MY102_ARATH
ID MY102_ARATH Reviewed; 350 AA.
AC Q9LDR8; O65409; Q8LBF0; Q8W4E0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcription factor MYB102 {ECO:0000305};
DE AltName: Full=Myb-related protein 102 {ECO:0000305};
DE Short=AtMYB102 {ECO:0000303|PubMed:12857823};
DE AltName: Full=Myb-related protein M4 {ECO:0000305};
DE Short=AtM4 {ECO:0000303|PubMed:8980549};
GN Name=MYB102 {ECO:0000303|PubMed:12857823};
GN OrderedLocusNames=At4g21440 {ECO:0000312|Araport:AT4G21440};
GN ORFNames=F18E5.60 {ECO:0000312|EMBL:CAA18708.1},
GN T6K22.170 {ECO:0000312|EMBL:CAA20209.1};
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND INDUCTION
RP BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=8980549; DOI=10.1007/bf00020495;
RA Quaedvlieg N., Dockx J., Keultjes G., Kock P., Wilmering J., Weisbeek P.,
RA Smeekens S.;
RT "Identification of a light-regulated MYB gene from an Arabidopsis
RT transcription factor gene collection.";
RL Plant Mol. Biol. 32:987-993(1996).
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=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 [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=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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=12857823; DOI=10.1104/pp.102.019273;
RA Denekamp M., Smeekens S.C.;
RT "Integration of wounding and osmotic stress signals determines the
RT expression of the AtMYB102 transcription factor gene.";
RL Plant Physiol. 132:1415-1423(2003).
RN [8]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19517001; DOI=10.4161/psb.1.6.3512;
RA De Vos M., Denekamp M., Dicke M., Vuylsteke M., Van Loon L., Smeekens S.C.,
RA Pieterse C.M.;
RT "The Arabidopsis thaliana transcription factor AtMYB102 functions in
RT defense against the insect herbivore Pieris rapae.";
RL Plant Signal. Behav. 1:305-311(2006).
CC -!- FUNCTION: Probable transcription factor that may function in osmotic
CC stress and wounding signaling pathways (Probable). Contributes to basal
CC resistance against the herbivore Pieris rapae (white cabbage butterfly)
CC feeding (PubMed:19517001). {ECO:0000269|PubMed:19517001,
CC ECO:0000305|PubMed:12857823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, cauline leaves and
CC flowers. {ECO:0000269|PubMed:8980549}.
CC -!- INDUCTION: Induced by light (PubMed:8980549). Induced by wounding, salt
CC stress and abscisic acid (PubMed:12857823). Induced by the lepidopteran
CC herbivore Pieris rapae (white cabbage butterfly) feeding
CC (PubMed:19517001). {ECO:0000269|PubMed:12857823,
CC ECO:0000269|PubMed:19517001, ECO:0000269|PubMed:8980549}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plant show increased susceptibility to the
CC herbivore Pieris rapae (white cabbage butterfly) feeding.
CC {ECO:0000269|PubMed:19517001}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18708.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA20209.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81251.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X90381; CAB77384.1; -; Genomic_DNA.
DR EMBL; X90382; CAB81661.1; -; mRNA.
DR EMBL; AY519607; AAS10077.1; -; mRNA.
DR EMBL; AL022603; CAA18708.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031187; CAA20209.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84451.1; -; Genomic_DNA.
DR EMBL; AY062619; AAL32697.1; -; mRNA.
DR EMBL; BT001235; AAN65122.1; -; mRNA.
DR EMBL; AY087252; AAM64808.1; -; mRNA.
DR PIR; T05152; S58293.
DR RefSeq; NP_567626.1; NM_118264.3.
DR AlphaFoldDB; Q9LDR8; -.
DR SMR; Q9LDR8; -.
DR STRING; 3702.AT4G21440.1; -.
DR PaxDb; Q9LDR8; -.
DR PRIDE; Q9LDR8; -.
DR EnsemblPlants; AT4G21440.1; AT4G21440.1; AT4G21440.
DR GeneID; 826916; -.
DR Gramene; AT4G21440.1; AT4G21440.1; AT4G21440.
DR KEGG; ath:AT4G21440; -.
DR Araport; AT4G21440; -.
DR TAIR; locus:2141231; AT4G21440.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_15_2_1; -.
DR InParanoid; Q9LDR8; -.
DR OMA; CTTEDEM; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9LDR8; -.
DR PRO; PR:Q9LDR8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LDR8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; 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 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Plant defense; Reference proteome; Repeat;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..350
FT /note="Transcription factor MYB102"
FT /id="PRO_0000439656"
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 CONFLICT 19
FT /note="S -> F (in Ref. 5; AAL32697)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> D (in Ref. 6; AAM64808)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> H (in Ref. 6; AAM64808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 40167 MW; 63D8508DAC1E636E CRC64;
MARSPCCEKN GLKKGPWTSE EDQKLVDYIQ KHGYGNWRTL PKNAGLQRCG KSCRLRWTNY
LRPDIKRGRF SFEEEETIIQ LHSFLGNKWS AIAARLPGRT DNEIKNFWNT HIRKKLLRMG
IDPVTHSPRL DLLDISSILA SSLYNSSSHH MNMSRLMMDT NRRHHQQHPL VNPEILKLAT
SLFSQNQNQN LVVDHDSRTQ EKQTVYSQTG VNQYQTNQYF ENTITQELQS SMPPFPNEAR
QFNNMDHHFN GFGEQNLVST STTSVQDCYN PSFNDYSSSN FVLDPSYSDQ SFNFANSVLN
TPSSSPSPTT LNSSYINSSS CSTEDEIESY CSNLMKFDIP DFLDVNGFII
