GTL1_ARATH
ID GTL1_ARATH Reviewed; 587 AA.
AC Q9C882; O48590; O48591; Q7FPN7; Q8L6Y5; Q9LP25;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Trihelix transcription factor GTL1 {ECO:0000303|PubMed:19717615};
DE AltName: Full=GT2-LIKE protein 1 {ECO:0000303|PubMed:9501260};
DE Short=AtGTL1 {ECO:0000303|PubMed:9501260};
DE Short=Protein GT-2-LIKE1 {ECO:0000303|PubMed:19717615};
DE AltName: Full=Trihelix DNA-binding protein GTL1 {ECO:0000305};
GN Name=GTL1 {ECO:0000303|PubMed:19717615};
GN OrderedLocusNames=At1g33240 {ECO:0000312|Araport:AT1G33240};
GN ORFNames=T16O9.10 {ECO:0000312|EMBL:AAG51283.1},
GN T9L6.10 {ECO:0000312|EMBL:AAF97353.1};
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], NUCLEOTIDE SEQUENCE [MRNA] OF 66-498
RP (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9501260; DOI=10.1073/pnas.95.6.3318;
RA Smalle J.A.H., Kurepa J., Haegman M., Gielen J., Van Montagu M.,
RA Van Der Straeten D.;
RT "The trihelix DNA-binding motif in higher plants is not restricted to the
RT transcription factors GT-1 and GT-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3318-3322(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 2).
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19717615; DOI=10.1105/tpc.109.068387;
RA Breuer C., Kawamura A., Ichikawa T., Tominaga-Wada R., Wada T., Kondou Y.,
RA Muto S., Matsui M., Sugimoto K.;
RT "The trihelix transcription factor GTL1 regulates ploidy-dependent cell
RT growth in the Arabidopsis trichome.";
RL Plant Cell 21:2307-2322(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION BY WATER STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=21169508; DOI=10.1105/tpc.110.078691;
RA Yoo C.Y., Pence H.E., Jin J.B., Miura K., Gosney M.J., Hasegawa P.M.,
RA Mickelbart M.V.;
RT "The Arabidopsis GTL1 transcription factor regulates water use efficiency
RT and drought tolerance by modulating stomatal density via transrepression of
RT SDD1.";
RL Plant Cell 22:4128-4141(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29439132; DOI=10.1242/dev.159707;
RA Shibata M., Breuer C., Kawamura A., Clark N.M., Rymen B., Braidwood L.,
RA Morohashi K., Busch W., Benfey P.N., Sozzani R., Sugimoto K.;
RT "GTL1 and DF1 regulate root hair growth through transcriptional repression
RT of ROOT HAIR DEFECTIVE 6-LIKE 4 in Arabidopsis.";
RL Development 145:0-0(2018).
CC -!- FUNCTION: Transcription repressor that binds specific DNA sequence such
CC as GT3 box 5'-GGTAAA-3' in the SDD1 promoter (PubMed:21169508).
CC Negative regulator of water use efficiency (WUE) via the promotion of
CC stomatal density and distribution by the transcription repression of
CC SDD1 (PubMed:21169508). Regulates the expression of several cell cycle
CC genes and endoreduplication, especially in trichomes where it prevents
CC ploidy-dependent plant cell growth (PubMed:19717615). Regulates
CC negatively root hair growth by directly binding RSL4 promoter and
CC repressing RSL4 expression (PubMed:29439132).
CC {ECO:0000269|PubMed:19717615, ECO:0000269|PubMed:21169508,
CC ECO:0000269|PubMed:29439132}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19717615,
CC ECO:0000269|PubMed:21169508, ECO:0000269|PubMed:29439132}. Note=Present
CC within the nucleus during the postbranching stages of trichome
CC development. {ECO:0000269|PubMed:19717615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C882-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C882-2; Sequence=VSP_040713;
CC Name=3;
CC IsoId=Q9C882-3; Sequence=VSP_040714;
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques, and, to a lower
CC extent, in growing root hairs, leaves, stems, and flowers
CC (PubMed:9501260). Present in abaxial epidermal cells, predominantly in
CC guard cells, pavement cells, and meristemoids (PubMed:21169508).
CC {ECO:0000269|PubMed:21169508, ECO:0000269|PubMed:9501260}.
CC -!- INDUCTION: Down-regulated by water stress.
CC {ECO:0000269|PubMed:21169508}.
CC -!- DISRUPTION PHENOTYPE: Increased water deficit tolerance and higher
CC integrated water use efficiency (WUE) by reducing daytime transpiration
CC associated with a higher expression of SDD1 (PubMed:21169508).
