STKLS_ARATH
ID STKLS_ARATH Reviewed; 368 AA.
AC Q9SB42; Q8H0X7; Q94F05;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=GLABROUS1 enhancer-binding protein-like {ECO:0000303|PubMed:25877331};
DE AltName: Full=Mediator-associated protein 1 {ECO:0000303|PubMed:17560376};
DE AltName: Full=Protein GeBPL {ECO:0000303|PubMed:25877331};
DE AltName: Full=Storekeeper-like protein At4g25210 {ECO:0000305};
DE AltName: Full=Transcription factor At4g25210 {ECO:0000305};
GN Name=GEBPL {ECO:0000303|PubMed:25877331};
GN OrderedLocusNames=At4g25210 {ECO:0000312|Araport:AT4G25210};
GN ORFNames=F24A6.50 {ECO:0000312|EMBL:CAA23062.1};
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 [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND INTERACTION WITH MED6.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [7]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH MED10A; MED28 AND MED32, AND
RP MUTAGENESIS OF CYS-175; CYS-310 AND CYS-348.
RX PubMed=25877331; DOI=10.1042/bj20150132;
RA Shaikhali J., Davoine C., Braennstroem K., Rouhier N., Bygdell J.,
RA Bjoerklund S., Wingsle G.;
RT "Biochemical and redox characterization of the mediator complex and its
RT associated transcription factor GeBPL, a GLABROUS1 enhancer binding
RT protein.";
RL Biochem. J. 468:385-400(2015).
RN [9]
RP GENE FAMILY.
RX PubMed=27031427; DOI=10.1016/j.plaphy.2016.03.029;
RA Chung M.S., Lee S., Min J.H., Huang P., Ju H.W., Kim C.S.;
RT "Regulation of Arabidopsis thaliana plasma membrane glucose-responsive
RT regulator (AtPGR) expression by A. thaliana storekeeper-like transcription
RT factor, AtSTKL, modulates glucose response in Arabidopsis.";
RL Plant Physiol. Biochem. 104:155-164(2016).
CC -!- FUNCTION: Transcription factor that binds promoters containing the
CC CryR2 element, 5'-ACATAWCT-3' (PubMed:25877331). The DNA-binding
CC activity is decreased upon direct physical interaction with the
CC mediator subunits and is modulated by redox conditions
CC (PubMed:25877331). The oxidized protein is the preferential binding
CC form (PubMed:25877331). {ECO:0000269|PubMed:25877331}.
CC -!- SUBUNIT: Mono-, di- and oligomers (PubMed:25877331). Associated with
CC the Mediator complex (PubMed:17560376). Interacts with MED6
CC (PubMed:17560376). Interacts with MED10A, MED28 and MED32
CC (PubMed:25877331). Interacts with DEK3 (PubMed:25387881).
CC {ECO:0000269|PubMed:17560376, ECO:0000269|PubMed:25387881,
CC ECO:0000269|PubMed:25877331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GeBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AL035396; CAA23062.1; -; Genomic_DNA.
DR EMBL; AL161562; CAB79430.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85025.1; -; Genomic_DNA.
DR EMBL; AF325095; AAK17163.1; -; mRNA.
DR EMBL; AF386996; AAK62441.1; ALT_INIT; mRNA.
DR EMBL; BT001181; AAN65068.1; -; mRNA.
DR EMBL; AB493698; BAH30536.1; -; mRNA.
DR PIR; T05542; T05542.
DR RefSeq; NP_194251.1; NM_118653.4.
DR AlphaFoldDB; Q9SB42; -.
DR SMR; Q9SB42; -.
DR BioGRID; 13911; 4.
DR IntAct; Q9SB42; 4.
DR STRING; 3702.AT4G25210.1; -.
DR iPTMnet; Q9SB42; -.
DR PaxDb; Q9SB42; -.
DR PRIDE; Q9SB42; -.
DR ProteomicsDB; 228353; -.
DR EnsemblPlants; AT4G25210.1; AT4G25210.1; AT4G25210.
DR GeneID; 828624; -.
DR Gramene; AT4G25210.1; AT4G25210.1; AT4G25210.
DR KEGG; ath:AT4G25210; -.
DR Araport; AT4G25210; -.
DR TAIR; locus:2122659; AT4G25210.
DR eggNOG; ENOG502RQE9; Eukaryota.
DR HOGENOM; CLU_856181_0_0_1; -.
DR InParanoid; Q9SB42; -.
DR OMA; IDAFCIY; -.
DR OrthoDB; 1137098at2759; -.
DR PhylomeDB; Q9SB42; -.
DR PRO; PR:Q9SB42; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB42; baseline and differential.
DR Genevisible; Q9SB42; AT.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
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 Nucleus; Reference proteome.
FT CHAIN 1..368
FT /note="GLABROUS1 enhancer-binding protein-like"
FT /id="PRO_0000419196"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 175
FT /note="C->S: Decreased DNA binding; when associated with S-
FT 310 or S-348. Loss of DNA binding; when associated with S-
FT 348 or S-310 and S-348."
FT /evidence="ECO:0000269|PubMed:25877331"
FT MUTAGEN 310
FT /note="C->S: Decreased DNA binding; when associated with S-
FT 175. Loss of DNA binding; when associated with S-348 or S-
FT 175 and S-348."
FT /evidence="ECO:0000269|PubMed:25877331"
FT MUTAGEN 348
FT /note="C->S: Decreased DNA binding; when associated with S-
FT 175. Loss of DNA binding; when associated with S-310 or S-
FT 175 and S-310."
FT /evidence="ECO:0000269|PubMed:25877331"
FT CONFLICT 221
FT /note="F -> S (in Ref. 3; AAK62441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40274 MW; 52B8EF99109BC8E4 CRC64;
MAPKKAEEVV ESPPVSSEEE ESGSSGEESE SSAEVPKKVE SSQKPESDSE GESESESSSG
PEPESEPAKT IKLKPVGTKP IPETSGSAAT VPESSTAKRP LKEAAPEAIK KQKTSDTEHV
KKPITNDEVK KISSEDAKKM FQRLFSETDE IALLQGIIDF TSTKGDPYED IDAFCIYVKK
LIDFDATKNQ IVTKLQRLKK KFNNAVKNSL KKGKTEDDIE FAKDLEQKGF ELSRKIWGSN
GVLVTGKSSR KKVGGTPAPK EMKLVAHSTP KKQQEEAKKP ERTEAKVVNT GLSIGKEIAS
FLNADNGSSC GLDESTLTAV WAKVADGAEK REVEEKWKKL KAKQFELCLQ RSGLVNETAK
MIFKAYES
