MYB51_ARATH
ID MYB51_ARATH Reviewed; 352 AA.
AC O49782;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Transcription factor MYB51;
DE AltName: Full=Myb-related protein 51;
DE Short=AtMYB51;
DE AltName: Full=Protein HIGH INDOLIC GLUCOSINOLATE 1;
DE AltName: Full=Transcription factor HIG1;
GN Name=MYB51; Synonyms=HIG1; OrderedLocusNames=At1g18570; ORFNames=F25I16.9;
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].
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 [MRNA].
RA Qu L., Gu H.;
RT "The MYB transcription factor family in Arabidopsis: a genome-wide cloning
RT and expression pattern analysis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA Stracke R., Werber M., Weisshaar B.;
RT "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL Curr. Opin. Plant Biol. 4:447-456(2001).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY WOUNDING AND TOUCH,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17461791; DOI=10.1111/j.1365-313x.2007.03099.x;
RA Gigolashvili T., Berger B., Mock H.P., Mueller C., Weisshaar B.,
RA Fluegge U.I.;
RT "The transcription factor HIG1/MYB51 regulates indolic glucosinolate
RT biosynthesis in Arabidopsis thaliana.";
RL Plant J. 50:886-901(2007).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Columbia;
RX PubMed=23115560; DOI=10.3389/fpls.2012.00242;
RA Frerigmann H., Boettcher C., Baatout D., Gigolashvili T.;
RT "Glucosinolates are produced in trichomes of Arabidopsis thaliana.";
RL Front. Plant Sci. 3:242-242(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23580754; DOI=10.1093/jxb/ert094;
RA Guo R., Qian H., Shen W., Liu L., Zhang M., Cai C., Zhao Y., Qiao J.,
RA Wang Q.;
RT "BZR1 and BES1 participate in regulation of glucosinolate biosynthesis by
RT brassinosteroids in Arabidopsis.";
RL J. Exp. Bot. 64:2401-2412(2013).
RN [11]
RP FUNCTION, AND INTERACTION WITH MYC2; MYC3 AND MYC4.
RX PubMed=23943862; DOI=10.1105/tpc.113.115139;
RA Schweizer F., Fernandez-Calvo P., Zander M., Diez-Diaz M., Fonseca S.,
RA Glauser G., Lewsey M.G., Ecker J.R., Solano R., Reymond P.;
RT "Arabidopsis basic helix-loop-helix transcription factors MYC2, MYC3, and
RT MYC4 regulate glucosinolate biosynthesis, insect performance, and feeding
RT behavior.";
RL Plant Cell 25:3117-3132(2013).
CC -!- FUNCTION: Transcription factor positively regulating indolic
CC glucosinolate biosynthetic pathway genes. {ECO:0000269|PubMed:17461791,
CC ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23943862}.
CC -!- SUBUNIT: Can form complexes with MYC2, MYC3 or MYC4.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:17461791}.
CC -!- TISSUE SPECIFICITY: Expressed in vegetative parts of the plant, mainly
CC in mature rosette leaves and in trichomes. Detected in roots, but not
CC in mature flowers or siliques. {ECO:0000269|PubMed:17461791,
CC ECO:0000269|PubMed:23115560}.
CC -!- INDUCTION: Up-regulated by touch or wounding.
CC {ECO:0000269|PubMed:17461791, ECO:0000269|PubMed:23115560}.
CC -!- DISRUPTION PHENOTYPE: Low levels of indolic glucosinolates.
CC {ECO:0000269|PubMed:17461791, ECO:0000269|PubMed:23580754}.
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DR EMBL; AF062887; AAC83609.1; -; mRNA.
DR EMBL; AY519555; AAS10025.1; -; mRNA.
DR EMBL; AC026238; AAF98417.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29730.1; -; Genomic_DNA.
DR EMBL; AK117331; BAC42001.1; -; mRNA.
DR EMBL; BT006244; AAP12893.1; -; mRNA.
DR PIR; T51659; T51659.
DR RefSeq; NP_173292.1; NM_101715.4.
DR AlphaFoldDB; O49782; -.
DR SMR; O49782; -.
DR BioGRID; 23677; 53.
DR IntAct; O49782; 2.
DR STRING; 3702.AT1G18570.1; -.
DR PaxDb; O49782; -.
DR PRIDE; O49782; -.
DR EnsemblPlants; AT1G18570.1; AT1G18570.1; AT1G18570.
DR GeneID; 838438; -.
DR Gramene; AT1G18570.1; AT1G18570.1; AT1G18570.
DR KEGG; ath:AT1G18570; -.
DR Araport; AT1G18570; -.
DR TAIR; locus:2027463; AT1G18570.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_6_1_1; -.
DR InParanoid; O49782; -.
DR OMA; NLLCHGT; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; O49782; -.
DR PRO; PR:O49782; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49782; baseline and differential.
DR Genevisible; O49782; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IEP: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 Activator; DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..352
FT /note="Transcription factor MYB51"
FT /id="PRO_0000424712"
FT DOMAIN 10..62
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 63..117
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 38..62
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 90..113
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 39154 MW; ABD3751C93516AA4 CRC64;
MVRTPCCKAE LGLKKGAWTP EEDQKLLSYL NRHGEGGWRT LPEKAGLKRC GKSCRLRWAN
YLRPDIKRGE FTEDEERSII SLHALHGNKW SAIARGLPGR TDNEIKNYWN THIKKRLIKK
GIDPVTHKGI TSGTDKSENL PEKQNVNLTT SDHDLDNDKA KKNNKNFGLS SASFLNKVAN
RFGKRINQSV LSEIIGSGGP LASTSHTTNT TTTSVSVDSE SVKSTSSSFA PTSNLLCHGT
VATTPVSSNF DVDGNVNLTC SSSTFSDSSV NNPLMYCDNF VGNNNVDDED TIGFSTFLND
EDFMMLEESC VENTAFMKEL TRFLHEDEND VVDVTPVYER QDLFDEIDNY FG
