ID BZP25_ARATH Reviewed; 403 AA.
AC Q9M1G6; F4JDZ5; F4JDZ6; Q712N9; Q940H0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Basic leucine zipper 25;
DE Short=AtbZIP25;
DE Short=bZIP protein 25;
DE AltName: Full=Basic leucine zipper OPAQUE 2 homolog 4;
DE Short=Basic leucine zipper O2 homolog 4;
GN Name=BZIP25; Synonyms=BZO2H4; OrderedLocusNames=At3g54620;
GN ORFNames=T14E10.190;
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), FUNCTION, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, INTERACTION WITH ABI3, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12657652; DOI=10.1074/jbc.m210538200;
RA Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I., Carbonero P.,
RA Vicente-Carbajosa J.;
RT "Synergistic activation of seed storage protein gene expression in
RT Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
RL J. Biol. Chem. 278:21003-21011(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 3).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
RA Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
RT "Evolutionary pattern of angiosperm bZIP factors homologous to the maize
RT Opaque2 regulatory protein.";
RL J. Mol. Evol. 56:105-116(2003).
RN [7]
RP INTERACTION WITH BZIP53.
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT by specific heterodimerisation of bZIP transcription factors.";
RL EMBO J. 25:3133-3143(2006).
RN [8]
RP SUBUNIT.
RX PubMed=16731568; DOI=10.1093/molbev/msl022;
RA Deppmann C.D., Alvania R.S., Taparowsky E.J.;
RT "Cross-species annotation of basic leucine zipper factor interactions:
RT Insight into the evolution of closed interaction networks.";
RL Mol. Biol. Evol. 23:1480-1492(2006).
RN [9]
RP INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP11; BZIP44 AND BZIP53.
RX PubMed=16709202; DOI=10.1111/j.1365-313x.2006.02731.x;
RA Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "Two-hybrid protein-protein interaction analysis in Arabidopsis
RT protoplasts: establishment of a heterodimerization map of group C and group
RT S bZIP transcription factors.";
RL Plant J. 46:890-900(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, AND INTERACTION WITH BZIP53 AND ABI3.
RX PubMed=19531597; DOI=10.1105/tpc.108.062968;
RA Alonso R., Onate-Sanchez L., Weltmeier F., Ehlert A., Diaz I., Dietrich K.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "A pivotal role of the basic leucine zipper transcription factor bZIP53 in
RT the regulation of Arabidopsis seed maturation gene expression based on
RT heterodimerization and protein complex formation.";
RL Plant Cell 21:1747-1761(2009).
RN [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
RA Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K., Wang X.,
RA Chaban C., Hanson J., Teige M., Harter K., Vicente-Carbajosa J.,
RA Smeekens S., Droege-Laser W.;
RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription factor
RT network: availability of heterodimerization partners controls gene
RT expression during stress response and development.";
RL Plant Mol. Biol. 69:107-119(2009).
RN [13]
RP FUNCTION, AND INTERACTION WITH BZIP53.
RX PubMed=19261733; DOI=10.1104/pp.109.136531;
RA Roschzttardtz H., Fuentes I., Vasquez M., Corvalan C., Leon G., Gomez I.,
RA Araya A., Holuigue L., Vicente-Carbajosa J., Jordana X.;
RT "A nuclear gene encoding the iron-sulfur subunit of mitochondrial complex
RT II is regulated by B3 domain transcription factors during seed development
RT in Arabidopsis.";
RL Plant Physiol. 150:84-95(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, 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 [15]
RP INTERACTION WITH BZIP1 AND BZIP63.
RX PubMed=20080816; DOI=10.1093/mp/ssp115;
RA Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
RT "The arabidopsis bZIP1 transcription factor is involved in sugar signaling,
RT protein networking, and DNA binding.";
RL Mol. Plant 3:361-373(2010).
CC -!- FUNCTION: Transcription factor that binds to the 5'-ACGT-3' box,
CC especially present in G-box-like motif (5'-CCACGTGGCC-3'), ABRE
CC elements, of seed storage protein (SSP) encoding gene promoters (e.g.
CC At2S and CRU3) and promotes their expression in seeds when in complex
CC with ABI3 and BZIP53. {ECO:0000269|PubMed:12657652,
CC ECO:0000269|PubMed:19261733, ECO:0000269|PubMed:19531597}.
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterodimer with BZIP1, BZIP1,
CC BZIP2, BZIP9, BZIP11, BZIP44, BZIP53 and BZIP63. Interacts with ABI3
CC and forms a complex made of ABI3, BZIP53 and BZIP25.
CC {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:16709202,
CC ECO:0000269|PubMed:16731568, ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:19261733, ECO:0000269|PubMed:19531597,
CC ECO:0000269|PubMed:20080816, ECO:0000305}.
