ATBH9_ARATH
ID ATBH9_ARATH Reviewed; 841 AA.
AC O04292; Q56ZC0; Q9S9Q0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Homeobox-leucine zipper protein ATHB-9;
DE AltName: Full=HD-ZIP protein ATHB-9;
DE AltName: Full=Homeodomain transcription factor ATHB-9;
DE AltName: Full=Protein PHAVOLUTA;
GN Name=ATHB-9; Synonyms=HB9, PHV; OrderedLocusNames=At1g30490;
GN ORFNames=F26G16.11;
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 [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=9747806; DOI=10.1023/a:1006016319613;
RA Sessa G., Steindler C., Morelli G., Ruberti I.;
RT "The Arabidopsis Athb-8, -9 and -14 genes are members of a small gene
RT family coding for highly related HD-ZIP proteins.";
RL Plant Mol. Biol. 38:609-622(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Ruzza V., Carabelli M., Ciarbelli A.R., Sessa G., Steindler C., Ruberti I.;
RT "Nucleotide sequence of the Arabidopsis ATHB-9 mRNA, encoding an HD-Zip III
RT protein related to ATHB-8.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-198.
RX PubMed=11395776; DOI=10.1038/35079635;
RA McConnell J.R., Emery J., Eshed Y., Bao N., Bowman J., Barton M.K.;
RT "Role of PHABULOSA and PHAVOLUTA in determining radial patterning in
RT shoots.";
RL Nature 411:709-713(2001).
RN [7]
RP INDUCTION.
RX PubMed=14999284; DOI=10.1038/nature02366;
RA Kidner C.A., Martienssen R.A.;
RT "Spatially restricted microRNA directs leaf polarity through ARGONAUTE1.";
RL Nature 428:81-84(2004).
RN [8]
RP INDUCTION.
RX PubMed=16033795; DOI=10.1242/dev.01942;
RA Williams L., Grigg S.P., Xie M., Christensen S., Fletcher J.C.;
RT "Regulation of Arabidopsis shoot apical meristem and lateral organ
RT formation by microRNA miR166g and its AtHD-ZIP target genes.";
RL Development 132:3657-3668(2005).
RN [9]
RP FUNCTION.
RX PubMed=15598805; DOI=10.1105/tpc.104.026161;
RA Prigge M.J., Otsuga D., Alonso J.M., Ecker J.R., Drews G.N., Clark S.E.;
RT "Class III homeodomain-leucine zipper gene family members have overlapping,
RT antagonistic, and distinct roles in Arabidopsis development.";
RL Plant Cell 17:61-76(2005).
RN [10]
RP GENE FAMILY.
RX PubMed=16805899; DOI=10.1111/j.1525-142x.2006.00107.x;
RA Prigge M.J., Clark S.E.;
RT "Evolution of the class III HD-Zip gene family in land plants.";
RL Evol. Dev. 8:350-361(2006).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-40; CYS-55; CYS-59 AND CYS-75.
RX PubMed=17900520; DOI=10.1016/j.abb.2007.08.003;
RA Comelli R.N., Gonzalez D.H.;
RT "Conserved homeodomain cysteines confer redox sensitivity and influence the
RT DNA binding properties of plant class III HD-Zip proteins.";
RL Arch. Biochem. Biophys. 467:41-47(2007).
RN [12]
RP INTERACTION WITH ESR1 AND ESR2.
RX PubMed=17376809; DOI=10.1242/dev.001016;
RA Chandler J.W., Cole M., Flier A., Grewe B., Werr W.;
RT "The AP2 transcription factors DORNROSCHEN and DORNROSCHEN-LIKE redundantly
RT control Arabidopsis embryo patterning via interaction with PHAVOLUTA.";
RL Development 134:1653-1662(2007).
RN [13]
RP INDUCTION.
RX PubMed=17237362; DOI=10.1093/pcp/pcm008;
RA Zhou G.-K., Kubo M., Zhong R., Demura T., Ye Z.-H.;
RT "Overexpression of miR165 affects apical meristem formation, organ polarity
RT establishment and vascular development in Arabidopsis.";
RL Plant Cell Physiol. 48:391-404(2007).
RN [14]
RP INTERACTION WITH ZPR3.
RX PubMed=18408069; DOI=10.1105/tpc.107.057448;
RA Kim Y.S., Kim S.G., Lee M., Lee I., Park H.Y., Seo P.J., Jung J.H.,
RA Kwon E.J., Suh S.W., Paek K.H., Park C.M.;
RT "HD-ZIP III activity is modulated by competitive inhibitors via a feedback
RT loop in Arabidopsis shoot apical meristem development.";
RL Plant Cell 20:920-933(2008).
