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MYB28_ARATH
ID   MYB28_ARATH             Reviewed;         366 AA.
AC   Q9SPG2; F4K3H4;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Transcription factor MYB28;
DE   AltName: Full=Myb-related protein 28;
DE            Short=AtMYB28;
DE   AltName: Full=Protein HIGH ALIPHATIC GLUCOSINOLATE 1;
DE   AltName: Full=Protein PRODUCTION OF METHIONINE-DERIVED GLUCOSINOLATE 1;
GN   Name=MYB28; Synonyms=HAG1, PMG1; OrderedLocusNames=At5g61420;
GN   ORFNames=MFB13.22;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), GENE FAMILY, AND
RP   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Qu L.-J., 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND INDUCTION BY GA; JA AND SA.
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   [7]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY MECHANICAL STIMULI AND GLUCOSE,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=17521412; DOI=10.1111/j.1365-313x.2007.03133.x;
RA   Gigolashvili T., Yatusevich R., Berger B., Mueller C., Fluegge U.-I.;
RT   "The R2R3-MYB transcription factor HAG1/MYB28 is a regulator of methionine-
RT   derived glucosinolate biosynthesis in Arabidopsis thaliana.";
RL   Plant J. 51:247-261(2007).
RN   [8]
RP   FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS.
RX   PubMed=17420480; DOI=10.1073/pnas.0611629104;
RA   Hirai M.Y., Sugiyama K., Sawada Y., Tohge T., Obayashi T., Suzuki A.,
RA   Araki R., Sakurai N., Suzuki H., Aoki K., Goda H., Nishizawa O.I.,
RA   Shibata D., Saito K.;
RT   "Omics-based identification of Arabidopsis Myb transcription factors
RT   regulating aliphatic glucosinolate biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:6478-6483(2007).
RN   [9]
RP   FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS.
RX   PubMed=18042203; DOI=10.1111/j.1469-8137.2007.02295.x;
RA   Gigolashvili T., Engqvist M., Yatusevich R., Mueller C., Fluegge U.I.;
RT   "HAG2/MYB76 and HAG3/MYB29 exert a specific and coordinated control on the
RT   regulation of aliphatic glucosinolate biosynthesis in Arabidopsis
RT   thaliana.";
RL   New Phytol. 177:627-642(2008).
RN   [10]
RP   FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS.
RC   STRAIN=cv. Columbia;
RX   PubMed=18446225; DOI=10.1371/journal.pone.0002068;
RA   Beekwilder J., van Leeuwen W., van Dam N.M., Bertossi M., Grandi V.,
RA   Mizzi L., Soloviev M., Szabados L., Molthoff J.W., Schipper B.,
RA   Verbocht H., de Vos R.C.H., Morandini P., Aarts M.G.M., Bovy A.;
RT   "The impact of the absence of aliphatic glucosinolates on insect herbivory
RT   in Arabidopsis.";
RL   PLoS ONE 3:E2068-E2068(2008).
RN   [11]
RP   FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=20348214; DOI=10.1104/pp.109.149286;
RA   Soenderby I.E., Burow M., Rowe H.C., Kliebenstein D.J., Halkier B.A.;
RT   "A complex interplay of three R2R3 MYB transcription factors determines the
RT   profile of aliphatic glucosinolates in Arabidopsis.";
RL   Plant Physiol. 153:348-363(2010).
RN   [12]
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   [13]
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   [14]
RP   FUNCTION, AND INDUCTION BY SULFUR.
RX   PubMed=23792303; DOI=10.1093/pcp/pct085;
RA   Li Y., Sawada Y., Hirai A., Sato M., Kuwahara A., Yan X., Hirai M.Y.;
RT   "Novel insights into the function of Arabidopsis R2R3-MYB transcription
RT   factors regulating aliphatic glucosinolate biosynthesis.";
RL   Plant Cell Physiol. 54:1335-1344(2013).
RN   [15]
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: Major regulator of short-chained aliphatic glucosinolates
CC       (GLSs) biosynthesis. Together with MYB29/HAG3 and MYB76/HAG2, promotes
CC       aliphatic glucosinolate biosynthesis but represses indolic
CC       glucosinolate biosynthesis. Prevents insect performance (e.g.
CC       lepidopteran insect Mamestra brassicae and Spodoptera exigua) by
CC       promoting glucosinolates. {ECO:0000269|PubMed:17420480,
CC       ECO:0000269|PubMed:17521412, ECO:0000269|PubMed:18042203,
CC       ECO:0000269|PubMed:18446225, ECO:0000269|PubMed:20348214,
CC       ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23792303,
CC       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:17521412}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SPG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SPG2-2; Sequence=VSP_042252;
CC   -!- TISSUE SPECIFICITY: Expressed in generative organs, mature leaves and
CC       trichomes. {ECO:0000269|PubMed:17521412, ECO:0000269|PubMed:23115560}.
