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HDG11_ARATH
ID   HDG11_ARATH             Reviewed;         722 AA.
AC   Q9FX31;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Homeobox-leucine zipper protein HDG11 {ECO:0000305};
DE   AltName: Full=HD-ZIP protein HDG11 {ECO:0000305};
DE   AltName: Full=Homeodomain GLABRA 2-like protein 11 {ECO:0000303|PubMed:10809443};
DE   AltName: Full=Homeodomain transcription factor HDG11 {ECO:0000305};
DE   AltName: Full=Protein ENHANCED DROUGHT TOLERANCE 1 {ECO:0000303|PubMed:18451323};
DE   AltName: Full=Protein HOMEODOMAIN GLABROUS 11 {ECO:0000303|PubMed:16778018};
GN   Name=HDG11 {ECO:0000303|PubMed:16778018};
GN   Synonyms=EDT1 {ECO:0000303|PubMed:18451323},
GN   HDGL2-11 {ECO:0000303|PubMed:10809443};
GN   OrderedLocusNames=At1g73360 {ECO:0000312|Araport:AT1G73360};
GN   ORFNames=T9L24.43 {ECO:0000312|EMBL:AAG30978.1};
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=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   [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   GENE FAMILY.
RX   PubMed=10809443; DOI=10.1023/a:1006368316413;
RA   Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT   "Organization and structural evolution of four multigene families in
RT   Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL   Plant Mol. Biol. 42:703-717(2000).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16778018; DOI=10.1104/pp.106.077388;
RA   Nakamura M., Katsumata H., Abe M., Yabe N., Komeda Y., Yamamoto K.T.,
RA   Takahashi T.;
RT   "Characterization of the class IV homeodomain-leucine zipper gene family in
RT   Arabidopsis.";
RL   Plant Physiol. 141:1363-1375(2006).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18451323; DOI=10.1105/tpc.108.058263;
RA   Yu H., Chen X., Hong Y.Y., Wang Y., Xu P., Ke S.D., Liu H.Y., Zhu J.K.,
RA   Oliver D.J., Xiang C.B.;
RT   "Activated expression of an Arabidopsis HD-START protein confers drought
RT   tolerance with improved root system and reduced stomatal density.";
RL   Plant Cell 20:1134-1151(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=23095885; DOI=10.1242/dev.082925;
RA   Roeder A.H.K., Cunha A., Ohno C.K., Meyerowitz E.M.;
RT   "Cell cycle regulates cell type in the Arabidopsis sepal.";
RL   Development 139:4416-4427(2012).
RN   [8]
RP   FUNCTION.
RX   PubMed=24821957; DOI=10.1093/jxb/eru202;
RA   Xu P., Cai X.T., Wang Y., Xing L., Chen Q., Xiang C.B.;
RT   "HDG11 upregulates cell-wall-loosening protein genes to promote root
RT   elongation in Arabidopsis.";
RL   J. Exp. Bot. 65:4285-4295(2014).
RN   [9]
RP   FUNCTION.
RX   PubMed=24824485; DOI=10.1105/tpc.113.120360;
RA   Khosla A., Paper J.M., Boehler A.P., Bradley A.M., Neumann T.R.,
RA   Schrick K.;
RT   "HD-ZIP proteins GL2 and HDG11 have redundant functions in Arabidopsis
RT   trichomes, and GL2 activates a positive feedback loop via MYB23.";
RL   Plant Cell 26:2184-2200(2014).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP   BBM.
RC   STRAIN=cv. Columbia;
RX   PubMed=25564655; DOI=10.1242/dev.117168;
RA   Horstman A., Fukuoka H., Muino J.M., Nitsch L., Guo C., Passarinho P.,
RA   Sanchez-Perez G., Immink R., Angenent G., Boutilier K.;
RT   "AIL and HDG proteins act antagonistically to control cell proliferation.";
RL   Development 142:454-464(2015).
RN   [11]
RP   FUNCTION.
RX   PubMed=25752924; DOI=10.1111/jipb.12347;
RA   Cai X.T., Xu P., Wang Y., Xiang C.B.;
RT   "Activated expression of AtEDT1/HDG11 promotes lateral root formation in
RT   Arabidopsis mutant edt1 by upregulating jasmonate biosynthesis.";
RL   J. Integr. Plant Biol. 57:1017-1030(2015).
CC   -!- FUNCTION: Transcription factor which acts as positive regulator of
CC       drought stress tolerance. Can transactivate CIPK3, NCED3 and ERECTA
CC       (PubMed:18451323). Transactivates several cell-wall-loosening protein
CC       genes by directly binding to HD motifs in their promoters. These target
CC       genes play important roles in coordinating cell-wall extensibility with
CC       root development and growth (PubMed:24821957). Transactivates
CC       CYP74A/AOS, AOC3, OPR3 and 4CLL5/OPCL1 genes by directly binding to HD
CC       motifs in their promoters. These target genes are involved in jasmonate
CC       (JA) biosynthesis, and JA signaling affects root architecture by
CC       activating auxin signaling, which promotes lateral root formation
CC       (PubMed:25752924). Acts as negative regulator of trichome branching
CC       (PubMed:16778018, PubMed:24824485). Required for the establishment of
CC       giant cell identity on the abaxial side of sepals (PubMed:23095885).
CC       Seems to promote cell differentiation (PubMed:25564655). May regulate
CC       cell differentiation and proliferation during root and shoot meristem
CC       development (PubMed:25564655). {ECO:0000269|PubMed:16778018,
CC       ECO:0000269|PubMed:18451323, ECO:0000269|PubMed:23095885,
CC       ECO:0000269|PubMed:24821957, ECO:0000269|PubMed:24824485,
CC       ECO:0000269|PubMed:25564655, ECO:0000269|PubMed:25752924}.
