PUR_ARATH
ID PUR_ARATH Reviewed; 296 AA.
AC Q9SKZ1; Q8W590; Q9XHC4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transcription factor Pur-alpha 1;
DE AltName: Full=Purine-rich single-stranded DNA-binding protein alpha 1;
GN Name=PURA1; OrderedLocusNames=At2g32080; ORFNames=F22D22.17;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=10652127; DOI=10.1046/j.1365-313x.1999.00627.x;
RA Tremousaygue D., Manevski A., Bardet C., Lescure N., Lescure B.;
RT "Plant interstitial telomere motifs participate in the control of gene
RT expression in root meristems.";
RL Plant J. 20:553-561(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORMS 1 AND 2).
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 HOMODIMERIZATION, AND INTERACTION WITH TCP20.
RX PubMed=12631321; DOI=10.1046/j.1365-313x.2003.01682.x;
RA Tremousaygue D., Garnier L., Bardet C., Dabos P., Herve C., Lescure B.;
RT "Internal telomeric repeats and 'TCP domain' protein-binding sites co-
RT operate to regulate gene expression in Arabidopsis thaliana cycling
RT cells.";
RL Plant J. 33:957-966(2003).
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Transcription factor that specifically binds the purine-rich
CC double-stranded telomeric repeated sequence 5'-AAACCCTAA-3' found in
CC promoter telo boxes. {ECO:0000269|PubMed:10652127}.
CC -!- SUBUNIT: Homodimer. Interacts with TCP20.
CC {ECO:0000269|PubMed:12631321}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19245862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SKZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SKZ1-2; Sequence=VSP_033113;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AF136152; AAD39465.1; -; mRNA.
DR EMBL; AC006223; AAD15396.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08631.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08632.1; -; Genomic_DNA.
DR EMBL; AF419556; AAL31888.1; -; mRNA.
DR EMBL; AF446882; AAL38615.1; -; mRNA.
DR EMBL; AY052714; AAK96618.1; -; mRNA.
DR PIR; G84728; G84728.
DR RefSeq; NP_565736.1; NM_128768.3. [Q9SKZ1-1]
DR RefSeq; NP_850182.1; NM_179851.3. [Q9SKZ1-2]
DR AlphaFoldDB; Q9SKZ1; -.
DR SMR; Q9SKZ1; -.
DR BioGRID; 3115; 2.
DR STRING; 3702.AT2G32080.1; -.
DR iPTMnet; Q9SKZ1; -.
DR MetOSite; Q9SKZ1; -.
DR PaxDb; Q9SKZ1; -.
DR PRIDE; Q9SKZ1; -.
DR ProteomicsDB; 226019; -. [Q9SKZ1-1]
DR DNASU; 817768; -.
DR EnsemblPlants; AT2G32080.1; AT2G32080.1; AT2G32080. [Q9SKZ1-1]
DR EnsemblPlants; AT2G32080.2; AT2G32080.2; AT2G32080. [Q9SKZ1-2]
DR GeneID; 817768; -.
DR Gramene; AT2G32080.1; AT2G32080.1; AT2G32080. [Q9SKZ1-1]
DR Gramene; AT2G32080.2; AT2G32080.2; AT2G32080. [Q9SKZ1-2]
DR KEGG; ath:AT2G32080; -.
DR Araport; AT2G32080; -.
DR TAIR; locus:2045497; AT2G32080.
DR eggNOG; KOG3074; Eukaryota.
DR HOGENOM; CLU_057873_0_1_1; -.
DR InParanoid; Q9SKZ1; -.
DR OMA; WAKFGST; -.
DR PhylomeDB; Q9SKZ1; -.
DR PRO; PR:Q9SKZ1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKZ1; baseline and differential.
DR Genevisible; Q9SKZ1; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006628; PUR-bd_fam.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR Pfam; PF04845; PurA; 2.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..296
FT /note="Transcription factor Pur-alpha 1"
FT /id="PRO_0000330767"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_033113"
SQ SEQUENCE 296 AA; 32201 MW; D6B6E7F41622F97D CRC64;
MEANSGGGGG AEGGRAVTGG GGGGGGSDVE LVSKTLQVEH KLFYFDLKEN PRGRYLKISE
KTSATRSTII VPSSGISWFL DLFNYYVNSE EHELFSKELQ LDSKVFYFDI GENRRGRFLK
VSEASVSRNR STIIVPAGSS PDEGWAAFRN ILAEIHEASG LFVMPNQVKP SDGQEHLVDD
VGAGFIPGHG SQQPSSSEHN VDRTIDSPGQ EETGMTGVSK VIRADQKRFF FDLGNNNRGH
FLRISEVAGS DRSSIILPLS GLKQFHEVIG HFVEITKDKI EGMTGANVRT VDPPQR
