TEEEDELIIK LHSLLGNKWS LIAGRLPGRT DNEIKNYWNT HIRRKLINRG
IDPTSHRPIQ ESSASQDSKP TQLEPVTSNT INISFTSAPK VETFHESISF PGKSEKISML
TFKEEKDECP VQEKFPDLNL ELRISLPDDV DRLQGHGKST TPRCFKCSLG MINGMECRCG
RMRCDVVGGS SKGSDMSNGF DFLGLAKKET TSLLGFRSLE MK