CC   -!- SUBUNIT: Interacts with BBM. {ECO:0000269|PubMed:25564655}.
CC   -!- INTERACTION:
CC       Q9FX31; Q8L7H4: HDG4; NbExp=2; IntAct=EBI-4443010, EBI-4450571;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:18451323}.
CC   -!- TISSUE SPECIFICITY: Expressed in apical meristems and young epidermal
CC       tissue including trichomes and stipules. Expressed in lateral root
CC       tips, the L1 layer of apical inflorescence meristems and early flower
CC       primordia, carpel and petal epidermis, stigma papillae, ovule
CC       primordia, nucellus and embryo. {ECO:0000269|PubMed:16778018}.
CC   -!- DEVELOPMENTAL STAGE: During embryo development, expressed in all cells
CC       at the 4- and 16-cell embryo stages (PubMed:25564655). Expression is
CC       restricted to the protoderm from the globular stage onward
CC       (PubMed:25564655). In primary and lateral roots, observed in the
CC       epidermis, the outer layer of columella cells and lateral root cap
CC       (PubMed:25564655). {ECO:0000269|PubMed:25564655}.
CC   -!- DISRUPTION PHENOTYPE: Plants show excess branching of trichomes
CC       (PubMed:16778018, PubMed:24824485). In plants missing HDG3, HDG7,
CC       HDG11, PDF2 and ATML1, increased cell division leading to cell
CC       overproliferation (PubMed:25564655). {ECO:0000269|PubMed:16778018,
CC       ECO:0000269|PubMed:24824485, ECO:0000269|PubMed:25564655}.
CC   -!- MISCELLANEOUS: The gain-of-function mutant edt1 (T-DNA tagging) exhibit
CC       enhanced drought tolerance, increased root system development, reduced
CC       leaf stomatal density, increased levels of abscisic acid and prolamine,
CC       increased resistance to oxidative stress and high levels of superoxide
CC       dismutase. {ECO:0000269|PubMed:18451323}.
CC   -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC012396; AAG30978.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35449.1; -; Genomic_DNA.
DR   EMBL; BT003979; AAO42020.1; -; mRNA.
DR   EMBL; BT004915; AAO50448.1; -; mRNA.
DR   PIR; B96760; B96760.
DR   RefSeq; NP_177479.1; NM_105996.4.
DR   AlphaFoldDB; Q9FX31; -.
DR   BioGRID; 28890; 4.
DR   IntAct; Q9FX31; 4.
DR   STRING; 3702.AT1G73360.1; -.
DR   MetOSite; Q9FX31; -.
DR   PaxDb; Q9FX31; -.
DR   PRIDE; Q9FX31; -.
DR   ProteomicsDB; 230291; -.
DR   EnsemblPlants; AT1G73360.1; AT1G73360.1; AT1G73360.
DR   GeneID; 843671; -.
DR   Gramene; AT1G73360.1; AT1G73360.1; AT1G73360.
DR   KEGG; ath:AT1G73360; -.
DR   Araport; AT1G73360; -.
DR   TAIR; locus:2206880; AT1G73360.
DR   eggNOG; ENOG502QQXM; Eukaryota.
DR   HOGENOM; CLU_015002_2_1_1; -.
DR   InParanoid; Q9FX31; -.
DR   OMA; QRACERY; -.
DR   OrthoDB; 250988at2759; -.
DR   PhylomeDB; Q9FX31; -.
DR   PRO; PR:Q9FX31; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FX31; baseline and differential.
DR   Genevisible; Q9FX31; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009828; P:plant-type cell wall loosening; IMP:TAIR.
DR   GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR042160; GLABRA2/ANL2/PDF2/ATML1-like.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR45654; PTHR45654; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS50848; START; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..722
FT                   /note="Homeobox-leucine zipper protein HDG11"
FT                   /id="PRO_0000331672"
FT   DOMAIN          227..460
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   DNA_BIND        32..91
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          81..161
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   722 AA;  79120 MW;  1A865CC474F8C178 CRC64;
     MSFVVGVGGS GSGSGGDGGG SHHHDGSETD RKKKRYHRHT AQQIQRLESS FKECPHPDEK
     QRNQLSRELG LAPRQIKFWF QNRRTQLKAQ HERADNSALK AENDKIRCEN IAIREALKHA
     ICPNCGGPPV SEDPYFDEQK LRIENAHLRE ELERMSTIAS KYMGRPISQL STLHPMHISP
     LDLSMTSLTG CGPFGHGPSL DFDLLPGSSM AVGPNNNLQS QPNLAISDMD KPIMTGIALT
     AMEELLRLLQ TNEPLWTRTD GCRDILNLGS YENVFPRSSN RGKNQNFRVE ASRSSGIVFM
     NAMALVDMFM DCVKWTELFP SIIAASKTLA VISSGMGGTH EGALHLLYEE MEVLSPLVAT
     REFCELRYCQ QTEQGSWIVV NVSYDLPQFV SHSQSYRFPS GCLIQDMPNG YSKVTWVEHI
     ETEEKELVHE LYREIIHRGI AFGADRWVTT LQRMCERFAS LSVPASSSRD LGGVILSPEG
     KRSMMRLAQR MISNYCLSVS RSNNTRSTVV SELNEVGIRV TAHKSPEPNG TVLCAATTFW
     LPNSPQNVFN FLKDERTRPQ WDVLSNGNAV QEVAHISNGS HPGNCISVLR GSNATHSNNM
     LILQESSTDS SGAFVVYSPV DLAALNIAMS GEDPSYIPLL SSGFTISPDG NGSNSEQGGA
     STSSGRASAS GSLITVGFQI MVSNLPTAKL NMESVETVNN LIGTTVHQIK TALSGPTAST
     TA
 
 
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