RN [15]
RP GENE FAMILY.
RX PubMed=25263420; DOI=10.1016/j.ympev.2014.06.017;
RA Floyd S.K., Ryan J.G., Conway S.J., Brenner E., Burris K.P., Burris J.N.,
RA Chen T., Edger P.P., Graham S.W., Leebens-Mack J.H., Pires J.C.,
RA Rothfels C.J., Sigel E.M., Stevenson D.W., Neal Stewart C. Jr., Wong G.K.,
RA Bowman J.L.;
RT "Origin of a novel regulatory module by duplication and degeneration of an
RT ancient plant transcription factor.";
RL Mol. Phylogenet. Evol. 81:159-173(2014).
CC -!- FUNCTION: Probable transcription factor involved in the determination
CC of adaxial-abaxial polarity in ovule primordium. Specifies adaxial leaf
CC fates. Binds to the DNA sequence 5'-GTAAT[GC]ATTAC-3'.
CC {ECO:0000269|PubMed:11395776, ECO:0000269|PubMed:15598805,
CC ECO:0000269|PubMed:17900520, ECO:0000269|PubMed:9747806}.
CC -!- SUBUNIT: Binds DNA as homodimer (PubMed:9747806). Interacts with ESR1
CC and ESR2 (PubMed:17376809). Interacts with ZPR3 (PubMed:18408069).
CC {ECO:0000269|PubMed:17376809, ECO:0000269|PubMed:18408069,
CC ECO:0000269|PubMed:9747806}.
CC -!- INTERACTION:
CC O04292; F4I9R1: At1g58110; NbExp=3; IntAct=EBI-1536772, EBI-15195737;
CC O04292; F4JI72: At4g03250; NbExp=5; IntAct=EBI-1536772, EBI-15192535;
CC O04292; P92953: ATHB-4; NbExp=4; IntAct=EBI-1536772, EBI-15192259;
CC O04292; Q94JL3: BHLH112; NbExp=3; IntAct=EBI-1536772, EBI-3133192;
CC O04292; Q9LEZ3: BIM1; NbExp=5; IntAct=EBI-1536772, EBI-617095;
CC O04292; Q9SAD4: ESR1; NbExp=5; IntAct=EBI-1536772, EBI-1536756;
CC O04292; Q9FYK5: ESR2; NbExp=2; IntAct=EBI-1536772, EBI-1536925;
CC O04292; P46602: HAT3; NbExp=5; IntAct=EBI-1536772, EBI-4450405;
CC O04292; Q8LAL2: IAA26; NbExp=4; IntAct=EBI-1536772, EBI-3947418;
CC O04292; Q9XGX0: SHI; NbExp=3; IntAct=EBI-1536772, EBI-15205274;
CC O04292; O82277: TCP10; NbExp=3; IntAct=EBI-1536772, EBI-3133327;
CC O04292; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-1536772, EBI-4424877;
CC O04292; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-1536772, EBI-15192325;
CC O04292; Q9FME3: TCP5; NbExp=4; IntAct=EBI-1536772, EBI-15192251;
CC O04292; Q9C518: TCP8; NbExp=4; IntAct=EBI-1536772, EBI-3134124;
CC O04292; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1536772, EBI-4426557;
CC O04292; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-1536772, EBI-4424568;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: By auxin. Repressed by miR165 and miR166.
CC {ECO:0000269|PubMed:14999284, ECO:0000269|PubMed:16033795,
CC ECO:0000269|PubMed:17237362}.
CC -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class III subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y10922; CAA71854.1; -; Genomic_DNA.
DR EMBL; AJ440967; CAD29544.1; -; mRNA.
DR EMBL; AC009917; AAF19752.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31232.1; -; Genomic_DNA.
DR EMBL; AK221046; BAD94803.1; -; mRNA.
DR EMBL; AK226570; BAE98697.1; -; mRNA.
DR PIR; H86429; H86429.
DR RefSeq; NP_174337.1; NM_102785.5.
DR AlphaFoldDB; O04292; -.
DR SMR; O04292; -.
DR BioGRID; 25163; 54.
DR IntAct; O04292; 53.
DR STRING; 3702.AT1G30490.1; -.
DR PaxDb; O04292; -.
DR PRIDE; O04292; -.
