TCP2_ARATH
ID TCP2_ARATH Reviewed; 365 AA.
AC Q93V43; O49509; O81384; Q8LGF2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transcription factor TCP2 {ECO:0000303|PubMed:10363373};
DE AltName: Full=Protein TEOSINTE BRANCHED 1 {ECO:0000303|PubMed:17307924};
DE AltName: Full=Protein TEOSINTE-LIKE1, CYCLOIDEA, and PROLIFERATING CELL FACTOR 2 {ECO:0000303|PubMed:10363373};
GN Name=TCP2 {ECO:0000303|PubMed:10363373};
GN Synonyms=BRC1 {ECO:0000303|PubMed:17307924};
GN OrderedLocusNames=At4g18390 {ECO:0000312|Araport:AT4G18390};
GN ORFNames=F28J12.50 {ECO:0000312|EMBL:CAA16719.1};
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 [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 [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].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-365.
RA Doebley J., Stec A., Lauter N.;
RT "Arabidopsis EST (Accession R30409) with homology to teosinte branched.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-365.
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=10363373; DOI=10.1046/j.1365-313x.1999.00444.x;
RA Cubas P., Lauter N., Doebley J., Coen E.;
RT "The TCP domain: a motif found in proteins regulating plant growth and
RT development.";
RL Plant J. 18:215-222(1999).
RN [7]
RP FUNCTION, AND INDUCTION BY MIR-JAW.
RX PubMed=12931144; DOI=10.1038/nature01958;
RA Palatnik J.F., Allen E., Wu X., Schommer C., Schwab R., Carrington J.C.,
RA Weigel D.;
RT "Control of leaf morphogenesis by microRNAs.";
RL Nature 425:257-263(2003).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17307924; DOI=10.1105/tpc.106.048934;
RA Aguilar-Martinez J.A., Poza-Carrion C., Cubas P.;
RT "Arabidopsis BRANCHED1 acts as an integrator of branching signals within
RT axillary buds.";
RL Plant Cell 19:458-472(2007).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17307931; DOI=10.1105/tpc.106.044792;
RA Koyama T., Furutani M., Tasaka M., Ohme-Takagi M.;
RT "TCP transcription factors control the morphology of shoot lateral organs
RT via negative regulation of the expression of boundary-specific genes in
RT Arabidopsis.";
RL Plant Cell 19:473-484(2007).
RN [10]
RP INTERACTION WITH SPL.
RX PubMed=25527103; DOI=10.1016/j.jgg.2014.08.009;
RA Chen G.H., Sun J.Y., Liu M., Liu J., Yang W.C.;
RT "SPOROCYTELESS is a novel embryophyte-specific transcription repressor that
RT interacts with TPL and TCP proteins in Arabidopsis.";
RL J. Genet. Genomics 41:617-625(2014).
RN [11]
RP FUNCTION, INTERACTION WITH SPL, AND DEVELOPMENTAL STAGE.
RX PubMed=25378179; DOI=10.1038/cr.2014.145;
RA Wei B., Zhang J., Pang C., Yu H., Guo D., Jiang H., Ding M., Chen Z.,
RA Tao Q., Gu H., Qu L.J., Qin G.;
RT "The molecular mechanism of sporocyteless/nozzle in controlling Arabidopsis
RT ovule development.";
RL Cell Res. 25:121-134(2015).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CRY1, AND INDUCTION BY
RP BLUE LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=26596765; DOI=10.1093/jxb/erv495;
RA He Z., Zhao X., Kong F., Zuo Z., Liu X.;
RT "TCP2 positively regulates HY5/HYH and photomorphogenesis in Arabidopsis.";
RL J. Exp. Bot. 67:775-785(2015).
CC -!- FUNCTION: Plays a pivotal role in the control of morphogenesis of shoot
CC organs by negatively regulating the expression of boundary-specific
CC genes such as CUC genes, probably through the induction of miRNA (e.g.
CC miR164). Participates in ovule develpment (PubMed:25378179).
CC Participates in ovule develpment (PubMed:25378179). Promotes light-
CC regulated transcription of CHS, CAB, HYH and HY5. Regulates positively
CC photomorphogenesis (e.g. hypocotyl elongation inhibition and cotyledon
CC opening in response to blue light) (PubMed:26596765).
CC {ECO:0000269|PubMed:12931144, ECO:0000269|PubMed:17307931,
CC ECO:0000269|PubMed:25378179, ECO:0000269|PubMed:26596765}.
CC -!- SUBUNIT: Interacts with SPL (PubMed:25378179, PubMed:25527103).
CC Interacts with CRY1 (PubMed:26596765). {ECO:0000269|PubMed:25378179,
CC ECO:0000269|PubMed:25527103, ECO:0000269|PubMed:26596765}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, particularly in the
CC vascular region, in leaves, roots, buds, flowers and immature siliques.
CC {ECO:0000269|PubMed:17307931}.
