HYH_ARATH
ID HYH_ARATH Reviewed; 149 AA.
AC Q8W191; Q8LB41; Q9LUN6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Transcription factor HY5-like;
DE AltName: Full=HY5 homolog;
DE AltName: Full=bZIP transcription factor 64 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP64 {ECO:0000303|PubMed:11906833};
GN Name=HYH; Synonyms=BZIP64 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g17609; ORFNames=MKP6.27;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP DNA-BINDING, DEGRADATION, HETERODIMERIZATION, INTERACTION WITH COP1, AND
RP MUTAGENESIS OF 31-VAL-PRO-32.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INTERACTION WITH BBX24/STO AND BBX25/STH.
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).
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. {ECO:0000269|PubMed:12023303}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with HY5 via the leucine-zipper
CC domains. Interacts with COP1 WD40 domain (PubMed:12023303). Interacts
CC with BBX24/STO and BBX25/STH (PubMed:23733077).
CC {ECO:0000269|PubMed:12023303, ECO:0000269|PubMed:23733077}.
CC -!- INTERACTION:
CC Q8W191-1; P43254: COP1; NbExp=3; IntAct=EBI-11463635, EBI-301649;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:12023303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W191-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W191-2; Sequence=VSP_012011;
CC -!- PTM: Ubiquitinated by COP1. Ubiquitination takes place in darkness and
CC leads to its subsequent degradation, thereby preventing the activation
CC of photomorphogenesis signals.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02051.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g17610 has been split into 2 genes: At3g17609 and At3g17611.; Evidence={ECO:0000305};
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DR EMBL; AF453477; AAL57834.1; -; mRNA.
DR EMBL; AB022219; BAB02051.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75974.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75975.1; -; Genomic_DNA.
DR EMBL; AY087436; AAM64982.1; -; mRNA.
DR EMBL; AK175440; BAD43203.1; -; mRNA.
DR EMBL; AK175523; BAD43286.1; -; mRNA.
DR RefSeq; NP_850604.1; NM_180273.2. [Q8W191-2]
DR RefSeq; NP_850605.1; NM_180274.3. [Q8W191-1]
DR PDB; 6QTT; X-ray; 1.51 A; B=27-35.
DR PDBsum; 6QTT; -.
DR AlphaFoldDB; Q8W191; -.
DR SMR; Q8W191; -.
DR BioGRID; 6360; 16.
DR IntAct; Q8W191; 3.
DR MINT; Q8W191; -.
DR STRING; 3702.AT3G17609.2; -.
DR PaxDb; Q8W191; -.
DR ProteomicsDB; 232180; -. [Q8W191-1]
DR EnsemblPlants; AT3G17609.1; AT3G17609.1; AT3G17609. [Q8W191-2]
DR EnsemblPlants; AT3G17609.2; AT3G17609.2; AT3G17609. [Q8W191-1]
DR GeneID; 821027; -.
DR Gramene; AT3G17609.1; AT3G17609.1; AT3G17609. [Q8W191-2]
DR Gramene; AT3G17609.2; AT3G17609.2; AT3G17609. [Q8W191-1]
DR KEGG; ath:AT3G17609; -.
DR Araport; AT3G17609; -.
DR TAIR; locus:1005716533; AT3G17609.
DR eggNOG; KOG1414; Eukaryota.
DR OMA; LFTVPDM; -.
DR PhylomeDB; Q8W191; -.
DR PRO; PR:Q8W191; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W191; baseline and differential.
DR Genevisible; Q8W191; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000976; F:transcription cis-regulatory region binding; IPI: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; IBA:GO_Central.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0010099; P:regulation of photomorphogenesis; IBA:GO_Central.
DR GO; GO:0010218; P:response to far red light; IBA:GO_Central.
DR GO; GO:0010114; P:response to red light; IBA:GO_Central.
DR GO; GO:0010224; P:response to UV-B; IEP:TAIR.
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; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Phosphoprotein; Phytochrome signaling pathway; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..149
FT /note="Transcription factor HY5-like"
FT /id="PRO_0000076562"
FT DOMAIN 78..141
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..36
FT /note="Interaction with COP1"
FT /evidence="ECO:0000269|PubMed:12023303"
FT REGION 80..100
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 106..134
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 39..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O24646"
FT VAR_SEQ 22..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_012011"
FT MUTAGEN 31..32
FT /note="VP->AA: Abolishes interaction with COP1."
FT /evidence="ECO:0000269|PubMed:12023303"
SQ SEQUENCE 149 AA; 16899 MW; FCAA23AFBED351B6 CRC64;
MSLQRPNGNS SSSSSHKKHK TEESDEELLM VPDMEAAGST CVLSSSADDG VNNPELDQTQ
NGVSTAKRRR GRNPVDKEYR SLKRLLRNRV SAQQARERKK VYVSDLESRA NELQNNNDQL
EEKISTLTNE NTMLRKMLIN TRPKTDDNH
