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WHY1_SOLTU
ID   WHY1_SOLTU              Reviewed;         274 AA.
AC   Q9LL85;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Single-stranded DNA-binding protein WHY1, chloroplastic;
DE   AltName: Full=DNA-binding protein p24;
DE   AltName: Full=PR-10a binding factor 2;
DE            Short=PBF-2;
DE   AltName: Full=Protein WHIRLY 1;
DE            Short=StWhy1;
DE   Flags: Precursor;
GN   Name=WHY1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-123 AND 192-198,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Kennebec;
RX   PubMed=10948264; DOI=10.2307/3871144;
RA   Desveaux D., Despres C., Joyeux A., Subramaniam R., Brisson N.;
RT   "PBF-2 is a novel single-stranded DNA binding factor implicated in PR-10a
RT   gene activation in potato.";
RL   Plant Cell 12:1477-1489(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44;
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [3]
RP   FUNCTION.
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 68-273 IN COMPLEX WITH
RP   SINGLE-STRANDED DNA, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP   100-LYS--LEU-105.
RX   PubMed=12080340; DOI=10.1038/nsb814;
RA   Desveaux D., Allard J., Brisson N., Sygusch J.;
RT   "A new family of plant transcription factors displays a novel ssDNA-binding
RT   surface.";
RL   Nat. Struct. Biol. 9:512-517(2002).
CC   -!- FUNCTION: Single-stranded DNA-binding protein that acts as a
CC       transcriptional activator of the pathogenesis-related gene PR-10a. Upon
CC       elicitation, binds a 30bp promoter sequence known as elicitor element
CC       response (ERE) and is required for PR-10a expression.
CC       {ECO:0000269|PubMed:10948264, ECO:0000269|PubMed:12080340,
CC       ECO:0000269|PubMed:14960277}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12080340}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10948264}. Plastid,
CC       chloroplast {ECO:0000250|UniProtKB:Q9M9S3}. Note=Can localize to both
CC       chloroplast and nucleus. {ECO:0000250|UniProtKB:Q9M9S3}.
CC   -!- SIMILARITY: Belongs to the Whirly family. {ECO:0000305}.
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DR   EMBL; AF233342; AAF91282.1; -; mRNA.
DR   RefSeq; NP_001275155.1; NM_001288226.1.
DR   PDB; 1L3A; X-ray; 2.30 A; A/B/C/D=68-273.
DR   PDBsum; 1L3A; -.
DR   AlphaFoldDB; Q9LL85; -.
DR   SMR; Q9LL85; -.
DR   STRING; 4113.PGSC0003DMT400045439; -.
DR   EnsemblPlants; PGSC0003DMT400045439; PGSC0003DMT400045439; PGSC0003DMG400017627.
DR   EnsemblPlants; RHC05H1G0698.2.1; RHC05H1G0698.2.1; RHC05H1G0698.2.
DR   GeneID; 102577544; -.
DR   Gramene; PGSC0003DMT400045439; PGSC0003DMT400045439; PGSC0003DMG400017627.
DR   Gramene; RHC05H1G0698.2.1; RHC05H1G0698.2.1; RHC05H1G0698.2.
DR   KEGG; sot:102577544; -.
DR   eggNOG; ENOG502QRRY; Eukaryota.
DR   HOGENOM; CLU_062935_1_0_1; -.
DR   InParanoid; Q9LL85; -.
DR   OMA; KESCEFF; -.
DR   OrthoDB; 1637760at2759; -.
DR   EvolutionaryTrace; Q9LL85; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; TAS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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; Activator; Chloroplast; Direct protein sequencing;
KW   DNA-binding; Nucleus; Plant defense; Plastid; Reference proteome;
KW   Transcription; Transcription regulation; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..274
FT                   /note="Single-stranded DNA-binding protein WHY1,
FT                   chloroplastic"
FT                   /id="PRO_0000420450"
FT   REGION          100..105
FT                   /note="Required for ssDNA binding"
FT   REGION          253..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           178..191
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        253..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         100..105
FT                   /note="KGKAAL->QGQGGV: Loss of ssDNA binding."
FT                   /evidence="ECO:0000269|PubMed:12080340"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          101..110
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          129..137
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          170..174
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          198..209
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   HELIX           224..241
FT                   /evidence="ECO:0007829|PDB:1L3A"
FT   HELIX           244..248
FT                   /evidence="ECO:0007829|PDB:1L3A"
SQ   SEQUENCE   274 AA;  30327 MW;  A4DDF3CD4045A5A2 CRC64;
     MSNFSLSPSP TSGFSLNLQN PTKTSYLSFS SSINTIFAPL SSNTTKSFSG LTHKAALPRN
     LSLTCRHSDY FEPQQQQQQQ QQQPQGASTP KVFVGYSIYK GKAALTVEPR SPEFSPLDSG
     AFKLSREGMV MLQFAPAAGV RQYDWSRKQV FSLSVTEIGS IISLGAKDSC EFFHDPNKGR
     SDEGRVRKVL KVEPLPDGSG HFFNLSVQNK LINLDENIYI PVTKAEFAVL VSAFNFVMPY
     LLGWHTAVNS FKPEDASRSN NANPRSGAEL EWNR
 
 
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