YY1_ARATH
ID YY1_ARATH Reviewed; 387 AA.
AC Q2V3L3; Q27GJ7; Q8W3M5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger transcription factor YY1 {ECO:0000303|PubMed:22508367};
DE AltName: Full=Protein YIN YANG 1 {ECO:0000303|PubMed:22508367};
DE Short=AtYY1 {ECO:0000303|PubMed:22508367};
GN Name=YY1 {ECO:0000303|PubMed:22508367};
GN OrderedLocusNames=At4g06634 {ECO:0000312|Araport:AT4G06634};
GN ORFNames=F8H12 {ECO:0000305};
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=11853315; DOI=10.1093/dnares/8.6.285;
RA Kumekawa N., Hosouchi T., Tsuruoka H., Kotani H.;
RT "The size and sequence organization of the centromeric region of
RT Arabidopsis thaliana chromosome 4.";
RL DNA Res. 8:285-290(2001).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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 [4]
RP FUNCTION.
RX PubMed=22508367; DOI=10.1093/abbs/gms020;
RA Wu X., Cheng Y., Li T., Wang Z., Liu J.-Y.;
RT "In vitro identification of DNA-binding motif for the new zinc finger
RT protein AtYY1.";
RL Acta Biochim. Biophys. Sin. 44:483-489(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MED18, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24451981; DOI=10.1038/ncomms4064;
RA Lai Z., Schluttenhofer C.M., Bhide K., Shreve J., Thimmapuram J., Lee S.Y.,
RA Yun D.-J., Mengiste T.;
RT "MED18 interaction with distinct transcription factors regulates multiple
RT plant functions.";
RL Nat. Commun. 5:3064-3064(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT; ABSCISIC ACID; OSMOTIC
RP STRESS; HIGH SALT AND DEHYDRATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=26961720; DOI=10.1016/j.molp.2016.02.010;
RA Li T., Wu X.-Y., Li H., Song J.-H., Liu J.-Y.;
RT "A dual-function transcription factor, AtYY1, is a novel negative regulator
RT of the Arabidopsis ABA response network.";
RL Mol. Plant 9:650-661(2016).
CC -!- FUNCTION: Dual-function transcription factor with both repression and
CC activation activities. Binds to 5'-CCATATT-3' motif in target gene
CC promoters (e.g. ABR1) (PubMed:26961720). Binds also to G-rich DNA motif
CC 5'-GGGGGCAGTGG-3' (PubMed:22508367). Regulates the expression of genes
CC involved in diverse cellular pathways, including glucose metabolism,
CC photosynthesis, phototropism and stress response (e.g. salt, drought
CC and osmotic stress) (PubMed:22508367, PubMed:26961720). Regulates plant
CC immunity, especially during necrotrophic fungal infection (e.g.
CC B.cinerea) (PubMed:24451981). Binds to ABR1 promoter and promotes its
CC expression, thus negatively regulating the abscisic acid (ABA)
CC signaling pathway. Represses ABA- and salt-responsive genes expression
CC (PubMed:26961720). {ECO:0000269|PubMed:22508367,
CC ECO:0000269|PubMed:24451981, ECO:0000269|PubMed:26961720}.
CC -!- SUBUNIT: Interacts with MED18 to suppress disease susceptibility via
CC the repression of genes glutaredoxins GRX480, GRXS13 and thioredoxin
CC TRX-h5. {ECO:0000269|PubMed:24451981}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24451981,
CC ECO:0000269|PubMed:26961720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2V3L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2V3L3-2; Sequence=VSP_028387, VSP_028388;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, to a lower extent in
CC seedlings, stems and leaves, and, at low levels, in roots and senescent
CC leaves. {ECO:0000269|PubMed:26961720}.
CC -!- DEVELOPMENTAL STAGE: Rapidly induced following seed germination,
CC especially in tender cotyledons. {ECO:0000269|PubMed:26961720}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) in an ABI1- and ABI4-
CC dependent manner. Stimulated by stress conditions including high salt,
CC osmotic stress (e.g. mannitol) and dehydration. May be induced by ABI4
CC but repressed by ABR1. Repressed by darkness but induced by light.
