STKLO_ARATH
ID STKLO_ARATH Reviewed; 302 AA.
AC Q9ASZ1; O23075;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=GLABROUS1 enhancer-binding protein {ECO:0000303|PubMed:12535344};
DE AltName: Full=Probable transcription factor At4g00270 {ECO:0000305};
DE AltName: Full=Protein GeBP {ECO:0000303|PubMed:12535344};
DE AltName: Full=Protein STOREKEEPER RELATED 1 {ECO:0000303|PubMed:29192025};
DE AltName: Full=Storekeeper-like protein At4g00270 {ECO:0000305};
GN Name=GEBP {ECO:0000303|PubMed:12535344};
GN Synonyms=STKR1 {ECO:0000303|PubMed:29192025};
GN OrderedLocusNames=At4g00270 {ECO:0000312|Araport:AT4G00270};
GN ORFNames=F5I10.11 {ECO:0000312|EMBL:AAF02789.1};
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP INDUCTION BY KNAT1, LACK OF INDUCTION BY GIBBERELLINS, AND GENE FAMILY.
RX PubMed=12535344; DOI=10.1046/j.1365-313x.2003.01622.x;
RA Curaba J., Herzog M., Vachon G.;
RT "GeBP, the first member of a new gene family in Arabidopsis, encodes a
RT nuclear protein with DNA-binding activity and is regulated by KNAT1.";
RL Plant J. 33:305-317(2003).
RN [5]
RP INTERACTION WITH GPL1; GPL2 AND GPL3, SUBUNIT, MUTAGENESIS OF LEU-256;
RP GLY-263; LEU-270; LEU-277; PHE-284 AND PHE-291, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=18162594; DOI=10.1104/pp.107.110270;
RA Chevalier F., Perazza D., Laporte F., Le Henanff G., Hornitschek P.,
RA Bonneville J.M., Herzog M., Vachon G.;
RT "GeBP and GeBP-like proteins are noncanonical leucine-zipper transcription
RT factors that regulate cytokinin response in Arabidopsis.";
RL Plant Physiol. 146:1142-1154(2008).
RN [6]
RP FUNCTION.
RX PubMed=21875893; DOI=10.1104/pp.111.179804;
RA Perazza D., Laporte F., Balague C., Chevalier F., Remo S., Bourge M.,
RA Larkin J., Herzog M., Vachon G.;
RT "GeBP/GPL transcription factors regulate a subset of CPR5-dependent
RT processes.";
RL Plant Physiol. 157:1232-1242(2011).
RN [7]
RP INTERACTION WITH KIN10; KIN11 AND FLZ4.
RX PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA Nietzsche M., Schiessl I., Boernke F.;
RT "The complex becomes more complex: protein-protein interactions of SnRK1
RT with DUF581 family proteins provide a framework for cell- and stimulus
RT type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:54-54(2014).
RN [8]
RP INTERACTION WITH KIN10; KIN11; GPL1 AND GPL3, SUBUNIT, PHOSPHORYLATION AT
RP SER-27, MUTAGENESIS OF SER-27, AND FUNCTION.
RX PubMed=29192025; DOI=10.1104/pp.17.01461;
RA Nietzsche M., Guerra T., Alseekh S., Wiermer M., Sonnewald S., Fernie A.R.,
RA Boernke F.;
RT "STOREKEEPER RELATED1/G-element binding protein (STKR1) interacts with
RT protein kinase SnRK1.";
RL Plant Physiol. 176:1773-1792(2018).
CC -!- FUNCTION: DNA-binding protein, which specifically recognizes the GL1
CC enhancer sequence (PubMed:12535344). May be involved in leaf initiation
CC (PubMed:12535344). May play redundant roles with GPL1 and GPL2 in
CC cytokinin responses by regulating the transcript levels of type-A ARR
CC response genes (PubMed:18162594). Involved in stress responses
CC (PubMed:21875893). Plays a repressive role in cell expansion by
CC counteracting the positive role of CPR5 in this process, but does not
CC regulate cell proliferation or endoreduplication (PubMed:21875893). May
CC play a role in plant defense (PubMed:29192025).
CC {ECO:0000269|PubMed:12535344, ECO:0000269|PubMed:21875893,
CC ECO:0000269|PubMed:29192025, ECO:0000305|PubMed:18162594}.
CC -!- SUBUNIT: Homo- and heterodimers (PubMed:18162594, PubMed:29192025).
CC Interacts with GPL1, GPL2 and GPL3 (PubMed:18162594). Interacts with
CC KIN10, KIN11 and FLZ4 (PubMed:24600465). Interacts with KIN10 and KIN11
CC via its N-terminal part (PubMed:29192025). Interacts with GPL1 and GPL3
CC via its C-terminal part (PubMed:29192025).
CC {ECO:0000269|PubMed:18162594, ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29192025}.
