ID   BPC6_ARATH              Reviewed;         342 AA.
AC   Q8L999; A8MQZ4; Q9FIG5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Protein BASIC PENTACYSTEINE6;
DE            Short=AtBPC6;
DE   AltName: Full=GAGA-binding transcriptional activator BBR/BPC6;
GN   Name=BPC6; Synonyms=BBR/BPC6; OrderedLocusNames=At5g42520;
GN   ORFNames=MDH9.22;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=cv. Shokei;
RX   PubMed=12795701; DOI=10.1046/j.1365-313x.2003.01767.x;
RA   Santi L., Wang Y., Stile M.R., Berendzen K.W., Wanke D., Roig C., Pozzi C.,
RA   Mueller K., Mueller J., Rohde W., Salamini F.;
RT   "The GA octodinucleotide repeat binding factor BBR participates in the
RT   transcriptional regulation of the homeobox gene Bkn3.";
RL   Plant J. 34:813-826(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14731261; DOI=10.1046/j.1365-313x.2003.01971.x;
RA   Meister R.J., Williams L.A., Monfared M.M., Gallagher T.L., Kraft E.A.,
RA   Nelson C.G., Gasser C.S.;
RT   "Definition and interactions of a positive regulatory element of the
RT   Arabidopsis INNER NO OUTER promoter.";
RL   Plant J. 37:426-438(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [8]
RP   GENE FAMILY.
RA   Bloss U., Hohenstatt M.L., Hummel S., Harter K., Wanke D.;
RT   "The plant specific BPC/BBR family of GAGA-repeat binding proteins.";
RL   (In) Proceedings of the 20th international conference on Arabidopsis
RL   research, abstract#084, Edinburgh (2009).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=21435046; DOI=10.1111/j.1365-313x.2011.04562.x;
RA   Monfared M.M., Simon M.K., Meister R.J., Roig-Villanova I., Kooiker M.,
RA   Colombo L., Fletcher J.C., Gasser C.S.;
RT   "Overlapping and antagonistic activities of BASIC PENTACYSTEINE genes
RT   affect a range of developmental processes in Arabidopsis.";
RL   Plant J. 66:1020-1031(2011).
RN   [10]
RP   DOMAIN DIMERIZATION, AND SUBUNIT.
RX   PubMed=21347358; DOI=10.1371/journal.pone.0016070;
RA   Wanke D., Hohenstatt M.L., Dynowski M., Bloss U., Hecker A., Elgass K.,
RA   Hummel S., Hahn A., Caesar K., Schleifenbaum F., Harter K., Berendzen K.W.;
RT   "Alanine zipper-like coiled-coil domains are necessary for homotypic
RT   dimerization of plant GAGA-factors in the nucleus and nucleolus.";
RL   PLoS ONE 6:E16070-E16070(2011).
CC   -!- FUNCTION: Transcriptional regulator that specifically binds to GA-rich
CC       elements (GAGA-repeats) present in regulatory sequences of genes
CC       involved in developmental processes. {ECO:0000269|PubMed:14731261}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with BPC4.
CC       {ECO:0000269|PubMed:21347358}.
CC   -!- INTERACTION:
CC       Q8L999-2; F4JUI3: BPC5; NbExp=3; IntAct=EBI-15196639, EBI-15194873;
CC       Q8L999-2; O22800-2: COL14; NbExp=4; IntAct=EBI-15196639, EBI-15192033;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14731261}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:14731261}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8L999-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8L999-2; Sequence=VSP_041900;
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves and pistils.
CC       Detected in the base of flowers and tips of carpels, in sepal
CC       vasculature, in young rosette, in the lateral and tip of primary roots,
CC       and in ovule at the exception of the outer integument.
CC       {ECO:0000269|PubMed:14731261, ECO:0000269|PubMed:21435046}.
CC   -!- DOMAIN: Alanine-zipper domain is involved in homo- or hetero-
CC       dimerization via electrostatic interaction.