CC   -!- DEVELOPMENTAL STAGE: First present in stems, petioles and the main
CC       veins of true leaves in young seedlings. Later accumulates in leaves
CC       and present in lateral roots. During transition from the vegetative to
CC       the generative stage, preferentially expressed in inflorescence.
CC       {ECO:0000269|PubMed:17521412}.
CC   -!- INDUCTION: Slightly induced by glucose, gibberellic acid (GA), jasmonic
CC       acid (JA) and salicylic acid (SA). Transiently induced in inflorescence
CC       by mechanical stimuli such as touch or wounding, including herbivory-
CC       wounding. Up-regulated by sulfur-deficient stress.
CC       {ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:17521412,
CC       ECO:0000269|PubMed:23115560, ECO:0000269|PubMed:23792303}.
CC   -!- DISRUPTION PHENOTYPE: Low levels of aliphatic glucosinolates and
CC       decreased repressing effect of brassinosteroid on glucosinolates.
CC       {ECO:0000269|PubMed:23580754}.
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DR   EMBL; AB010073; BAB08498.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97466.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97467.1; -; Genomic_DNA.
DR   EMBL; AF175998; AAD53103.1; -; mRNA.
DR   EMBL; AY519643; AAS10113.1; -; mRNA.
DR   EMBL; BT028959; ABI54334.1; -; mRNA.
DR   RefSeq; NP_200950.1; NM_125535.4. [Q9SPG2-1]
DR   RefSeq; NP_851241.1; NM_180910.2. [Q9SPG2-2]
DR   AlphaFoldDB; Q9SPG2; -.
DR   SMR; Q9SPG2; -.
DR   BioGRID; 21507; 8.
DR   IntAct; Q9SPG2; 4.
DR   STRING; 3702.AT5G61420.2; -.
DR   PaxDb; Q9SPG2; -.
DR   PRIDE; Q9SPG2; -.
DR   ProteomicsDB; 251330; -. [Q9SPG2-1]
DR   EnsemblPlants; AT5G61420.1; AT5G61420.1; AT5G61420. [Q9SPG2-2]
DR   EnsemblPlants; AT5G61420.2; AT5G61420.2; AT5G61420. [Q9SPG2-1]
DR   GeneID; 836263; -.
DR   Gramene; AT5G61420.1; AT5G61420.1; AT5G61420. [Q9SPG2-2]
DR   Gramene; AT5G61420.2; AT5G61420.2; AT5G61420. [Q9SPG2-1]
DR   KEGG; ath:AT5G61420; -.
DR   Araport; AT5G61420; -.
DR   TAIR; locus:2163233; AT5G61420.
DR   eggNOG; KOG0048; Eukaryota.
DR   HOGENOM; CLU_028567_0_1_1; -.
DR   InParanoid; Q9SPG2; -.
DR   OMA; YSEHEIN; -.
DR   PhylomeDB; Q9SPG2; -.
DR   PRO; PR:Q9SPG2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SPG2; baseline and differential.
DR   Genevisible; Q9SPG2; AT.
DR   GO; GO:0005634; C:nucleus; 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:0010438; P:cellular response to sulfur starvation; TAS:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR   GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP: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   Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..366
FT                   /note="Transcription factor MYB28"
FT                   /id="PRO_0000415436"
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          124..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042252"
SQ   SEQUENCE   366 AA;  41134 MW;  DD7533DCB1857D0B CRC64;
     MSRKPCCVGE GLKKGAWTTE EDKKLISYIH DHGEGGWRDI PQKAGLKRCG KSCRLRWTNY
     LKPEIKRGEF SSEEEQIIIM LHASRGNKWS VIARHLPRRT DNEIKNYWNT HLKKRLMEQG
     IDPVTHKPLA SSSNPTVDEN LNSPNASSSD KQYSRSSSMP FLSRPPPSSC NMVSKVSELS
     SNDGTPIQGS SLSCKKRFKK SSSTSRLLNK VAAKATSIKD ILSASMEGSL SATTISHASF
     FNGFTEQIRN EEDSSNTSLT NTLAEFDPFS PSSLYPEHEI NATSDLNMDQ DYDFSQFFEK
     FGGDNHNEEN SMNDLLMSDV SQEVSSTSVD DQDNMVGNFE GWSNYLLDHT NFMYDTDSDS
     LEKHFI
 
 
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