TT8_ARATH
ID TT8_ARATH Reviewed; 518 AA.
AC Q9FT81; A0MF61; Q1PEA5; Q9SZ97;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Transcription factor TT8;
DE AltName: Full=Basic helix-loop-helix protein 42;
DE Short=AtbHLH42;
DE Short=bHLH 42;
DE AltName: Full=Protein TRANSPARENT TESTA 8;
DE AltName: Full=Transcription factor EN 32;
DE AltName: Full=bHLH transcription factor bHLH042;
GN Name=TT8; Synonyms=BHLH42, EN32; OrderedLocusNames=At4g09820;
GN ORFNames=F17A8.170;
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], VARIANT TYR-307, AND MUTANT TT8-1.
RC STRAIN=cv. Columbia, cv. En-2, and cv. Wassilewskija-2; TISSUE=Silique;
RX PubMed=11041882; DOI=10.2307/3871198;
RA Nesi N., Debeaujon I., Jond C., Pelletier G., Caboche M., Lepiniec L.;
RT "The TT8 gene encodes a basic helix-loop-helix domain protein required for
RT expression of DFR and BAN genes in Arabidopsis siliques.";
RL Plant Cell 12:1863-1878(2000).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-458, TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH MYB75; MYB90; MYB4; MYB5; MYB6; MYB82;
RP MYB113; MYB114 AND TT2.
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).
CC -!- FUNCTION: Transcription activator, when associated with MYB75/PAP1 or
CC MYB90/PAP2. Involved in the control of flavonoid pigmentation. Plays a
CC key role in regulating leucoanthocyanidin reductase (BANYULS) and
CC dihydroflavonol-4-reductase (DFR). Not required for leucoanthocyanidin
CC dioxygenase (LDOX) expression. {ECO:0000269|PubMed:15361138}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with MYB4, MYB5, MYB6, MYB82,
CC MYB113, MYB114, MYB75/PAP1, MYB90/PAP2, and TT2.
CC {ECO:0000269|PubMed:15361138, ECO:0000305}.
CC -!- INTERACTION:
CC Q9FT81; Q9C9A5: ARABIDOPSIS MYB-LIKE 2; NbExp=3; IntAct=EBI-395790, EBI-1546577;
CC Q9FT81; Q9FNV8: MYB114; NbExp=3; IntAct=EBI-395790, EBI-1546262;
CC Q9FT81; Q9FE25: MYB75; NbExp=5; IntAct=EBI-395790, EBI-1545177;
CC Q9FT81; Q9ZTC3: MYB90; NbExp=2; IntAct=EBI-395790, EBI-1545203;
CC Q9FT81; Q9FJA2: TT2; NbExp=5; IntAct=EBI-395790, EBI-395778;
CC Q9FT81; Q9XGN1: TTG1; NbExp=5; IntAct=EBI-395790, EBI-395803;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Buds, flowers and developing siliques, but not in
CC leaves, stems and roots. {ECO:0000269|PubMed:12679534}.
CC -!- DEVELOPMENTAL STAGE: Faint expression in buds and flowers. Increases
CC during the very early stages of seed development, reaches a maximum at
CC the globular embryo stage and stays high throughout seed formation.
CC -!- MISCELLANEOUS: TT8 might interact with TT2 and TTG1 to modulate the
CC late genes of the flavonoid pathway.
CC -!- SIMILARITY: Belongs to the bHLH protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28624.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB39649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ277509; CAC14865.1; -; mRNA.
DR EMBL; AL049482; CAB39649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161516; CAB78105.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82802.1; -; Genomic_DNA.
DR EMBL; DQ446813; ABE66051.1; -; mRNA.
DR EMBL; DQ653187; ABK28624.1; ALT_SEQ; mRNA.
DR RefSeq; NP_192720.2; NM_117050.3.
DR AlphaFoldDB; Q9FT81; -.
DR SMR; Q9FT81; -.
DR BioGRID; 11870; 15.
DR IntAct; Q9FT81; 13.
DR STRING; 3702.AT4G09820.1; -.
DR PaxDb; Q9FT81; -.
DR PRIDE; Q9FT81; -.
DR ProteomicsDB; 234598; -.
DR EnsemblPlants; AT4G09820.1; AT4G09820.1; AT4G09820.
DR GeneID; 826571; -.
DR Gramene; AT4G09820.1; AT4G09820.1; AT4G09820.
DR KEGG; ath:AT4G09820; -.
DR Araport; AT4G09820; -.
DR TAIR; locus:2118524; AT4G09820.
DR eggNOG; ENOG502QT7W; Eukaryota.
DR HOGENOM; CLU_023211_1_1_1; -.
DR InParanoid; Q9FT81; -.
DR OMA; VCIPVVD; -.
DR OrthoDB; 547309at2759; -.
DR PhylomeDB; Q9FT81; -.
DR PRO; PR:Q9FT81; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FT81; baseline and differential.
DR Genevisible; Q9FT81; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0031542; P:positive regulation of anthocyanin biosynthetic process; IMP:TAIR.
DR GO; GO:0009962; P:regulation of flavonoid biosynthetic process; TAS:TAIR.
DR GO; GO:2000029; P:regulation of proanthocyanidin biosynthetic process; IEP:TAIR.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR025610; MYC/MYB_N.
DR Pfam; PF14215; bHLH-MYC_N; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; DNA-binding; Flavonoid biosynthesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..518
FT /note="Transcription factor TT8"
FT /id="PRO_0000127431"
FT DOMAIN 359..408
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT COILED 220..240
FT /evidence="ECO:0000255"
FT COILED 405..428
FT /evidence="ECO:0000255"
FT VARIANT 307
FT /note="S -> Y (in strain: cv. Wassilewskija-2)"
FT /evidence="ECO:0000269|PubMed:11041882"
FT MUTAGEN 268
FT /note="L->LDIYIYPKLLIFCGFISLYLRNYHLYIYV: In tt8-1; loss of
FT seed pigmentation."
SQ SEQUENCE 518 AA; 59198 MW; 25988482FE25C99C CRC64;
MDESSIIPAE KVAGAEKKEL QGLLKTAVQS VDWTYSVFWQ FCPQQRVLVW GNGYYNGAIK
TRKTTQPAEV TAEEAALERS QQLRELYETL LAGESTSEAR ACTALSPEDL TETEWFYLMC
VSFSFPPPSG MPGKAYARRK HVWLSGANEV DSKTFSRAIL AKSAKIQTVV CIPMLDGVVE
LGTTKKVRED VEFVELTKSF FYDHCKTNPK PALSEHSTYE VHEEAEDEEE VEEEMTMSEE
MRLGSPDDED VSNQNLHSDL HIESTHTLDT HMDMMNLMEE GGNYSQTVTT LLMSHPTSLL
SDSVSTSSYI QSSFATWRVE NGKEHQQVKT APSSQWVLKQ MIFRVPFLHD NTKDKRLPRE
DLSHVVAERR RREKLNEKFI TLRSMVPFVT KMDKVSILGD TIAYVNHLRK RVHELENTHH
EQQHKRTRTC KRKTSEEVEV SIIENDVLLE MRCEYRDGLL LDILQVLHEL GIETTAVHTS
VNDHDFEAEI RAKVRGKKAS IAEVKRAIHQ VIIHDTNL
