BZP34_ARATH
ID BZP34_ARATH Reviewed; 321 AA.
AC F4IN23; F4IN22; Q8S9M0; Q9SLC1;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Basic leucine zipper 34 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP34 {ECO:0000303|PubMed:11906833};
DE Short=bZIP protein 34;
GN Name=BZIP34 {ECO:0000303|PubMed:11906833}; OrderedLocusNames=At2g42380;
GN ORFNames=MHK10.10;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-321 (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-321 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RA Tiedemann J.;
RT "The family of bZIP transcription factors in Arabidopsis thaliana.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, INTERACTION WITH BZIP43 AND VIP1/BZIP51, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF PRO-230.
RX PubMed=17719007; DOI=10.1016/j.bbrc.2007.08.026;
RA Shen H., