WHY1_ARATH
ID WHY1_ARATH Reviewed; 263 AA.
AC Q9M9S3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Single-stranded DNA-binding protein WHY1, chloroplastic;
DE AltName: Full=Protein PLASTID TRANSCRIPTIONALLY ACTIVE 1;
DE AltName: Full=Protein WHIRLY 1;
DE Short=AtWHY1;
DE Flags: Precursor;
GN Name=WHY1; Synonyms=PTAC1; OrderedLocusNames=At1g14410; ORFNames=F14L17.18;
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF GLY-148 AND
RP PRO-183.
RX PubMed=14960277; DOI=10.1016/s1534-5807(04)00028-0;
RA Desveaux D., Subramaniam R., Despres C., Mess J.N., Levesque C.,
RA Fobert P.R., Dangl J.L., Brisson N.;
RT "A 'Whirly' transcription factor is required for salicylic acid-dependent
RT disease resistance in Arabidopsis.";
RL Dev. Cell 6:229-240(2004).
RN [5]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15967440; DOI=10.1016/j.febslet.2005.05.059;
RA Krause K., Kilbienski I., Mulisch M., Roediger A., Schaefer A.,
RA Krupinska K.;
RT "DNA-binding proteins of the Whirly family in Arabidopsis thaliana are
RT targeted to the organelles.";
RL FEBS Lett. 579:3707-3712(2005).
RN [6]
RP GENE FAMILY.
RX PubMed=15708347; DOI=10.1016/j.tplants.2004.12.008;
RA Desveaux D., Marechal A., Brisson N.;
RT "Whirly transcription factors: defense gene regulation and beyond.";
RL Trends Plant Sci. 10:95-102(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17217467; DOI=10.1111/j.1365-313x.2006.02974.x;
RA Yoo H.H., Kwon C., Lee M.M., Chung I.K.;
RT "Single-stranded DNA binding factor AtWHY1 modulates telomere length
RT homeostasis in Arabidopsis.";
RL Plant J. 49:442-451(2007).
RN [8]
RP FUNCTION, INDUCTION BY SALICYLIC ACID, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19669906; DOI=10.1007/s11103-009-9533-7;
RA Xiong J.Y., Lai C.X., Qu Z., Yang X.Y., Qin X.H., Liu G.Q.;
RT "Recruitment of AtWHY1 and AtWHY3 by a distal element upstream of the
RT kinesin gene AtKP1 to mediate transcriptional repression.";
RL Plant Mol. Biol. 71:437-449(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19666500; DOI=10.1073/pnas.0901710106;
RA Marechal A., Parent J.S., Veronneau-Lafortune F., Joyeux A., Lang B.F.,
RA Brisson N.;
RT "Whirly proteins maintain plastid genome stability in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14693-14698(2009).
RN [10]
RP FUNCTION.
RX PubMed=20551348; DOI=10.1105/tpc.109.071399;
RA Cappadocia L., Marechal A., Parent J.S., Lepage E., Sygusch J., Brisson N.;
RT "Crystal structures of DNA-Whirly complexes and their role in Arabidopsis
RT organelle genome repair.";
RL Plant Cell 22:1849-1867(2010).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF LYS-91.
RX PubMed=21911368; DOI=10.1093/nar/gkr740;
RA Cappadocia L., Parent J.S., Zampini E., Lepage E., Sygusch J., Brisson N.;
RT "A conserved lysine residue of plant Whirly proteins is necessary for
RT higher order protein assembly and protection against DNA damage.";
RL Nucleic Acids Res. 40:258-269(2012).
CC -!- FUNCTION: Single-stranded DNA-binding protein that functions in both
CC chloroplasts and nucleus. In chloroplasts, maintains plastid genome
CC stability by preventing break-induced and short homology-dependent
CC illegitimate recombinations. In nucleus, modulates telomere length
CC homeostasis by inhibiting the action of the telomerase at the extreme
CC termini of chromosomes. Is recruited to a distal element upstream of
CC the kinesin KP1 to mediate the transcriptional repression of KP1. Is
CC required for full salicylic acid-dependent plant disease resistance
CC responses. Can bind double-stranded DNA in vivo.