CC {ECO:0000269|PubMed:26961720}.
CC -!- DISRUPTION PHENOTYPE: Deregulated expression of glutaredoxins GRX480,
CC GRXS13 and thioredoxin TRX-h5 leading to enhanced susceptibility to
CC fungal infection (e.g. B.cinerea) (PubMed:24451981). Increased
CC sensitivity to abscisic acid (ABA), drought, and salt (NaCl) stress.
CC Reduced induction of ABR1, but reduced repression of RD29A, RD29B, and
CC COR15A in response to abiotic stresses (PubMed:26961720).
CC {ECO:0000269|PubMed:24451981, ECO:0000269|PubMed:26961720}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB83613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073162; BAB83613.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82553.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82554.1; -; Genomic_DNA.
DR RefSeq; NP_001031589.1; NM_001036512.2. [Q2V3L3-2]
DR RefSeq; NP_849323.1; NM_178992.4. [Q2V3L3-1]
DR AlphaFoldDB; Q2V3L3; -.
DR SMR; Q2V3L3; -.
DR BioGRID; 11401; 5.
DR IntAct; Q2V3L3; 3.
DR STRING; 3702.AT4G06634.1; -.
DR iPTMnet; Q2V3L3; -.
DR PaxDb; Q2V3L3; -.
DR PRIDE; Q2V3L3; -.
DR ProteomicsDB; 242960; -. [Q2V3L3-1]
DR EnsemblPlants; AT4G06634.1; AT4G06634.1; AT4G06634. [Q2V3L3-1]
DR EnsemblPlants; AT4G06634.2; AT4G06634.2; AT4G06634. [Q2V3L3-2]
DR GeneID; 826093; -.
DR Gramene; AT4G06634.1; AT4G06634.1; AT4G06634. [Q2V3L3-1]
DR Gramene; AT4G06634.2; AT4G06634.2; AT4G06634. [Q2V3L3-2]
DR KEGG; ath:AT4G06634; -.
DR Araport; AT4G06634; -.
DR TAIR; locus:1005716361; AT4G06634.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_040248_0_0_1; -.
DR InParanoid; Q2V3L3; -.
DR OMA; HNEKQYI; -.
DR PhylomeDB; Q2V3L3; -.
DR PRO; PR:Q2V3L3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2V3L3; baseline and differential.
DR GO; GO:0031011; C:Ino80 complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; Alternative splicing;
KW Coiled coil; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Plant defense; Reference proteome; Repeat; Repressor; Stress response;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..387
FT /note="Zinc finger transcription factor YY1"
FT /id="PRO_0000305942"
FT ZN_FING 79..103
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 108..132
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 138..162
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..193
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 230..255
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 201..290
FT /note="MED18-binding"
FT /evidence="ECO:0000269|PubMed:24451981"
FT REGION 258..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 339..367
FT /evidence="ECO:0000255"
FT MOTIF 319..326
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 272..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028387"
FT VAR_SEQ 39..50
FT /note="TGGKCHLHKWVT -> MLNCIIVLLLLP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028388"
SQ SEQUENCE 387 AA; 44703 MW; 070C11CC3A1A97E3 CRC64;
MDHQNYQYQN PFERRPILKS KAPAVKWIKE WVPQDIVATG GKCHLHKWVT EDTFSRLKEK
EKEPDVPEPE PEPTTEILFL CSYDGCGKTF FDVSALRKHS HIHGERQYVC DQEGCGKKFL
DSSKLKRHYL IHTGERNYIC TYEGCGKAFS LDFNLRSHMK THSQENYHIC PYSGCVKRYA
HEYKLKNHVA AYHEKNGGGE TPKYTPPAEK VLRTVKTPAT VCGPSSDRPY ACPYEGCEKA
YIHEYKLKLH LKREHPGHLQ EENADTPTLN KHNGNDRNEI DDGSDQDVYR KHASNGKGQT
HKQQSRAKPN MRTPPAKVGK KGSTSSPAKA RIAKKPWQAK ETFEEVEREE EEDSEETEED
RDNVEDGWRF GENNEDDDDD EETEYED