DR ProteomicsDB; 246720; -.
DR EnsemblPlants; AT1G30490.1; AT1G30490.1; AT1G30490.
DR GeneID; 839928; -.
DR Gramene; AT1G30490.1; AT1G30490.1; AT1G30490.
DR KEGG; ath:AT1G30490; -.
DR Araport; AT1G30490; -.
DR TAIR; locus:2028140; AT1G30490.
DR eggNOG; ENOG502QPKR; Eukaryota.
DR HOGENOM; CLU_012517_0_0_1; -.
DR InParanoid; O04292; -.
DR OMA; FRDCRCV; -.
DR OrthoDB; 146876at2759; -.
DR PhylomeDB; O04292; -.
DR PRO; PR:O04292; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04292; baseline and differential.
DR Genevisible; O04292; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009943; P:adaxial/abaxial axis specification; IMP:TAIR.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009855; P:determination of bilateral symmetry; IMP:TAIR.
DR GO; GO:0009880; P:embryonic pattern specification; IGI:TAIR.
DR GO; GO:0080060; P:integument development; IGI:TAIR.
DR GO; GO:0010014; P:meristem initiation; IMP:TAIR.
DR GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:TAIR.
DR GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR044830; HD-Zip_III.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR013978; MEKHLA.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR45950; PTHR45950; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF08670; MEKHLA; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Differentiation; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..841
FT /note="Homeobox-leucine zipper protein ATHB-9"
FT /id="PRO_0000331659"
FT DOMAIN 160..388
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT DNA_BIND 18..81
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..118
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 40
FT /note="C->A: Decrease in DNA-binding efficiency."
FT /evidence="ECO:0000269|PubMed:17900520"
FT MUTAGEN 55
FT /note="C->A: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:17900520"
FT MUTAGEN 59
FT /note="C->A: No effect on DNA-binding."
FT /evidence="ECO:0000269|PubMed:17900520"
FT MUTAGEN 75
FT /note="C->A: Decrease in DNA-binding efficiency."
FT /evidence="ECO:0000269|PubMed:17900520"
FT MUTAGEN 198
FT /note="G->D: In phv-1d, phv-2d, phv-3d and phv-4d;
FT constitutively active. Transformation of abaxial leaf fates
FT into adaxial leaf fates."
FT /evidence="ECO:0000269|PubMed:11395776"
SQ SEQUENCE 841 AA; 92402 MW; E11FB264485F91CA CRC64;
MMAHHSMDDR DSPDKGFDSG KYVRYTPEQV EALERVYAEC PKPSSLRRQQ LIRECPILCN
IEPRQIKVWF QNRRCREKQR KESARLQTVN RKLSAMNKLL MEENDRLQKQ VSNLVYENGF
MKHRIHTASG TTTDNSCESV VVSGQQRQQQ NPTHQHPQRD VNNPANLLSI AEETLAEFLC
KATGTAVDWV QMIGMKPGPD SIGIVAVSRN CSGIAARACG LVSLEPMKVA EILKDRPSWF
RDCRCVETLN VIPTGNGGTI ELVNTQIYAP TTLAAARDFW TLRYSTSLED GSYVVCERSL
TSATGGPNGP LSSSFVRAKM LSSGFLIRPC DGGGSIIHIV DHVDLDVSSV PEVLRPLYES
SKILAQKMTV AALRHVRQIA QETSGEVQYS GGRQPAVLRT FSQRLCRGFN DAVNGFVDDG
WSPMSSDGGE DITIMINSSS AKFAGSQYGS SFLPSFGSGV LCAKASMLLQ NVPPLVLIRF
LREHRAEWAD YGVDAYSAAS LRATPYAVPC VRTGGFPSNQ VILPLAQTLE HEEFLEVVRL
GGHAYSPEDM GLSRDMYLLQ LCSGVDENVV GGCAQLVFAP IDESFADDAP LLPSGFRVIP
LDQKTNPNDH QSASRTRDLA SSLDGSTKTD SETNSRLVLT IAFQFTFDNH SRDNVATMAR
QYVRNVVGSI QRVALAITPR PGSMQLPTSP EALTLVRWIT RSYSIHTGAD LFGADSQSCG
GDTLLKQLWD HSDAILCCSL KTNASPVFTF ANQAGLDMLE TTLVALQDIM LDKTLDDSGR
RALCSEFAKI MQQGYANLPA GICVSSMGRP VSYEQATVWK VVDDNESNHC LAFTLVSWSF
V