CC       {ECO:0000269|PubMed:21347358}.
CC   -!- SIMILARITY: Belongs to the BBR/BPC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10493.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EF123107; ABL67948.1; -; Genomic_DNA.
DR   EMBL; EF123108; ABL67949.1; -; mRNA.
DR   EMBL; AY380572; AAR25825.1; -; mRNA.
DR   EMBL; AB016888; BAB10493.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94820.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94821.1; -; Genomic_DNA.
DR   EMBL; BT024874; ABD85145.1; -; mRNA.
DR   EMBL; AK221752; BAD93808.1; -; mRNA.
DR   EMBL; AK227246; BAE99281.1; -; mRNA.
DR   EMBL; AY088564; AAM67342.1; -; mRNA.
DR   RefSeq; NP_001078690.1; NM_001085221.1. [Q8L999-2]
DR   RefSeq; NP_568605.1; NM_123617.3. [Q8L999-1]
DR   AlphaFoldDB; Q8L999; -.
DR   SMR; Q8L999; -.
DR   BioGRID; 19509; 19.
DR   IntAct; Q8L999; 15.
DR   STRING; 3702.AT5G42520.1; -.
DR   PaxDb; Q8L999; -.
DR   PRIDE; Q8L999; -.
DR   ProteomicsDB; 240550; -. [Q8L999-1]
DR   EnsemblPlants; AT5G42520.1; AT5G42520.1; AT5G42520. [Q8L999-1]
DR   EnsemblPlants; AT5G42520.2; AT5G42520.2; AT5G42520. [Q8L999-2]
DR   GeneID; 834259; -.
DR   Gramene; AT5G42520.1; AT5G42520.1; AT5G42520. [Q8L999-1]
DR   Gramene; AT5G42520.2; AT5G42520.2; AT5G42520. [Q8L999-2]
DR   KEGG; ath:AT5G42520; -.
DR   Araport; AT5G42520; -.
DR   TAIR; locus:2162291; AT5G42520.
DR   eggNOG; ENOG502QSGE; Eukaryota.
DR   InParanoid; Q8L999; -.
DR   OMA; FGKSHEW; -.
DR   PhylomeDB; Q8L999; -.
DR   PRO; PR:Q8L999; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L999; baseline and differential.
DR   Genevisible; Q8L999; AT.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IGI:TAIR.
DR   InterPro; IPR010409; GAGA-bd_tscrpt_act.
DR   PANTHER; PTHR31421; PTHR31421; 1.
DR   Pfam; PF06217; GAGA_bind; 1.
DR   SMART; SM01226; GAGA_bind; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..342
FT                   /note="Protein BASIC PENTACYSTEINE6"
FT                   /id="PRO_0000413440"
FT   REGION          41..76
FT                   /note="Alanine-zipper"
FT   REGION          143..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..195
FT                   /note="Required for nucleus and nucleolus localization"
FT   COILED          41..67
FT                   /evidence="ECO:0000255"
FT   MOTIF           192..195
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         19..22
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041900"
SQ   SEQUENCE   342 AA;  38239 MW;  01E93528CF6AA87D CRC64;
     MDDGGHRENG RHKAAVQGQW LMQHQPSMKQ VMSIIAERDA AIQERNLAIS EKKAAVAERD
     MAFLQRDTAI AERNNAIMER DSALTALQYR ENSMVTAPAA NMSACPPGCQ ISRGVKHLHH
     PHMHHHHQQH HIPQLTENAY ETREMEPNDG LPTSPPAGST LESAKPKRGK RVNPKATTQT
     AANKRGPKNQ RKVKKESEDD LNKIMFVKTT HDYTDEDSSK HILIGSKSDW KSQEMVGLNQ
     VVYDETTMPP PVCSCTGVLR QCYKWGNGGW QSSCCTTTLS MYPLPALPNK RHARVGGRKM
     SGSAFNKLLS RLAAEGHHDL SNPVDLKDHW AKHGTNRYIT IK