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ATHB8_ARATH
ID   ATHB8_ARATH             Reviewed;         833 AA.
AC   Q39123;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Homeobox-leucine zipper protein ATHB-8;
DE   AltName: Full=HD-ZIP protein ATHB-8;
DE   AltName: Full=Homeodomain transcription factor ATHB-8;
GN   Name=ATHB-8; Synonyms=HB8; OrderedLocusNames=At4g32880; ORFNames=T16I18.90;
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], DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=8575317; DOI=10.1242/dev.121.12.4171;
RA   Baima S., Nobili F., Sessa G., Lucchetti S., Ruberti I., Morelli G.;
RT   "The expression of the Athb-8 homeobox gene is restricted to provascular
RT   cells in Arabidopsis thaliana.";
RL   Development 121:4171-4182(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sessa G., Carabelli M., Ciarbelli A.R., Ruzza V., Steindler C., Ruberti I.;
RT   "Nucleotide sequence of the Arabidopsis ATHB-8 mRNA, encoding an HD-Zip III
RT   protein.";
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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;
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   [6]
RP   FUNCTION.
RX   PubMed=11402194; DOI=10.1104/pp.126.2.643;
RA   Baima S., Possenti M., Matteucci A., Wisman E., Altamura M.M., Ruberti I.,
RA   Morelli G.;
RT   "The arabidopsis ATHB-8 HD-zip protein acts as a differentiation-promoting
RT   transcription factor of the vascular meristems.";
RL   Plant Physiol. 126:643-655(2001).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12447534; DOI=10.1007/s00425-002-0847-9;
RA   Kang J., Dengler N.;
RT   "Cell cycling frequency and expression of the homeobox gene ATHB-8 during
RT   leaf vein development in Arabidopsis.";
RL   Planta 216:212-219(2002).
RN   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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 regulation of
CC       vascular development. May promote differentiation of precambial and
CC       cambial cells. {ECO:0000269|PubMed:11402194,
CC       ECO:0000269|PubMed:15598805}.
CC   -!- SUBUNIT: Interacts with ESR1 and ESR2 (PubMed:17376809). Interacts with
CC       ZPR3 (PubMed:18408069). {ECO:0000269|PubMed:17376809,
CC       ECO:0000269|PubMed:18408069}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the procambial cells and the
CC       developing vascular system of embryos, roots and shoots. Expressed
CC       during the early stages of revascularization after cutting experiment.
CC       {ECO:0000269|PubMed:12447534, ECO:0000269|PubMed:8575317}.
CC   -!- INDUCTION: By auxin. Repressed by miR165. {ECO:0000269|PubMed:17237362,
CC       ECO:0000269|PubMed:8575317}.
CC   -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class III subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z50851; CAA90703.1; -; Genomic_DNA.
DR   EMBL; AJ441292; CAD29660.1; -; mRNA.
DR   EMBL; AL161582; CAB80005.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86138.1; -; Genomic_DNA.
DR   EMBL; AY099631; AAM20482.1; -; mRNA.
DR   EMBL; BT008798; AAP68237.1; -; mRNA.
DR   PIR; T10695; T10695.
DR   RefSeq; NP_195014.1; NM_119441.5.
DR   AlphaFoldDB; Q39123; -.
DR   SMR; Q39123; -.
DR   BioGRID; 14709; 2.
DR   IntAct; Q39123; 3.
DR   STRING; 3702.AT4G32880.1; -.
DR   iPTMnet; Q39123; -.
DR   PaxDb; Q39123; -.
DR   PRIDE; Q39123; -.
DR   ProteomicsDB; 246557; -.
DR   EnsemblPlants; AT4G32880.1; AT4G32880.1; AT4G32880.
DR   GeneID; 829424; -.
DR   Gramene; AT4G32880.1; AT4G32880.1; AT4G32880.
DR   KEGG; ath:AT4G32880; -.
DR   Araport; AT4G32880; -.
DR   TAIR; locus:2134088; AT4G32880.
DR   eggNOG; ENOG502QPKR; Eukaryota.
DR   HOGENOM; CLU_012517_0_0_1; -.
DR   InParanoid; Q39123; -.
DR   OMA; EGWSILE; -.
DR   OrthoDB; 183246at2759; -.
DR   PhylomeDB; Q39123; -.
DR   PRO; PR:Q39123; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q39123; baseline and differential.
DR   Genevisible; Q39123; AT.
DR   GO; GO:0005634; C:nucleus; IDA: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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010014; P:meristem initiation; IMP:TAIR.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:TAIR.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:TAIR.
DR   GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
DR   GO; GO:0010067; P:procambium histogenesis; IEP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR   GO; GO:0010089; P:xylem development; 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..833
FT                   /note="Homeobox-leucine zipper protein ATHB-8"
FT                   /id="PRO_0000331658"
FT   DOMAIN          150..378
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   DNA_BIND        12..75
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   COILED          70..108
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   833 AA;  91996 MW;  656CA177466BEFEA CRC64;
     MGGGSNNSHN MDNGKYVRYT PEQVEALERL YNDCPKPSSM RRQQLIRECP ILSNIEPKQI
     KVWFQNRRCR EKQRKEASRL QAVNRKLTAM NKLLMEENDR LQKQVSHLVY ENSYFRQHPQ
     NQGNLATTDT SCESVVTSGQ HHLTPQHQPR DASPAGLLSI ADETLTEFIS KATGTAVEWV
     QMPGMKPGPD SIGIVAISHG CTGIAARACG LVGLDPTRVA EILKDKPCWL RDCRSLDIVN
     VLSTANGGTL ELIYMQLYAP TTLAPARDFW MLRYTSVMED GSLVICERSL NNTQNGPSMP
     PSPHFVRAEI LPSGYLIRPC EGGGSILHIV DHFDLEPWSV PEVLRSLYES STLLAQRTTM
     AALRYLRQIS QEISQPNVTG WGRRPAALRA LSQRLSKGFN EAVNGFSDEG WSILESDGID
     DVTLLVNSSP TKMMMTSSLP FANGYTSMPS AVLCAKASML LQNVPPSILL RFLREHRQEW
     ADNSIDAYSA AAIKAGPCSL PIPRPGSFGG QVILPLAHTI ENEEFMEVIK LESLGHYQED
     MMMPADIFLL QMCSGVDENA VESCAELIFA PIDASFSDDA PIIPSGFRII PLDSKSEGLS
     PNRTLDLASA LDVGSRTAGD SCGSRGNSKS VMTIAFQLAF EMHMQENVAS MARQYVRSVI
     ASVQRVALAL SPSSHQLSGL RPPPASPEAH TLARWISHSY RCYLGVDLLK PHGTDLLKSL
     WHHPDAVMCC SLKALSPVFT FANQAGLDML ETTLVALQDI TLDKIFDNNN GKKTLSSEFP
     QIMQQGFMCM DGGICMSSMG RAVTYEKAVG WKVLNDDEDP HCICFMFLNW SFI
 
 
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