HY5_ARATH
ID HY5_ARATH Reviewed; 168 AA.
AC O24646;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcription factor HY5 {ECO:0000303|PubMed:9367981};
DE AltName: Full=Protein LONG HYPOCOTYL 5 {ECO:0000303|PubMed:9367981};
DE AltName: Full=bZIP transcription factor 56 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP56 {ECO:0000303|PubMed:11906833};
GN Name=HY5 {ECO:0000303|PubMed:9367981};
GN Synonyms=BZIP56 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At5g11260 {ECO:0000312|Araport:AT5G11260};
GN ORFNames=F2I11_150 {ECO:0000312|EMBL:CAB96661.1};
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 [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=9367981; DOI=10.1101/gad.11.22.2983;
RA Oyama T., Shimura Y., Okada K.;
RT "The Arabidopsis HY5 gene encodes a bZIP protein that regulates stimulus-
RT induced development of root and hypocotyl.";
RL Genes Dev. 11:2983-2995(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 UBIQUITINATION, AND SUBSEQUENT DEGRADATION.
RX PubMed=10839542; DOI=10.1038/35013076;
RA Osterlund M.T., Hardtke C.S., Wei N., Deng X.-W.;
RT "Targeted destabilization of HY5 during light-regulated development of
RT Arabidopsis.";
RL Nature 405:462-466(2000).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=10990463; DOI=10.1093/emboj/19.18.4997;
RA Hardtke C.S., Gohda K., Osterlund M.T., Oyama T., Okada K., Deng X.-W.;
RT "HY5 stability and activity in Arabidopsis is regulated by phosphorylation
RT in its COP1 binding domain.";
RL EMBO J. 19:4997-5006(2000).
RN [6]
RP INTERACTION WITH COP1, AND MUTAGENESIS OF 43-VAL-PRO-44.
RC TISSUE=Etiolated seedling;
RX PubMed=11226162; DOI=10.1093/emboj/20.1.118;
RA Holm M., Hardtke C.S., Gaudet R., Deng X.-W.;
RT "Identification of a structural motif that confers specific interaction
RT with the WD40 repeat domain of Arabidopsis COP1.";
RL EMBO J. 20:118-127(2001).
RN [7]
RP UBIQUITINATION BY CIP8.
RX PubMed=12028569; DOI=10.1046/j.1365-313x.2002.01298.x;
RA Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.;
RT "Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1
RT interacting protein 8 (CIP8).";
RL Plant J. 30:385-394(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [9]
RP HETERODIMERIZATION.
RX PubMed=12023303; DOI=10.1101/gad.969702;
RA Holm M., Ma L.-G., Qu L.-J., Deng X.-W.;
RT "Two interacting bZIP proteins are direct targets of COP1-mediated control
RT of light-dependent gene expression in Arabidopsis.";
RL Genes Dev. 16:1247-1259(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP INTERACTION WITH BBX21.
RX PubMed=21632973; DOI=10.1104/pp.111.177139;
RA Holtan H.E., Bandong S., Marion C.M., Adam L., Tiwari S., Shen Y.,
RA Maloof J.N., Maszle D.R., Ohto M.A., Preuss S., Meister R., Petracek M.,
RA Repetti P.P., Reuber T.L., Ratcliffe O.J., Khanna R.;
RT "BBX32, an Arabidopsis B-Box protein, functions in light signaling by
RT suppressing HY5-regulated gene expression and interacting with
RT STH2/BBX21.";
RL Plant Physiol. 156:2109-2123(2011).
RN [12]
RP INTERACTION WITH BBX25/STH.
RX PubMed=23624715; DOI=10.1105/tpc.113.109751;
RA Gangappa S.N., Crocco C.D., Johansson H., Datta S., Hettiarachchi C.,
RA Holm M., Botto J.F.;
RT "The Arabidopsis B-BOX protein BBX25 interacts with HY5, negatively
RT regulating BBX22 expression to suppress seedling photomorphogenesis.";
RL Plant Cell 25:1243-1257(2013).
RN [13]
RP INTERACTION WITH BBX24/STO.
RX PubMed=23733077; DOI=10.4161/psb.25208;
RA Gangappa S.N., Holm M., Botto J.F.;
RT "Molecular interactions of BBX24 and BBX25 with HYH, HY5 HOMOLOG, to
RT modulate Arabidopsis seedling development.";
RL Plant Signal. Behav. 8:0-0(2013).
RN [14]
RP FUNCTION, AND INTERACTION WITH SPL7.
RX PubMed=25516599; DOI=10.1105/tpc.114.127340;
RA Zhang H., Zhao X., Li J., Cai H., Deng X.W., Li L.;
RT "MicroRNA408 is critical for the HY5-SPL7 gene network that mediates the
RT coordinated response to light and copper.";
RL Plant Cell 26:4933-4953(2014).
RN [15]
RP DISRUPTION PHENOTYPE, INTERACTION WITH SHW1, UBIQUITINATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26474641; DOI=10.1104/pp.15.01184;
RA Srivastava A.K., Senapati D., Srivastava A., Chakraborty M., Gangappa S.N.,
RA Chattopadhyay S.;
RT "SHORT HYPOCOTYL IN WHITE LIGHT1 interacts with ELONGATED HYPOCOTYL5 (HY5)
RT and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1) and promotes COP1-mediated
RT degradation of HY5 during Arabidopsis seedling development.";
RL Plant Physiol. 169:2922-2934(2015).
RN [16]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28735869; DOI=10.1016/j.bbrc.2017.07.110;
RA Kim S.-H., Kim H., Chung S., Lee J.-H.;
RT "DHU1 negatively regulates UV-B signaling via its direct interaction with
RT COP1 and RUP1.";
RL Biochem. Biophys. Res. Commun. 491:285-290(2017).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY COLD, INTERACTION WITH PFD4,
RP AND UBIQUITINATION.
RC STRAIN=cv. Columbia;
RX PubMed=28412546; DOI=10.1016/j.molp.2017.03.012;
RA Perea-Resa C., Rodriguez-Milla M.A., Iniesto E., Rubio V., Salinas J.;
RT "Prefoldins negatively regulate cold acclimation in Arabidopsis thaliana by
RT promoting nuclear proteasome-mediated HY5 degradation.";
RL Mol. Plant 10:791-804(2017).
RN [18]
RP INTERACTION WITH HDA15, AND SUBCELLULAR LOCATION.
RX PubMed=31061103; DOI=10.1104/pp.19.00055;
RA Zhao L., Peng T., Chen C.Y., Ji R., Gu D., Li T., Zhang D., Tu Y.T., Wu K.,
RA Liu X.;
RT "HY5 interacts with the histone deacetylase HDA15 to repress hypocotyl cell
RT elongation in photomorphogenesis.";
RL Plant Physiol. 180:1450-1466(2019).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 11-150, AND HOMODIMERIZATION.
RX PubMed=17261584; DOI=10.1074/jbc.m611465200;
RA Yoon M.K., Kim H.M., Choi G., Lee J.O., Choi B.S.;
RT "Structural basis for the conformational integrity of the Arabidopsis
RT thaliana HY5 leucine zipper homodimer.";
RL J. Biol. Chem. 282:12989-13002(2007).
CC -!- FUNCTION: Transcription factor that promotes photomorphogenesis in
CC light. Acts downstream of the light receptor network and directly
CC affects transcription of light-induced genes. Specifically involved in
CC the blue light specific pathway, suggesting that it participates in
CC transmission of cryptochromes (CRY1 and CRY2) signals to downstream
CC responses. In darkness, its degradation prevents the activation of
CC light-induced genes (Probable). Involved in responses to cold
CC conditions probably by modulating the expression of several genes and
CC triggering anthocyanin biosynthesis (PubMed:28412546). Acts
CC coordinately with SPL7 to regulate the microRNA miR408 and its target
CC genes in response to changes in light and copper conditions
CC (PubMed:25516599). Regulates the abscisic acid (ABA) signaling pathway.