CC -!- INTERACTION:
CC Q9ASZ1; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-15191723, EBI-15192745;
CC Q9ASZ1; Q9SJM4: GPL3; NbExp=3; IntAct=EBI-15191723, EBI-15199331;
CC Q9ASZ1; Q05153: SSRP1; NbExp=3; IntAct=EBI-15191723, EBI-15191543;
CC Q9ASZ1; Q84JG2: SWI3B; NbExp=3; IntAct=EBI-15191723, EBI-1102271;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12535344}.
CC Nucleus {ECO:0000269|PubMed:18162594}.
CC -!- TISSUE SPECIFICITY: Expressed in the apical meristem and young leaf
CC primordia (PubMed:12535344, PubMed:18162594). Not detected in emerging
CC or mature leaves (PubMed:12535344). Detected in the vascular tissues of
CC cotyledons and leaves, in hydathodes and at the base of flowers and
CC siliques, but not in roots (PubMed:18162594).
CC {ECO:0000269|PubMed:12535344, ECO:0000269|PubMed:18162594}.
CC -!- INDUCTION: Up-regulated by KNAT1. Not regulated by gibberellins.
CC {ECO:0000269|PubMed:12535344}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12535344}.
CC -!- MISCELLANEOUS: Overexpression of GEBP results in a reduced plant
CC growth, a delay in flowering, a reduced anthocyanin accumulation, a
CC delayed senescence and an enhanced resistance toward a virulent strain
CC of the biotrophic oomycete pathogen H.arabidopsidis.
CC {ECO:0000269|PubMed:29192025}.
CC -!- SIMILARITY: Belongs to the GeBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62831.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF02789.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Plant Transcription Factor Database;
CC URL="http://planttfdb.cbi.pku.edu.cn/family.php?sp=Ath&fam=GeBP#family_intro";
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DR EMBL; AF013293; AAB62831.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02789.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81848.1; -; Genomic_DNA.
DR EMBL; AF361590; AAK32758.1; -; mRNA.
DR EMBL; AY074837; AAL69535.1; -; mRNA.
DR PIR; T01544; T01544.
DR RefSeq; NP_567163.1; NM_116248.4.
DR AlphaFoldDB; Q9ASZ1; -.
DR IntAct; Q9ASZ1; 22.
DR STRING; 3702.AT4G00270.1; -.
DR iPTMnet; Q9ASZ1; -.
DR PaxDb; Q9ASZ1; -.
DR PRIDE; Q9ASZ1; -.
DR ProteomicsDB; 228305; -.
DR EnsemblPlants; AT4G00270.1; AT4G00270.1; AT4G00270.
DR GeneID; 827164; -.
DR Gramene; AT4G00270.1; AT4G00270.1; AT4G00270.
DR KEGG; ath:AT4G00270; -.
DR Araport; AT4G00270; -.
DR TAIR; locus:2126031; AT4G00270.
DR eggNOG; ENOG502R1KX; Eukaryota.
DR HOGENOM; CLU_055192_0_0_1; -.
DR InParanoid; Q9ASZ1; -.
DR OMA; DNANQIE; -.
DR OrthoDB; 1137098at2759; -.
DR PhylomeDB; Q9ASZ1; -.
DR PRO; PR:Q9ASZ1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ASZ1; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR007592; GEBP.
DR PANTHER; PTHR31662; PTHR31662; 1.
DR Pfam; PF04504; DUF573; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..302
FT /note="GLABROUS1 enhancer-binding protein"
FT /id="PRO_0000436989"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..291
FT /note="Non-canonical leucine-zipper"
FT /evidence="ECO:0000305|PubMed:18162594"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29192025"
FT MUTAGEN 27
FT /note="S->A: Strongly reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:29192025"
FT MUTAGEN 256
FT /note="L->A: No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:18162594"
FT MUTAGEN 263
FT /note="G->A: No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:18162594"
FT MUTAGEN 270
FT /note="L->A: Loss of dinerization."
FT /evidence="ECO:0000269|PubMed:18162594"
FT MUTAGEN 277
FT /note="L->A: Loss of dinerization."
FT /evidence="ECO:0000269|PubMed:18162594"
FT MUTAGEN 284
FT /note="F->A: Loss of dinerization."
FT /evidence="ECO:0000269|PubMed:18162594"
FT MUTAGEN 291
FT /note="F->A: Loss of dinerization."
FT /evidence="ECO:0000269|PubMed:18162594"
SQ SEQUENCE 302 AA; 34058 MW; 9A266BC06BA3FF95 CRC64;
MVTPKQIDFS SCVGADNSNG TLSHRRSPRN IPSSKRAASV AEEETMKKKM KMKKKKKKLD
PPLIVRIWNE EDELSILKGL VDYRAKTGFN PKIDWDAFCS FLGSSIVERF SKDQVLSKIR
KLKRRFHVHS EKINQGNDPK FTRSSDSEAF GFSSMIWGQG DDDGMDKEHE VNGNGAAENR
TNESGEEMLK EHEEEVANTE LLNENGAAKT TENGTSSGKE RHDEDNDDDD ELCAVQDAFE
AVMSQGLSGY QKKLQLEKLM NLGNGKRREL SDEWKALCVE ETRFNIKKLR FSAKLAEAAN
DS
