ZHD9_ARATH
ID ZHD9_ARATH Reviewed; 312 AA.
AC Q9LHF0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Zinc-finger homeodomain protein 9;
DE Short=AtZHD9;
DE AltName: Full=Homeobox protein 34;
DE Short=AtHB-34;
GN Name=ZHD9; Synonyms=HB34; OrderedLocusNames=At3g28920; ORFNames=MYI13.1;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 INTERACTION WITH ZHD1; ZHD2 AND ZHD11, TISSUE SPECIFICITY, AND GENE FAMILY.
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-273, AND
RP IDENTIFICATION BY 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 [7]
RP INTERACTION WITH 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).
CC -!- FUNCTION: Putative transcription factor.
CC -!- SUBUNIT: Homo- and heterodimer with other ZFHD proteins (By
CC similarity). Interacts with MIF3; this interaction prevents nuclear
CC localization and DNA-binding to inhibit transcription regulation
CC activity. Binds to ZHD1, ZHD2 and ZHD11. {ECO:0000250,
CC ECO:0000269|PubMed:16428600, ECO:0000269|PubMed:21059647}.
CC -!- INTERACTION:
CC Q9LHF0; Q8LCT6: At1g24210; NbExp=3; IntAct=EBI-1806440, EBI-15203222;
CC Q9LHF0; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-1806440, EBI-15193025;
CC Q9LHF0; Q9FIW9: ZHD10; NbExp=4; IntAct=EBI-1806440, EBI-1806298;
CC Q9LHF0; Q9M9S0: ZHD4; NbExp=3; IntAct=EBI-1806440, EBI-1806420;
CC Q9LHF0; Q9FRL5: ZHD5; NbExp=3; IntAct=EBI-1806440, EBI-1806169;
CC Q9LHF0; Q9ZPW7: ZHD6; NbExp=3; IntAct=EBI-1806440, EBI-1806363;
CC Q9LHF0; Q9SVL0: ZHD7; NbExp=3; IntAct=EBI-1806440, EBI-1806382;
CC Q9LHF0; Q9LXG0: ZHD8; NbExp=3; IntAct=EBI-1806440, EBI-1806405;
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.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, stems and
CC inflorescence and, to a lower extent, in leaves and stems.
CC {ECO:0000269|PubMed:16428600}.
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.
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DR EMBL; AP002049; BAB02255.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77508.1; -; Genomic_DNA.
DR EMBL; AY093171; AAM13170.1; -; mRNA.
DR EMBL; AY128820; AAM91220.1; -; mRNA.
DR RefSeq; NP_189534.1; NM_113813.4.
DR AlphaFoldDB; Q9LHF0; -.
DR SMR; Q9LHF0; -.
DR BioGRID; 7856; 26.
DR IntAct; Q9LHF0; 25.
DR STRING; 3702.AT3G28920.1; -.
DR iPTMnet; Q9LHF0; -.
DR PaxDb; Q9LHF0; -.
DR PRIDE; Q9LHF0; -.
DR ProteomicsDB; 232344; -.
DR EnsemblPlants; AT3G28920.1; AT3G28920.1; AT3G28920.
DR GeneID; 822527; -.
DR Gramene; AT3G28920.1; AT3G28920.1; AT3G28920.
DR KEGG; ath:AT3G28920; -.
DR Araport; AT3G28920; -.
DR TAIR; locus:2095157; AT3G28920.
DR eggNOG; ENOG502QWG3; Eukaryota.
DR HOGENOM; CLU_039237_0_0_1; -.
DR InParanoid; Q9LHF0; -.
DR OMA; NTFAKRD; -.
DR OrthoDB; 1442390at2759; -.
DR PhylomeDB; Q9LHF0; -.
DR PRO; PR:Q9LHF0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHF0; baseline and differential.
DR Genevisible; Q9LHF0; AT.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; Homeobox; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..312
FT /note="Zinc-finger homeodomain protein 9"
FT /id="PRO_0000426023"
FT ZN_FING 52..103
FT /note="ZF-HD dimerization-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00856"
FT DNA_BIND 192..255
FT /note="Homeobox"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 244
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 312 AA; 33560 MW; 8EE55DFABE6C1C03 CRC64;
MLEVRSMDMT PKSPEPESET PTRIQPAKPI SFSNGIIKRH HHHHHNNNKV TYKECLKNHA
AAIGGHALDG CGEFMPSPSS TPSDPTSLKC AACGCHRNFH RRETDDSSAV PPPSLLPSST
TTAAIEYQPH HRHHPPPPLA PPLPRSPNSS SPPPISSSYM LLALSGNNKT APFSDLNFAA
AANHLSATPG SRKRFRTKFS SNQKEKMHEF ADRIGWKIQK RDEDEVRDFC REIGVDKGVL
KVWMHNNKNS FKFSGGGATT VQRNDNGIGG ENSNDDGVRG LANDGDGGGG RFESDSGGAD
GGGNVNASSS SS
