ZHD10_ARATH
ID ZHD10_ARATH Reviewed; 334 AA.
AC Q9FIW9; Q0WUG8; Q8LCV0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Zinc-finger homeodomain protein 10;
DE Short=AtZHD10;
DE AltName: Full=Homeobox protein 23;
DE Short=AtHB-23;
GN Name=ZHD10; Synonyms=HB23; OrderedLocusNames=At5g39760; ORFNames=MKM21.8;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION.
RX PubMed=11289511; DOI=10.1023/a:1006450005648;
RA Windhoevel A., Hein I., Dabrowa R., Stockhaus J.;
RT "Characterization of a novel class of plant homeodomain proteins that bind
RT to the C4 phosphoenolpyruvate carboxylase gene of Flaveria trinervia.";
RL Plant Mol. Biol. 45:201-214(2001).
RN [7]
RP HOMODIMERIZATION, INTERACTION WITH ZHD1; ZHD2; ZHD4; ZHD5; ZHD6; ZHD7 AND
RP ZHD8, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16428600; DOI=10.1104/pp.105.070565;
RA Tan Q.K., Irish V.F.;
RT "The Arabidopsis zinc finger-homeodomain genes encode proteins with unique
RT biochemical properties that are coordinately expressed during floral
RT development.";
RL Plant Physiol. 140:1095-1108(2006).
RN [8]
RP FUNCTION, INDUCTION BY GIBBERELLIC ACID, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=17387478; DOI=10.1007/s00299-007-0340-9;
RA Kim Y.-K., Son O., Kim M.-R., Nam K.-H., Kim G.-T., Lee M.-S., Choi S.-Y.,
RA Cheon C.-I.;
RT "ATHB23, an Arabidopsis class I homeodomain-leucine zipper gene, is
RT expressed in the adaxial region of young leaves.";
RL Plant Cell Rep. 26:1179-1185(2007).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18713354; DOI=10.1111/j.1744-7909.2008.00681.x;
RA Hu W., dePamphilis C.W., Ma H.;
RT "Phylogenetic analysis of the plant-specific zinc finger-homeobox and mini
RT zinc finger gene families.";
RL J. Integr. Plant Biol. 50:1031-1045(2008).
RN [10]
RP INTERACTION WITH MIF1; MIF2 AND MIF3, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21059647; DOI=10.1074/jbc.m110.167692;
RA Hong S.-Y., Kim O.-K., Kim S.-G., Yang M.-S., Park C.-M.;
RT "Nuclear import and DNA binding of the ZHD5 transcription factor is
RT modulated by a competitive peptide inhibitor in Arabidopsis.";
RL J. Biol. Chem. 286:1659-1668(2011).
RN [11]
RP INTERACTION WITH KIN10 AND KIN11.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
CC -!- FUNCTION: Putative transcription factor. Probably involved in
CC establishing polarity during leaf development through the gibberellic
CC acid (GA) signaling pathway. {ECO:0000269|PubMed:17387478}.
CC -!- SUBUNIT: Homo- and heterodimer with other ZFHD proteins. Interacts with
CC MIF1, MIF2 and MIF3; these interactions prevent nuclear localization
CC and DNA-binding to inhibit transcription regulation activity. Binds to
CC ZHD1, ZHD2, ZHD4, ZHD5, ZHD6, ZHD7 and ZHD8. Interacts with KIN10 and
CC KIN11 (Ref.11). {ECO:0000269|PubMed:16428600,
CC ECO:0000269|PubMed:21059647, ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC Q9FIW9; Q8GWP4: At2g21530; NbExp=3; IntAct=EBI-1806298, EBI-15199129;
CC Q9FIW9; F4JI72: At4g03250; NbExp=3; IntAct=EBI-1806298, EBI-15192535;
CC Q9FIW9; Q9FKP8: ZHD1; NbExp=3; IntAct=EBI-1806298, EBI-766685;
CC Q9FIW9; Q9FMY7: ZHD13; NbExp=4; IntAct=EBI-1806298, EBI-1806559;
CC Q9FIW9; Q9LQW3: ZHD14; NbExp=3; IntAct=EBI-1806298, EBI-1806701;
CC Q9FIW9; O64722: ZHD3; NbExp=4; IntAct=EBI-1806298, EBI-1806244;
CC Q9FIW9; Q9M9S0: ZHD4; NbExp=4; IntAct=EBI-1806298, EBI-1806420;
CC Q9FIW9; Q9FRL5: ZHD5; NbExp=4; IntAct=EBI-1806298, EBI-1806169;
CC Q9FIW9; Q9ZPW7: ZHD6; NbExp=5; IntAct=EBI-1806298, EBI-1806363;
CC Q9FIW9; Q9SVL0: ZHD7; NbExp=5; IntAct=EBI-1806298, EBI-1806382;
CC Q9FIW9; Q9LXG0: ZHD8; NbExp=7; IntAct=EBI-1806298, EBI-1806405;
CC Q9FIW9; Q9LHF0: ZHD9; NbExp=4; IntAct=EBI-1806298, EBI-1806440;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Interactions with MIF
CC proteins prevent nuclear subcellular location and leads to a scattered
CC repartition throughout the cytoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in rosettes (e.g. young leaves),
CC flowers (e.g. styles), siliques and inflorescence.