CC Also involved in root gravitropism (PubMed:26474641). Involved in the
CC repression of hypocotyl cell elongation to promote photomorphogenesis
CC (PubMed:31061103). Recruits the histone deacetylase HDA15 to the
CC promoters of a subset of cell wall organization and auxin signaling-
CC related genes (PubMed:31061103). HDA15 represses their transcription by
CC decreasing the levels of histone H4 acetylation in a light-dependent
CC manner (PubMed:31061103). {ECO:0000269|PubMed:25516599,
CC ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28412546,
CC ECO:0000269|PubMed:31061103, ECO:0000305}.
CC -!- SUBUNIT: Homodimer; homodimerizes via the leucine-zipper domains
CC (PubMed:17261584). Heterodimer; heterodimerizes with HYH via the
CC leucine-zipper domains (PubMed:12023303). Interacts with COP1 WD40
CC domain (PubMed:11226162). Interacts with BBX21 (PubMed:21632973),
CC BBX24/STO (PubMed:23733077) and BBX25/STH (PubMed:23624715). Interacts
CC with SPL7 (PubMed:25516599). Binds to SHW1 in the nucleus
CC (PubMed:26474641). Interacts with HDA15 in the nucleus
CC (PubMed:31061103). Interacts with PFD4 in the nucleus and at low
CC temperature (e.g. at 4 degrees Celsius) (PubMed:28412546).
CC {ECO:0000269|PubMed:11226162, ECO:0000269|PubMed:12023303,
CC ECO:0000269|PubMed:21632973, ECO:0000269|PubMed:23624715,
CC ECO:0000269|PubMed:23733077, ECO:0000269|PubMed:25516599,
CC ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28412546,
CC ECO:0000269|PubMed:31061103}.
CC -!- INTERACTION:
CC O24646; Q0IGM7: BBX20; NbExp=3; IntAct=EBI-301660, EBI-15191597;
CC O24646; Q9LQZ7: BBX21; NbExp=4; IntAct=EBI-301660, EBI-1994459;
CC O24646; Q9SYM2: BBX22; NbExp=3; IntAct=EBI-301660, EBI-1994217;
CC O24646; O82617: BBX23; NbExp=4; IntAct=EBI-301660, EBI-15191793;
CC O24646; Q9SID1: BBX25; NbExp=3; IntAct=EBI-301660, EBI-631960;
CC O24646; P43254: COP1; NbExp=8; IntAct=EBI-301660, EBI-301649;
CC O24646; A8MS70: HYH; NbExp=5; IntAct=EBI-301660, EBI-15191595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26474641,
CC ECO:0000269|PubMed:28412546, ECO:0000269|PubMed:31061103,
CC ECO:0000269|PubMed:9367981}.
CC -!- TISSUE SPECIFICITY: Expressed in root, hypocotyl, cotyledon, leaf, stem
CC and floral organs.
CC -!- INDUCTION: Accumulates transiently within 2 days in response to cold;
CC the proteasome-mediated degradation observed after accumulation is
CC triggered by prefoldin co-chaperone complex (e.g. PFD3, PFD4 and PFD5).
CC {ECO:0000269|PubMed:28412546}.
CC -!- PTM: Phosphorylated by CK2. Shows a stronger interaction with COP1 when
CC unphosphorylated. However, phosphorylation does not affect its
CC susceptibility to be ubiquitinated. {ECO:0000269|PubMed:10990463}.
CC -!- PTM: Ubiquitinated by COP1 and/or CIP8. Ubiquitination takes place in
CC darkness and leads to its subsequent degradation, thereby preventing
CC activation of photomorphogenesis signals (PubMed:10839542,
CC PubMed:12028569). Ubiquitination and subsequent COP1-mediated
CC degradation is triggered by SHW1 in the darkness during seedling
CC development (PubMed:26474641). Ubiquinated and degraded in response to
CC cold when reaching an accumulation peak after 2 days; this proteasome-
CC mediated decay is promoted by prefoldin co-chaperone complex (e.g.
CC PFD4) (PubMed:28412546). {ECO:0000269|PubMed:10839542,
CC ECO:0000269|PubMed:12028569, ECO:0000269|PubMed:26474641,
CC ECO:0000269|PubMed:28412546}.
CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to abscisic acid (ABA)
CC leading to impaired ABA-mediated reduction of seed germination
CC (PubMed:26474641). Abrogated induction of DHU1 in response to UV-B
CC (PubMed:28735869). The double mutant shw1 hy5 has altered root growth,
CC hypocotyl length and hook angle similar to the single mutant shw1 in
CC the darkness and far red light (FR), but shorter hypocotyl in WL, red
CC light (RL) and blue light (BL) (PubMed:26474641). In addition, shw1 hy5
CC is recued for gravitropic root growth defect observed in hy5 single
CC mutant (PubMed:26474641). The double mutant dhu1-1 hy5-215 phenotype
CC resemble that of the single mutant hy5-215 (PubMed:28735869).
CC {ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28735869}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AB005456; BAA21327.1; -; mRNA.
DR EMBL; AB005295; BAA21116.1; -; mRNA.
DR EMBL; AL360314; CAB96661.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91653.1; -; Genomic_DNA.
DR PIR; T50922; T50922.
DR RefSeq; NP_568246.1; NM_121164.5.
DR PDB; 2OQQ; X-ray; 2.00 A; A/B=111-150.
DR PDB; 5KWN; X-ray; 1.42 A; U=34-52.
DR PDB; 6QTO; X-ray; 1.27 A; B=39-49.
DR PDB; 6QTR; X-ray; 1.37 A; B=39-49.
DR PDBsum; 2OQQ; -.
DR PDBsum; 5KWN; -.
DR PDBsum; 6QTO; -.
DR PDBsum; 6QTR; -.
DR AlphaFoldDB; O24646; -.
DR SMR; O24646; -.
DR BioGRID; 16274; 48.
DR IntAct; O24646; 15.
DR MINT; O24646; -.
DR STRING; 3702.AT5G11260.1; -.
DR iPTMnet; O24646; -.
DR PaxDb; O24646; -.
DR PRIDE; O24646; -.
DR ProteomicsDB; 232124; -.
DR EnsemblPlants; AT5G11260.1; AT5G11260.1; AT5G11260.
DR GeneID; 830996; -.
DR Gramene; AT5G11260.1; AT5G11260.1; AT5G11260.
DR KEGG; ath:AT5G11260; -.
DR Araport; AT5G11260; -.
DR TAIR; locus:2148007; AT5G11260.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_068771_1_0_1; -.
DR InParanoid; O24646; -.
DR OMA; MDMEVKE; -.
DR PhylomeDB; O24646; -.
DR EvolutionaryTrace; O24646; -.
DR PRO; PR:O24646; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O24646; baseline and differential.
DR Genevisible; O24646; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CAFA.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:UniProtKB.
DR GO; GO:0031539; P:positive regulation of anthocyanin metabolic process; IMP:TAIR.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010099; P:regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0010114; P:response to red light; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR DisProt; DP00469; -.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR044280; Hac1/HY5.
DR PANTHER; PTHR46714; PTHR46714; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Activator; DNA-binding;
KW Nucleus; Phosphoprotein; Phytochrome signaling pathway; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..168
FT /note="Transcription factor HY5"
FT /id="PRO_0000076560"
FT DOMAIN 88..151
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..46
FT /note="Interaction with COP1"
FT /evidence="ECO:0000269|PubMed:11226162"
FT REGION 90..110
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 116..144
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MUTAGEN 43..44
FT /note="VP->AA: Abolishes interaction with COP1."
FT /evidence="ECO:0000269|PubMed:11226162"
FT HELIX 111..149
FT /evidence="ECO:0007829|PDB:2OQQ"
SQ SEQUENCE 168 AA; 18463 MW; 1E3C4672B192D8A9 CRC64;
MQEQATSSLA ASSLPSSSER SSSSAPHLEI KEGIESDEEI RRVPEFGGEA VGKETSGRES
GSATGQERTQ ATVGESQRKR GRTPAEKENK RLKRLLRNRV SAQQARERKK AYLSELENRV
KDLENKNSEL EERLSTLQNE NQMLRHILKN TTGNKRGGGG GSNADASL
