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BPC5_ARATH
ID   BPC5_ARATH              Reviewed;         283 AA.
AC   F4JUI3; E6Y2M5; E6Y2M6; F4JUI4; Q9SVK1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein BASIC PENTACYSTEINE5;
DE            Short=AtBPC5;
DE   AltName: Full=GAGA-motif binding transcriptional activator BBR/BPC5;
GN   Name=BPC5; Synonyms=BBR/BPC5; OrderedLocusNames=At4g38910;
GN   ORFNames=F19H22.10;
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] (ISOFORM 1).
RC   STRAIN=cv. Ak-1, and cv. Bay-0;
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 2), FUNCTION, DNA-BINDING, AND TISSUE
RP   SPECIFICITY.
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [6]
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).
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. {ECO:0000250}.
CC   -!- INTERACTION:
CC       F4JUI3; Q8L999-2: BPC6; NbExp=3; IntAct=EBI-15194873, EBI-15196639;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4JUI3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4JUI3-2; Sequence=VSP_041899;
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves and pistils.
CC       {ECO:0000269|PubMed:14731261}.
CC   -!- DOMAIN: Alanine-zipper domain is involved in homo- or hetero-
CC       dimerization via electrostatic interaction.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BBR/BPC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABU63289.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ABU63290.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB38811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80554.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EF633604; ABU63289.1; ALT_INIT; Genomic_DNA.
DR   EMBL; EF633605; ABU63290.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY380571; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL035679; CAB38811.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161594; CAB80554.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86991.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86992.1; -; Genomic_DNA.
DR   EMBL; BX827792; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T06051; T06051.
DR   RefSeq; NP_001190957.1; NM_001204028.2. [F4JUI3-1]
DR   RefSeq; NP_195602.5; NM_120051.6. [F4JUI3-2]
DR   AlphaFoldDB; F4JUI3; -.
DR   SMR; F4JUI3; -.
DR   BioGRID; 15326; 7.
DR   IntAct; F4JUI3; 7.
DR   STRING; 3702.AT4G38910.2; -.
DR   PaxDb; F4JUI3; -.
DR   PRIDE; F4JUI3; -.
DR   ProteomicsDB; 240807; -. [F4JUI3-1]
DR   EnsemblPlants; AT4G38910.1; AT4G38910.1; AT4G38910. [F4JUI3-2]
DR   EnsemblPlants; AT4G38910.2; AT4G38910.2; AT4G38910. [F4JUI3-1]
DR   GeneID; 830046; -.
DR   Gramene; AT4G38910.1; AT4G38910.1; AT4G38910. [F4JUI3-2]
DR   Gramene; AT4G38910.2; AT4G38910.2; AT4G38910. [F4JUI3-1]
DR   KEGG; ath:AT4G38910; -.
DR   Araport; AT4G38910; -.
DR   TAIR; locus:2120227; AT4G38910.
DR   eggNOG; ENOG502R48X; Eukaryota.
DR   InParanoid; F4JUI3; -.
DR   OMA; RCQGADD; -.
DR   OrthoDB; 1076395at2759; -.
DR   PRO; PR:F4JUI3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JUI3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009723; P:response to ethylene; IBA:GO_Central.
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..283
FT                   /note="Protein BASIC PENTACYSTEINE5"
FT                   /id="PRO_0000413439"
FT   REGION          51..86
FT                   /note="Alanine-zipper"
FT   REGION          122..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          63..89
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        122..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..25
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14731261,
FT                   ECO:0000303|PubMed:14993207"
FT                   /id="VSP_041899"
FT   VARIANT         114
FT                   /note="G -> D (in strain: cv. Ak-1)"
FT   VARIANT         188
FT                   /note="M -> T (in strain: cv. Ak-1; cv. Bay-0 and cv.
FT                   Landsberg erecta)"
FT   VARIANT         196
FT                   /note="T -> A (in strain: cv. Bay-0)"
FT   CONFLICT        29
FT                   /note="K -> E (in Ref. 5; BX827792)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="C -> F (in Ref. 5; BX827792)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  31776 MW;  8B877DB078BD3030 CRC64;
     MESGGQYENG RYKPDYYKGT QSVNVMPKKE QHNALVMNKK IISILAERDA AVKERNEAVA
     ATKEALASRD EALEQRDKAL SERDNAIMET ESALNALRYR ENNLNYILSC AKRGGSQRFI
     TEESHLPNPS PISTIPPEAA NTRPTKRKKE SKQGKKMGED LNRPVASPGK KSRKDWDSND
     VLVTFDEMTM PVPMCTCTGT ARQCYKWGNG GWQSSCCTTT LSEYPLPQMP NKRHSRVGGR
     KMSGSVFSRL LSRLAGEGHE LSSPVDLKNY WARHGTNRYI TIK
 
 
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