CC {ECO:0000269|PubMed:16428600, ECO:0000269|PubMed:17387478}.
CC -!- DEVELOPMENTAL STAGE: In young leaves, accumulates in the adaxial domain
CC of leaf primordia and the rib meristem. {ECO:0000269|PubMed:17387478}.
CC -!- INDUCTION: By gibberellic acid (GA). {ECO:0000269|PubMed:17387478}.
CC -!- DOMAIN: The homeodomain differs form the typical one by having namely 4
CC instead of 3 extra amino acids inserted in the loop between helix 1 and
CC helix 2.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB016876; BAB11382.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94472.1; -; Genomic_DNA.
DR EMBL; AY091034; AAM13855.1; -; mRNA.
DR EMBL; AY117347; AAM51422.1; -; mRNA.
DR EMBL; AK227191; BAE99230.1; -; mRNA.
DR EMBL; AY086395; AAM64462.1; ALT_INIT; mRNA.
DR RefSeq; NP_568570.1; NM_123338.3.
DR AlphaFoldDB; Q9FIW9; -.
DR SMR; Q9FIW9; -.
DR BioGRID; 19223; 30.
DR IntAct; Q9FIW9; 36.
DR STRING; 3702.AT5G39760.1; -.
DR PaxDb; Q9FIW9; -.
DR PRIDE; Q9FIW9; -.
DR ProteomicsDB; 232335; -.
DR EnsemblPlants; AT5G39760.1; AT5G39760.1; AT5G39760.
DR GeneID; 833972; -.
DR Gramene; AT5G39760.1; AT5G39760.1; AT5G39760.
DR KEGG; ath:AT5G39760; -.
DR Araport; AT5G39760; -.
DR TAIR; locus:2167052; AT5G39760.
DR eggNOG; ENOG502QWG3; Eukaryota.
DR HOGENOM; CLU_039237_0_0_1; -.
DR InParanoid; Q9FIW9; -.
DR OMA; THHVLEY; -.
DR OrthoDB; 1442390at2759; -.
DR PhylomeDB; Q9FIW9; -.
DR PRO; PR:Q9FIW9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIW9; baseline and differential.
DR Genevisible; Q9FIW9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0001173; P:DNA-templated transcriptional start site selection; IEP:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009637; P:response to blue light; IDA:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006455; Homeodomain_ZF_HD.
DR InterPro; IPR006456; ZF_HD_homeobox_Cys/His_dimer.
DR Pfam; PF04770; ZF-HD_dimer; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01565; homeo_ZF_HD; 1.
DR TIGRFAMs; TIGR01566; ZF_HD_prot_N; 1.
DR PROSITE; PS51523; ZF_HD_DIMER; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Gibberellin signaling pathway; Homeobox; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..334
FT /note="Zinc-finger homeodomain protein 10"
FT /id="PRO_0000426024"
FT ZN_FING 56..107
FT /note="ZF-HD dimerization-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00856"
FT DNA_BIND 200..263
FT /note="Homeobox"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 252
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT CONFLICT 106
FT /note="R -> L (in Ref. 4; BAE99230)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Y -> N (in Ref. 5; AAM64462)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> Z (in Ref. 5; AAM64462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36386 MW; F5F3445BA2CB0E22 CRC64;
MMDMTPTITT TTTPTPKSPE PESETPTRIQ PAKPISFSNG IIKRHHHHHH PLLFTYKECL
KNHAAALGGH ALDGCGEFMP SPSSISSDPT SLKCAACGCH RNFHRRDPDN NNDSSQIPPP
PSTAVEYQPH HRHHPPPPPP PPPPRSPNSA SPPPISSSYM LLSLSGTNNN NNNLASFSDL
NFSAGNNHHH HHQHTLHGSR KRFRTKFSQF QKEKMHEFAE RVGWKMQKRD EDDVRDFCRQ
IGVDKSVLKV WMHNNKNTFN RRDIAGNEIR QIDNGGGNHT PILAGEINNH NNGHHGVGGG
GELHQSVSSG GGGGGFDSDS GGANGGNVNG SSSS