CC -!- INTERACTION:
CC Q9M1G6; Q9FGX2: BZIP1; NbExp=6; IntAct=EBI-942696, EBI-942623;
CC Q9M1G6; O65683: BZIP11; NbExp=6; IntAct=EBI-942696, EBI-942769;
CC Q9M1G6; Q9SI15: BZIP2; NbExp=6; IntAct=EBI-942696, EBI-942735;
CC Q9M1G6; C0Z2L5: BZIP44; NbExp=6; IntAct=EBI-942696, EBI-942804;
CC Q9M1G6; Q9LZP8: BZIP53; NbExp=6; IntAct=EBI-942696, EBI-942845;
CC Q9M1G6; O81002: BZIP6; NbExp=3; IntAct=EBI-942696, EBI-3133475;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9M1G6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M1G6-2; Sequence=VSP_042645, VSP_042647;
CC Name=3;
CC IsoId=Q9M1G6-3; Sequence=VSP_042644, VSP_042646;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems, leaves,
CC stipulae, siliques, seeds, pollen, and flowers.
CC {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
CC -!- DEVELOPMENTAL STAGE: First observed in seeds at early stages of
CC development, mostly in embryo and, at lower extent, in the endosperm.
CC Accumulates and peaks at maturation. Fade out during late seed
CC development steps, restricted to the inner layer of the seed coat, and,
CC at very low levels, in the mature embryo and the remaining endosperm.
CC Also present in the lignified inner subepidermal layer of the valves.
CC {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE79258.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ010860; CAC79658.1; -; mRNA.
DR EMBL; AL138656; CAB77582.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79256.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79257.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79258.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY054645; AAK96836.1; -; mRNA.
DR EMBL; AY057509; AAL09750.1; -; mRNA.
DR EMBL; AY081494; AAM10056.1; -; mRNA.
DR PIR; T47621; T47621.
DR RefSeq; NP_001118838.1; NM_001125366.1. [Q9M1G6-2]
DR RefSeq; NP_001190091.1; NM_001203162.1.
DR RefSeq; NP_567003.2; NM_115319.4. [Q9M1G6-1]
DR AlphaFoldDB; Q9M1G6; -.
DR SMR; Q9M1G6; -.
DR BioGRID; 9943; 12.
DR IntAct; Q9M1G6; 13.
DR MINT; Q9M1G6; -.
DR STRING; 3702.Q9M1G6; -.
DR iPTMnet; Q9M1G6; -.
DR PaxDb; 3702-AT3G54620-1; -.
DR ProteomicsDB; 240444; -. [Q9M1G6-1]
DR EnsemblPlants; AT3G54620.1; AT3G54620.1; AT3G54620. [Q9M1G6-1]
DR EnsemblPlants; AT3G54620.2; AT3G54620.2; AT3G54620. [Q9M1G6-2]
DR GeneID; 824627; -.
DR Gramene; AT3G54620.1; AT3G54620.1; AT3G54620. [Q9M1G6-1]
DR Gramene; AT3G54620.2; AT3G54620.2; AT3G54620. [Q9M1G6-2]
DR KEGG; ath:AT3G54620; -.
DR Araport; AT3G54620; -.
DR TAIR; AT3G54620; BZIP25.
DR eggNOG; ENOG502QX6A; Eukaryota.
DR HOGENOM; CLU_037575_3_0_1; -.
DR InParanoid; Q9M1G6; -.
DR OMA; AQNMPDG; -.
DR OrthoDB; 393915at2759; -.
DR PhylomeDB; Q9M1G6; -.
DR PRO; PR:Q9M1G6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1G6; baseline and differential.
DR Genevisible; Q9M1G6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:2000693; P:positive regulation of seed maturation; IDA:UniProtKB.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46408:SF5; BASIC LEUCINE ZIPPER 25; 1.
DR PANTHER; PTHR46408; BASIC LEUCINE ZIPPER 63; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Seed storage protein; Storage protein; Transcription;
KW Transcription regulation.
FT CHAIN 1..403
FT /note="Basic leucine zipper 25"
FT /id="PRO_0000416561"
FT DOMAIN 229..292
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 13..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..250
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 264..271
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 332..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 233..240
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 28..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 261..262
FT /note="VG -> AN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042644"
FT VAR_SEQ 262..295
FT /note="GQLRAEHSTLINRLSDMNHKYDAAAVDNRILRAD -> RSFISCSYIYTFLE
FT SFLLFNSLQGFIGKVFTNCR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042645"
FT VAR_SEQ 263..403
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042646"
FT VAR_SEQ 296..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042647"
FT CONFLICT 244
FT /note="R -> K (in Ref. 1; CAC79658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44331 MW; 1AF17B764F03F5A1 CRC64;
MHIVFSVDDL TESFWPVPAP APSPGSSSTP SPTQNVADGM TRSQSEWAFH RLINELSGSD
SSPTTNTIER SPPPVQSLSR LEETVDETED VVEIQKPQNH RRLPVDDQGK NRNRAPSSDP
VDSSAPVVVD PNQYHAILKS KLELACAAVA RRVGTVKPED SSASASNQKQ AQGSIVAQTS
PGASSVRFSP TTSTQKKPDV PARQTSISSR DDSDDDDLDG DADNGDPTDV KRARRMLSNR
ESARRSRRRK QEQMNEFDTQ VGQLRAEHST LINRLSDMNH KYDAAAVDNR ILRADIETLR
TKVKMAEETV KRVTGVNPLH WSRPNMGIPF SNTPSASSSI PPNSNHILKP ANSSTNTSAG
LAQNQRVETA NFLPEQVNRE GMQNPFAPDS NLYETLPHWN HKH
//