CC -!- DEVELOPMENTAL STAGE: During flower development, first observed
CC throughout the floral meristem. Later expressed in rapidly growing
CC floral primordia. Detected to a lower extent in vegetative primordia.
CC During flower development, first observed throughout the floral
CC meristem. Expressed during ovule development (PubMed:25378179).
CC {ECO:0000269|PubMed:10363373, ECO:0000269|PubMed:25378179}.
CC -!- INDUCTION: Repressed by the miRNA miR-JAW (PubMed:12931144). Induced by
CC blue light. Stabilized by light but labile in darkness due to
CC proteasome-dependent proteolysis (at protein level) (PubMed:26596765).
CC {ECO:0000269|PubMed:12931144, ECO:0000269|PubMed:26596765}.
CC -!- DISRUPTION PHENOTYPE: Reduced light-mediated transcription of CHS, CAB,
CC HYH and HY5. Impaired influence of blue light on hypocotyl elongation.
CC {ECO:0000269|PubMed:26596765}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16719.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78841.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL021710; CAA16719.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161548; CAB78841.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84039.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84040.1; -; Genomic_DNA.
DR EMBL; AF367270; AAK56259.1; -; mRNA.
DR EMBL; AF367292; AAK56280.1; -; mRNA.
DR EMBL; AY102141; AAM26708.1; -; mRNA.
DR EMBL; AF072691; AAC26786.1; -; mRNA.
DR EMBL; AY084306; AAM67351.1; -; mRNA.
DR PIR; T04535; T04535.
DR PIR; T52249; T52249.
DR RefSeq; NP_001078407.1; NM_001084938.1.
DR RefSeq; NP_567553.1; NM_117950.5.
DR AlphaFoldDB; Q93V43; -.
DR SMR; Q93V43; -.
DR BioGRID; 12861; 160.
DR IntAct; Q93V43; 134.
DR STRING; 3702.AT4G18390.1; -.
DR PaxDb; Q93V43; -.
DR PRIDE; Q93V43; -.
DR ProteomicsDB; 234150; -.
DR EnsemblPlants; AT4G18390.1; AT4G18390.1; AT4G18390.
DR EnsemblPlants; AT4G18390.2; AT4G18390.2; AT4G18390.
DR GeneID; 827568; -.
DR Gramene; AT4G18390.1; AT4G18390.1; AT4G18390.
DR Gramene; AT4G18390.2; AT4G18390.2; AT4G18390.
DR KEGG; ath:AT4G18390; -.
DR Araport; AT4G18390; -.
DR TAIR; locus:2124539; AT4G18390.
DR eggNOG; ENOG502QQFU; Eukaryota.
DR HOGENOM; CLU_036572_0_0_1; -.
DR InParanoid; Q93V43; -.
DR OMA; HQEFSFV; -.
DR OrthoDB; 1110972at2759; -.
DR PhylomeDB; Q93V43; -.
DR PRO; PR:Q93V43; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93V43; baseline and differential.
DR Genevisible; Q93V43; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:1903508; P:positive regulation of nucleic acid-templated transcription; IDA:UniProtKB.
DR GO; GO:2000306; P:positive regulation of photomorphogenesis; IMP:UniProtKB.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009637; P:response to blue light; IEP:UniProtKB.
DR InterPro; IPR017888; CYC/TB1_R_domain.
DR InterPro; IPR017887; TF_TCP_subgr.
DR InterPro; IPR005333; Transcription_factor_TCP.
DR PANTHER; PTHR31072; PTHR31072; 1.
DR Pfam; PF03634; TCP; 1.
DR PROSITE; PS51370; R; 1.
DR PROSITE; PS51369; TCP; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..365
FT /note="Transcription factor TCP2"
FT /id="PRO_0000330776"
FT DOMAIN 42..100
FT /note="TCP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00701"
FT DOMAIN 151..172
FT /note="R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00702"
FT REGION 130..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 150
FT /note="R -> S (in Ref. 4; AAC26786)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="Missing (in Ref. 4; AAC26786)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="E -> D (in Ref. 4; AAC26786 and 5; AAM67351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40179 MW; F88BF7B73C4B17D6 CRC64;
MIGDLMKNNN NGDVVDNEVN NRLSRWHHNS SRIIRVSRAS GGKDRHSKVL TSKGPRDRRV
RLSVSTALQF YDLQDRLGYD QPSKAVEWLI KAAEDSISEL PSLNNTHFPT DDENHQNQTL
TTVAANSLSK SACSSNSDTS KNSSGLSLSR SELRDKARER ARERTAKETK ERDHNHTSFT
DLLNSGSDPV NSNRQWMASA PSSSPMEYFS SGLILGSGQQ THFPISTNSH PFSSISDHHH
HHPHHQHQEF SFVPDHLISP AESNGGAFNL DFNMSTPSGA GAAVSAASGG GFSGFNRGTL
QSNSTNQHQS FLANLQRFPT SESGGGPQFL FGALPAENHH HNHQFQLYYE NGCRNSSEHK
GKGKN