CC {ECO:0000269|PubMed:14960277, ECO:0000269|PubMed:17217467,
CC ECO:0000269|PubMed:19666500, ECO:0000269|PubMed:19669906,
CC ECO:0000269|PubMed:20551348, ECO:0000269|PubMed:21911368}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15967440}. Nucleus {ECO:0000269|PubMed:14960277,
CC ECO:0000269|PubMed:15967440}. Note=Can localize to both chloroplast and
CC nucleus (PubMed:15967440).
CC -!- INDUCTION: By salicylic acid (SA) and infection by H.parasitica.
CC {ECO:0000269|PubMed:14960277, ECO:0000269|PubMed:19669906}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants present a progressive lengthening of
CC telomeric repeats. {ECO:0000269|PubMed:17217467,
CC ECO:0000269|PubMed:19666500}.
CC -!- SIMILARITY: Belongs to the Whirly family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305|PubMed:15967440}.
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DR EMBL; AC012188; AAF43941.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29160.1; -; Genomic_DNA.
DR EMBL; AF332452; AAG48815.1; -; mRNA.
DR EMBL; AF370156; AAK43971.1; -; mRNA.
DR EMBL; AY059097; AAL15203.1; -; mRNA.
DR PIR; F86278; F86278.
DR RefSeq; NP_172893.1; NM_101308.4.
DR PDB; 4KOO; X-ray; 1.88 A; A/B/C/D=74-241.
DR PDBsum; 4KOO; -.
DR AlphaFoldDB; Q9M9S3; -.
DR SMR; Q9M9S3; -.
DR BioGRID; 23243; 3.
DR ComplexPortal; CPX-1337; WHY1 complex.
DR STRING; 3702.AT1G14410.1; -.
DR PaxDb; Q9M9S3; -.
DR PRIDE; Q9M9S3; -.
DR ProteomicsDB; 242654; -.
DR EnsemblPlants; AT1G14410.1; AT1G14410.1; AT1G14410.
DR GeneID; 838003; -.
DR Gramene; AT1G14410.1; AT1G14410.1; AT1G14410.
DR KEGG; ath:AT1G14410; -.
DR Araport; AT1G14410; -.
DR TAIR; locus:2012542; AT1G14410.
DR eggNOG; ENOG502QRRY; Eukaryota.
DR HOGENOM; CLU_062935_1_0_1; -.
DR InParanoid; Q9M9S3; -.
DR OMA; KESCEFF; -.
DR OrthoDB; 1637760at2759; -.
DR PhylomeDB; Q9M9S3; -.
DR PRO; PR:Q9M9S3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9S3; baseline and differential.
DR Genevisible; Q9M9S3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:ComplexPortal.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:ComplexPortal.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:TAIR.
DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IDA:ComplexPortal.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:ComplexPortal.
DR Gene3D; 2.30.31.10; -; 1.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR013742; Whirly.
DR PANTHER; PTHR31745; PTHR31745; 1.
DR Pfam; PF08536; Whirly; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Plant defense; Plastid; Reference proteome; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..263
FT /note="Single-stranded DNA-binding protein WHY1,
FT chloroplastic"
FT /id="PRO_0000420447"
FT REGION 89..94
FT /note="Required for ssDNA binding"
FT /evidence="ECO:0000250"
FT MOTIF 167..180
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MUTAGEN 91
FT /note="K->A: No effect on DNA binding. Affects its function
FT in DNA repair."
FT /evidence="ECO:0000269|PubMed:21911368"
FT MUTAGEN 148
FT /note="G->E: In atwhy1.2; reduces binding activity to
FT single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:14960277"
FT MUTAGEN 183
FT /note="P->S: In atwhy1.1; reduces binding activity to
FT single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:14960277"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:4KOO"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4KOO"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4KOO"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:4KOO"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:4KOO"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:4KOO"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:4KOO"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:4KOO"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:4KOO"
SQ SEQUENCE 263 AA; 29058 MW; E90F85763198C614 CRC64;
MSQLLSTPLM AVNSNPRFLS SSSVLVTGGF AVKRHGFALK PTTKTVKLFS VKSRQTDYFE
KQRFGDSSSS PSPAEGLPAR FYVGHSIYKG KAALTVDPRA PEFVALDSGA FKLSKDGFLL
LQFAPSAGVR QYDWSKKQVF SLSVTEIGTL VSLGPRESCE FFHDPFKGKS DEGKVRKVLK
VEPLPDGSGH FFNLSVQNKL VNVDESIYIP ITRAEFAVLI SAFNFVLPYL IGWHAFANSI
KPEETSRVNN ASPNYGGDYE WNR
