WHY2_ARATH
ID WHY2_ARATH Reviewed; 238 AA.
AC Q8VYF7; Q9FVV2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Single-stranded DNA-binding protein WHY2, mitochondrial;
DE AltName: Full=Protein WHIRLY 2;
DE Short=AtWHY2;
DE Flags: Precursor;
GN Name=WHY2; OrderedLocusNames=At1g71260; ORFNames=F3I17.9;
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 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 [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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18423020; DOI=10.1186/1471-2229-8-42;
RA Marechal A., Parent J.S., Sabar M., Veronneau-Lafortune F., Abou-Rached C.,
RA Brisson N.;
RT "Overexpression of mtDNA-associated AtWhy2 compromises mitochondrial
RT function.";
RL BMC Plant Biol. 8:42-42(2008).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22762281; DOI=10.1111/j.1365-313x.2012.05097.x;
RA Janicka S., Kuehn K., Le Ret M., Bonnard G., Imbault P., Augustyniak H.,
RA Gualberto J.M.;
RT "A RAD52-like single-stranded DNA binding protein affects mitochondrial DNA
RT repair by recombination.";
RL Plant J. 72:423-435(2012).
CC -!- FUNCTION: Single-stranded DNA-binding protein that associates with
CC mitochondrial DNA and may play a role in the regulation of the gene
CC expression machinery. Seems also to be required to prevent break-
CC induced DNA rearrangements in the mitochondrial genome. Can bind to
CC melt double-stranded DNA in vivo. {ECO:0000269|PubMed:18423020,
CC ECO:0000269|PubMed:20551348, ECO:0000269|PubMed:22762281}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VYF7; Q9SAC6: GWD1; NbExp=3; IntAct=EBI-15219982, EBI-2355356;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15967440,
CC ECO:0000269|PubMed:18423020, ECO:0000269|PubMed:22762281}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18423020}.
CC -!- MISCELLANEOUS: Plants over-expressing WHY2 are small with dark-green
CC distorted leaves, exhibit early senescence and produces shorter
CC siliques with half the amount of seeds found in wild-type plants.
CC {ECO:0000305|PubMed:18423020}.
CC -!- SIMILARITY: Belongs to the Whirly family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC016162; AAG51881.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35181.1; -; Genomic_DNA.
DR EMBL; AY072110; AAL59932.1; -; mRNA.
DR EMBL; AY122961; AAM67494.1; -; mRNA.
DR EMBL; AB493532; BAH30370.1; -; mRNA.
DR PIR; C96737; C96737.
DR RefSeq; NP_177282.2; NM_105795.5.
DR PDB; 4KOP; X-ray; 1.75 A; A/B/C/D=45-212.
DR PDBsum; 4KOP; -.
DR AlphaFoldDB; Q8VYF7; -.
DR SMR; Q8VYF7; -.
DR BioGRID; 28687; 7.
DR ComplexPortal; CPX-3584; WHY2 complex.
DR IntAct; Q8VYF7; 5.
DR STRING; 3702.AT1G71260.1; -.
DR MetOSite; Q8VYF7; -.
DR PaxDb; Q8VYF7; -.
DR PRIDE; Q8VYF7; -.
DR ProteomicsDB; 242640; -.
DR EnsemblPlants; AT1G71260.1; AT1G71260.1; AT1G71260.
DR GeneID; 843467; -.
DR Gramene; AT1G71260.1; AT1G71260.1; AT1G71260.
DR KEGG; ath:AT1G71260; -.
DR Araport; AT1G71260; -.
DR TAIR; locus:2032293; AT1G71260.
DR eggNOG; ENOG502QRRY; Eukaryota.
DR HOGENOM; CLU_062935_0_0_1; -.
DR InParanoid; Q8VYF7; -.
DR OMA; GAIMLSW; -.
DR OrthoDB; 1637760at2759; -.
DR PhylomeDB; Q8VYF7; -.
DR PRO; PR:Q8VYF7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYF7; baseline and differential.
DR Genevisible; Q8VYF7; AT.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; DNA damage; DNA repair; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..238
FT /note="Single-stranded DNA-binding protein WHY2,
FT mitochondrial"
FT /id="PRO_0000420448"
FT REGION 62..67
FT /note="Required for ssDNA binding"
FT /evidence="ECO:0000250"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4KOP"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:4KOP"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4KOP"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:4KOP"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:4KOP"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:4KOP"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:4KOP"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4KOP"
SQ SEQUENCE 238 AA; 26295 MW; F5586CABDABF4E02 CRC64;
MMKQARSLLS RSLCDQSKSL FEASTLRGFA SWSNSSTPGR GFPGKDAAKP SGRLFAPYSI
FKGKAALSVE PVLPSFTEID SGNLRIDRRG SLMMTFMPAI GERKYDWEKK QKFALSPTEV
GSLISMGSKD SSEFFHDPSM KSSNAGQVRK SLSVKPHADG SGYFISLSVN NSILKTNDYF
VVPVTKAEFA VMKTAFSFAL PHIMGWNRLT GHVNTEALPS RNVSHLKTEP QLELEWDK
