MYB41_ARATH
ID MYB41_ARATH Reviewed; 282 AA.
AC Q9M0J5; Q9ZTE3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Transcription factor MYB41 {ECO:0000305};
DE AltName: Full=Myb-related protein 41 {ECO:0000303|PubMed:11597504};
DE Short=AtMYB41 {ECO:0000303|PubMed:11597504};
GN Name=MYB41 {ECO:0000303|PubMed:11597504};
GN OrderedLocusNames=At4g28110 {ECO:0000312|Araport:AT4G28110};
GN ORFNames=T13J8.220 {ECO:0000312|EMBL:CAB36780.1};
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].
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 [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=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-282.
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=19211694; DOI=10.1104/pp.108.134874;
RA Lippold F., Sanchez D.H., Musialak M., Schlereth A., Scheible W.R.,
RA Hincha D.K., Udvardi M.K.;
RT "AtMyb41 regulates transcriptional and metabolic responses to osmotic
RT stress in Arabidopsis.";
RL Plant Physiol. 149:1761-1772(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MPK6,
RP PHOSPHORYLATION AT SER-251, AND MUTAGENESIS OF SER-251.
RX PubMed=22575450; DOI=10.1016/j.bbrc.2012.04.137;
RA Hoang M.H., Nguyen X.C., Lee K., Kwon Y.S., Pham H.T., Park H.C., Yun D.J.,
RA Lim C.O., Chung W.S.;
RT "Phosphorylation by AtMPK6 is required for the biological function of
RT AtMYB41 in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 422:181-186(2012).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=25060192; DOI=10.1111/tpj.12624;
RA Kosma D.K., Murmu J., Razeq F.M., Santos P., Bourgault R., Molina I.,
RA Rowland O.;
RT "AtMYB41 activates ectopic suberin synthesis and assembly in multiple plant
RT species and cell types.";
RL Plant J. 80:216-229(2014).
CC -!- FUNCTION: Transcription factor involved in salt stress response.
CC Confers tolerance to salt stress (PubMed:22575450). Involved in
CC distinct cellular processes in response to osmotic stress, including
CC control of primary metabolism and negative regulation of short-term
CC transcriptional responses to osmotic stress (PubMed:19211694). Can
CC activate the steps necessary for aliphatic suberin synthesis and
CC deposition of cell wall-associated suberin-like lamellae. Involved in
CC the production of aliphatic suberin under abiotic stress conditions
CC (PubMed:25060192). {ECO:0000269|PubMed:19211694,
CC ECO:0000269|PubMed:22575450, ECO:0000269|PubMed:25060192}.
CC -!- SUBUNIT: Interacts with MPK6. {ECO:0000269|PubMed:22575450}.
CC -!- INTERACTION:
CC Q9M0J5; Q39026: MPK6; NbExp=2; IntAct=EBI-4474106, EBI-349548;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- INDUCTION: Induced by salt stress (PubMed:19211694, PubMed:25060192).
CC Induced by osmotic stress (PubMed:19211694). Induced by abscisic acid
CC (PubMed:25060192). {ECO:0000269|PubMed:19211694,
CC ECO:0000269|PubMed:25060192}.
CC -!- PTM: Phosphorylated at SER-251 by MPK6 in response to salt stress.
CC Phosphorylation is required for its function in salt stress tolerance.
CC {ECO:0000269|PubMed:22575450}.
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DR EMBL; AY519610; AAS10080.1; -; mRNA.
DR EMBL; AL035524; CAB36780.1; -; Genomic_DNA.
DR EMBL; AL161572; CAB79613.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85442.1; -; Genomic_DNA.
DR EMBL; BT001930; AAN71929.1; -; mRNA.
DR EMBL; AF062882; AAC83604.1; -; mRNA.
DR PIR; B85327; B85327.
DR PIR; T02912; T02912.
DR RefSeq; NP_194540.1; NM_118951.3.
DR AlphaFoldDB; Q9M0J5; -.
DR SMR; Q9M0J5; -.
DR IntAct; Q9M0J5; 2.
DR STRING; 3702.AT4G28110.1; -.
DR iPTMnet; Q9M0J5; -.
DR PaxDb; Q9M0J5; -.
DR PRIDE; Q9M0J5; -.
DR EnsemblPlants; AT4G28110.1; AT4G28110.1; AT4G28110.
DR GeneID; 828927; -.
DR Gramene; AT4G28110.1; AT4G28110.1; AT4G28110.
DR KEGG; ath:AT4G28110; -.
DR Araport; AT4G28110; -.
DR TAIR; locus:2132957; AT4G28110.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_15_5_1; -.
DR InParanoid; Q9M0J5; -.
DR OMA; QDFNPIY; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9M0J5; -.
DR PRO; PR:Q9M0J5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0J5; baseline and differential.
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:0006723; P:cuticle hydrocarbon biosynthetic process; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0080090; P:regulation of primary metabolic process; IMP:TAIR.
DR GO; GO:0080091; P:regulation of raffinose metabolic process; 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; Phosphoprotein; Reference proteome; Repeat;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..282
FT /note="Transcription factor MYB41"
FT /id="PRO_0000439927"
FT DOMAIN 9..65
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 66..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 180..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine; by MAPK6"
FT /evidence="ECO:0000269|PubMed:22575450"
FT MUTAGEN 251
FT /note="S->A: Loss of phosphorylation; loss of function in
FT salt tolerance."
FT /evidence="ECO:0000269|PubMed:22575450"
SQ SEQUENCE 282 AA; 31652 MW; 085D065C7980F7FE CRC64;
MGRSPCCDKN GVKKGPWTAE EDQKLIDYIR FHGPGNWRTL PKNAGLHRCG KSCRLRWTNY
LRPDIKRGRF SFEEEETIIQ LHSVMGNKWS AIAARLPGRT DNEIKNHWNT HIRKRLVRSG
IDPVTHSPRL DLLDLSSLLS ALFNQPNFSA VATHASSLLN PDVLRLASLL LPLQNPNPVY
PSNLDQNLQT PNTSSESSQP QAETSTVPTN YETSSLEPMN ARLDDVGLAD VLPPLSESFD
LDSLMSTPMS SPRQNSIEAE TNSSTFFDFG IPEDFILDDF MF
