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DOF53_ARATH
ID   DOF53_ARATH             Reviewed;         257 AA.
AC   Q84TE9; Q0WRV9; Q8LDE1; Q9LSS6;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Dof zinc finger protein DOF5.3 {ECO:0000303|PubMed:12475498};
DE            Short=AtDOF5.3 {ECO:0000303|PubMed:12475498};
DE   AltName: Full=Protein PHLOEM EARLY DOF TMO6 {ECO:0000303|PubMed:30626969};
DE   AltName: Full=Protein TARGET OF MONOPTEROS 6 {ECO:0000303|PubMed:20220754};
DE            Short=Protein TARGET OF MP 6 {ECO:0000303|PubMed:20220754};
GN   Name=DOF5.3 {ECO:0000303|PubMed:12475498};
GN   Synonyms=TMO6 {ECO:0000303|PubMed:20220754};
GN   OrderedLocusNames=At5g60200 {ECO:0000312|Araport:AT5G60200};
GN   ORFNames=F15L12.9 {ECO:0000312|EMBL:BAA97501.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=20563990; DOI=10.1387/ijdb.093006jg;
RA   Gardiner J., Sherr I., Scarpella E.;
RT   "Expression of DOF genes identifies early stages of vascular development in
RT   Arabidopsis leaves.";
RL   Int. J. Dev. Biol. 54:1389-1396(2010).
RN   [9]
RP   INDUCTION BY MONOPTEROS, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=20220754; DOI=10.1038/nature08836;
RA   Schlereth A., Moller B., Liu W., Kientz M., Flipse J., Rademacher E.H.,
RA   Schmid M., Jurgens G., Weijers D.;
RT   "MONOPTEROS controls embryonic root initiation by regulating a mobile
RT   transcription factor.";
RL   Nature 464:913-916(2010).
RN   [10]
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 binds specifically to a 5'-AA[AG]G-
CC       3' consensus core sequence (By similarity). 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:0000250|UniProtKB:Q9M2U1,
CC       ECO:0000269|PubMed:30626969}.
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) (PubMed:30626969).
CC       Accumulates in the stele (PubMed:20563990).
CC       {ECO:0000269|PubMed:20563990, ECO:0000269|PubMed:30626969}.
CC   -!- DEVELOPMENTAL STAGE: In embryos, present in cells relevant for root
CC       initiation and later in vascular tissues. At the globular stage,
CC       accumulates in cells adjacent to the hypophysis (extra-embryonic cell
CC       specified to become the founder cell of the primary root meristem)
CC       (PubMed:20220754). Expressed at preprocambial stages first in wide
CC       domains, and later confined to sites of vein development. In young
CC       seedlings, first observed in the central region of leaves primordia,
CC       and later strongly expressed at sites of midvein, first and second
CC       loops, and higher-order veins (PubMed:20563990).
CC       {ECO:0000269|PubMed:20220754, ECO:0000269|PubMed:20563990}.
CC   -!- INDUCTION: By cytokinin in procambium (PubMed:30626969). Induced by the
CC       transcription factor MONOPTEROS (MP) in cells relevant for root
CC       initiation, and later in vascular tissues and hypophysis
CC       (PubMed:20220754). {ECO:0000269|PubMed:20220754,
CC       ECO:0000269|PubMed:30626969}.
CC   -!- DISRUPTION PHENOTYPE: The pear1 pear2 tmo6 triple mutant variably
CC       displays reduced radial growth. The pear1 pear2 dof6 tmo6 quadruple
CC       mutant plants showed a greater uniform reduction in radial growth,
CC       associated with compromised symplastic trafficking.
CC       {ECO:0000269|PubMed:30626969}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM63264.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA97501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB026632; BAA97501.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97292.1; -; Genomic_DNA.
DR   EMBL; AK228185; BAF00140.1; -; mRNA.
DR   EMBL; BT005866; AAO64801.1; -; mRNA.
DR   EMBL; AY086054; AAM63264.1; ALT_INIT; mRNA.
DR   EMBL; AB493803; BAH30641.1; -; mRNA.
DR   RefSeq; NP_568920.1; NM_125413.4.
DR   AlphaFoldDB; Q84TE9; -.
DR   BioGRID; 21386; 4.
DR   STRING; 3702.AT5G60200.1; -.
DR   PaxDb; Q84TE9; -.
DR   PRIDE; Q84TE9; -.
DR   ProteomicsDB; 222125; -.
DR   EnsemblPlants; AT5G60200.1; AT5G60200.1; AT5G60200.
DR   GeneID; 836142; -.
DR   Gramene; AT5G60200.1; AT5G60200.1; AT5G60200.
DR   KEGG; ath:AT5G60200; -.
DR   Araport; AT5G60200; -.
DR   TAIR; locus:2144030; AT5G60200.
DR   eggNOG; ENOG502RB9Y; Eukaryota.
DR   HOGENOM; CLU_036438_2_1_1; -.
DR   OMA; MNGESFG; -.
DR   OrthoDB; 1111544at2759; -.
DR   PhylomeDB; Q84TE9; -.
DR   PRO; PR:Q84TE9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q84TE9; baseline and differential.
DR   Genevisible; Q84TE9; 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:0010087; P:phloem or xylem histogenesis; IDA:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   GO; GO:0048364; P:root development; IEP: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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..257
FT                   /note="Dof zinc finger protein DOF5.3"
FT                   /id="PRO_0000074293"
FT   ZN_FING         55..109
FT                   /note="Dof-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   REGION          23..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT   CONFLICT        31
FT                   /note="P -> Q (in Ref. 5; AAM63264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="V -> AAA (in Ref. 5; AAM63264)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   257 AA;  28201 MW;  E9A29940F86EB693 CRC64;
     MDHLLQHQDV FGNYNKAREA MGLSYSSNPT PLDNDQKKPS PATAVTRPQP PELALRCPRC
     DSTNTKFCYY NNYSLTQPRY FCKSCRRYWT KGGTLRNIPV GGGCRKNKRS TSSAARSLRT
     TPEPASHDGK VFSAAGFNGY SNNEHIDLSL AFALLNKQHP GSSSQLGFHS ELGSSHQSDM
     EGMFGTSQQK ENATYAFGNG SSGLGDPSRV LWGFPWQMNG ESFGMMNIGG GGGHVDQIDS
     GREMWTNMNY INSGALM
 
 
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