CC Increased trichome cell size with normal patterning and branching
CC accompanied with an increase in the nuclear DNA content only in
CC trichomes that have completed branching (PubMed:19717615). No visible
CC phenotype under normal growth conditions, but the double mutant
CC seedlings gtl1-1 and df1-1 exhibit increased root hair length
CC (PubMed:29439132). {ECO:0000269|PubMed:19717615,
CC ECO:0000269|PubMed:21169508, ECO:0000269|PubMed:29439132}.
CC -!- MISCELLANEOUS: Plants overexpressing GTL1 fail to develop root hairs.
CC {ECO:0000269|PubMed:29439132}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA05995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA05996.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AJ003215; CAA05995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ003216; CAA05996.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ003218; CAA05998.1; -; mRNA.
DR EMBL; AC021045; AAF97353.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC027035; AAG51283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31573.1; -; Genomic_DNA.
DR EMBL; AY140085; AAM98226.1; -; mRNA.
DR EMBL; BT008824; AAP68263.1; -; mRNA.
DR PIR; B86456; B86456.
DR RefSeq; NP_001322396.1; NM_001333032.1.
DR RefSeq; NP_174594.1; NM_103052.4. [Q9C882-3]
DR AlphaFoldDB; Q9C882; -.
DR SMR; Q9C882; -.
DR BioGRID; 25452; 11.
DR IntAct; Q9C882; 9.
DR STRING; 3702.AT1G33240.1; -.
DR iPTMnet; Q9C882; -.
DR PaxDb; Q9C882; -.
DR PeptideAtlas; Q9C882; -.
DR PRIDE; Q9C882; -.
DR ProteomicsDB; 247201; -. [Q9C882-1]
DR EnsemblPlants; AT1G33240.1; AT1G33240.1; AT1G33240. [Q9C882-3]
DR EnsemblPlants; AT1G33240.3; AT1G33240.3; AT1G33240.
DR GeneID; 840218; -.
DR Gramene; AT1G33240.1; AT1G33240.1; AT1G33240. [Q9C882-3]
DR Gramene; AT1G33240.3; AT1G33240.3; AT1G33240.
DR KEGG; ath:AT1G33240; -.
DR Araport; AT1G33240; -.
DR TAIR; locus:2196663; AT1G33240.
DR eggNOG; KOG4282; Eukaryota.
DR HOGENOM; CLU_013796_1_0_1; -.
DR InParanoid; Q9C882; -.
DR OMA; DEIWREP; -.
DR OrthoDB; 782634at2759; -.
DR PhylomeDB; Q9C882; -.
DR PRO; PR:Q9C882; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C882; baseline and differential.
DR Genevisible; Q9C882; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:TAIR.
DR GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:TAIR.
DR GO; GO:2000037; P:regulation of stomatal complex patterning; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF13837; Myb_DNA-bind_4; 2.
DR SMART; SM00717; SANT; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..587
FT /note="Trihelix transcription factor GTL1"
FT /id="PRO_0000405798"
FT DOMAIN 55..119
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 434..492
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..328
FT /evidence="ECO:0000255"
FT MOTIF 96..103
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 472..479
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 173..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 151..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040713"
FT VAR_SEQ 585..587
FT /note="KTL -> PEDLVMRELIQQQQQLQQQESMIGEYEKIEESHNYNNMEEEEDQE
FT MDEEELDEDEKSAAFEIAFQSPANRGGNGHTEPPFLTMVQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040714"
FT CONFLICT 70
FT /note="A -> V (in Ref. 1; CAA05995/CAA05996/CAA05998)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9C882-3:650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 587 AA; 64612 MW; 3C7CA27D8031CD53 CRC64;
MEQGGGGGGN EVVEEASPIS SRPPANNLEE LMRFSAAADD GGLGGGGGGG GGGSASSSSG
NRWPREETLA LLRIRSDMDS TFRDATLKAP LWEHVSRKLL ELGYKRSSKK CKEKFENVQK
YYKRTKETRG GRHDGKAYKF FSQLEALNTT PPSSSLDVTP LSVANPILMP SSSSSPFPVF
SQPQPQTQTQ PPQTHNVSFT PTPPPLPLPS MGPIFTGVTF SSHSSSTASG MGSDDDDDDM
DVDQANIAGS SSRKRKRGNR GGGGKMMELF EGLVRQVMQK QAAMQRSFLE ALEKREQERL
DREEAWKRQE MARLAREHEV MSQERAASAS RDAAIISLIQ KITGHTIQLP PSLSSQPPPP
YQPPPAVTKR VAEPPLSTAQ SQSQQPIMAI PQQQILPPPP PSHPHAHQPE QKQQQQPQQE
MVMSSEQSSL PSSSRWPKAE ILALINLRSG MEPRYQDNVP KGLLWEEIST SMKRMGYNRN
AKRCKEKWEN INKYYKKVKE SNKKRPQDAK TCPYFHRLDL LYRNKVLGSG GGSSTSGLPQ
DQKQSPVTAM KPPQEGLVNV QQTHGSASTE EEEPIEESPQ GTEKKTL
