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DOF32_ARATH
ID   DOF32_ARATH             Reviewed;         245 AA.
AC   Q9M1E6; Q9SUJ4;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Dof zinc finger protein DOF3.2 {ECO:0000303|PubMed:12475498};
DE            Short=AtDOF3.2 {ECO:0000303|PubMed:12475498};
DE   AltName: Full=Protein PHLOEM EARLY DOF6 {ECO:0000303|PubMed:30626969};
GN   Name=DOF3.2 {ECO:0000303|PubMed:12475498};
GN   Synonyms=DOF6 {ECO:0000303|PubMed:22155632};
GN   OrderedLocusNames=At3g45610 {ECO:0000312|Araport:AT3G45610};
GN   ORFNames=F9K21.190 {ECO:0000312|EMBL:CAB75490.1};
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 [MRNA].
RC   STRAIN=cv. C24;
RA   Malkowski B., Plesch G., Mueller-Roeber B.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [4]
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12475498; DOI=10.1016/s1360-1385(02)02362-2;
RA   Yanagisawa S.;
RT   "The Dof family of plant transcription factors.";
RL   Trends Plant Sci. 7:555-560(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH TCP14, AND DEVELOPMENTAL STAGE.
RX   PubMed=22155632; DOI=10.1093/jxb/err388;
RA   Rueda-Romero P., Barrero-Sicilia C., Gomez-Cadenas A., Carbonero P.,
RA   Onate-Sanchez L.;
RT   "Arabidopsis thaliana DOF6 negatively affects germination in non-after-
RT   ripened seeds and interacts with TCP14.";
RL   J. Exp. Bot. 63:1937-1949(2012).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP   CYTOKININ.
RX   PubMed=30626969; DOI=10.1038/s41586-018-0839-y;
RA   Miyashima S., Roszak P., Sevilem I., Toyokura K., Blob B., Heo J.-O.,
RA   Mellor N., Help-Rinta-Rahko H., Otero S., Smet W., Boekschoten M.,
RA   Hooiveld G., Hashimoto K., Smetana O., Siligato R., Wallner E.-S.,
RA   Maehoenen A.P., Kondo Y., Melnyk C.W., Greb T., Nakajima K., Sozzani R.,
RA   Bishopp A., De Rybel B., Helariutta Y.;
RT   "Mobile PEAR transcription factors integrate positional cues to prime
RT   cambial growth.";
RL   Nature 565:490-494(2019).
CC   -!- FUNCTION: Transcription factor that negatively affects seed germination
CC       and opposes TCP14 function in the regulation of a specific set of
CC       abscisic acid-related genes (PubMed:22155632). The PEAR proteins (e.g.
CC       DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3) activate gene
CC       expression that promotes radial growth of protophloem sieve elements
CC       (PubMed:30626969). {ECO:0000269|PubMed:22155632,
CC       ECO:0000269|PubMed:30626969}.
CC   -!- SUBUNIT: Interacts with TCP14. {ECO:0000269|PubMed:22155632}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071}.
CC   -!- TISSUE SPECIFICITY: The PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2,
CC       DOF1.1, DOF5.6 and DOF5.3) form a short-range concentration gradient
CC       that peaks at protophloem sieve elements (PSE).
CC       {ECO:0000269|PubMed:30626969}.
CC   -!- DEVELOPMENTAL STAGE: The transcript levels of the gene accumulate in
CC       dry seeds and decay gradually during after-ripening and also upon seed
CC       imbibition. {ECO:0000269|PubMed:22155632}.
CC   -!- INDUCTION: By cytokinin in procambium. {ECO:0000269|PubMed:30626969}.
CC   -!- DISRUPTION PHENOTYPE: The pear1 pear2 dof6 tmo6 quadruple mutant plants
CC       showed a uniform reduction in radial growth, associated with
CC       compromised symplastic trafficking. {ECO:0000269|PubMed:30626969}.
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DR   EMBL; AJ243033; CAB51901.1; -; mRNA.
DR   EMBL; AL138657; CAB75490.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78050.1; -; Genomic_DNA.
DR   EMBL; AY062783; AAL32861.1; -; mRNA.
DR   EMBL; BT006284; AAP13392.1; -; mRNA.
DR   PIR; T47501; T47501.
DR   RefSeq; NP_190147.1; NM_114430.3.
DR   AlphaFoldDB; Q9M1E6; -.
DR   BioGRID; 9023; 8.
DR   IntAct; Q9M1E6; 3.
DR   STRING; 3702.AT3G45610.1; -.
DR   PaxDb; Q9M1E6; -.
DR   PRIDE; Q9M1E6; -.
DR   EnsemblPlants; AT3G45610.1; AT3G45610.1; AT3G45610.
DR   GeneID; 823703; -.
DR   Gramene; AT3G45610.1; AT3G45610.1; AT3G45610.
DR   KEGG; ath:AT3G45610; -.
DR   Araport; AT3G45610; -.
DR   TAIR; locus:2085697; AT3G45610.
DR   eggNOG; ENOG502RB9Y; Eukaryota.
DR   HOGENOM; CLU_036438_2_1_1; -.
DR   InParanoid; Q9M1E6; -.
DR   OMA; NISNEQM; -.
DR   OrthoDB; 1111544at2759; -.
DR   PhylomeDB; Q9M1E6; -.
DR   PRO; PR:Q9M1E6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1E6; baseline and differential.
DR   Genevisible; Q9M1E6; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   GO; GO:0090057; P:root radial pattern formation; IGI:TAIR.
DR   InterPro; IPR045174; Dof.
DR   InterPro; IPR003851; Znf_Dof.
DR   PANTHER; PTHR31992; PTHR31992; 1.
DR   Pfam; PF02701; zf-Dof; 1.
DR   PROSITE; PS01361; ZF_DOF_1; 1.
DR   PROSITE; PS50884; ZF_DOF_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..245
FT                   /note="Dof zinc finger protein DOF3.2"
FT                   /id="PRO_0000074278"
FT   ZN_FING         40..94
FT                   /note="Dof-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   REGION          15..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   CONFLICT        18
FT                   /note="T -> S (in Ref. 1; CAB51901)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  26958 MW;  E7AA65580BF03C3A CRC64;
     MDYSSMHQNV MGVSSCSTQD YQNQKKPLSA TRPAPPEQSL RCPRCDSTNT KFCYYNNYSL
     SQPRYFCKSC RRYWTKGGIL RNIPIGGAYR KHKRSSSATK SLRTTPEPTM THDGKSFPTA
     SFGYNNNNIS NEQMELGLAY ALLNKQPLGV SSHLGFGSSQ SPMAMDGVYG TTSHQMENTG
     YAFGNGGGGM EQMATSDPNR VLWGFPWQMN MGGGSGHGHG HVDQIDSGRE IWSSTVNYIN
     TGALL
 
 
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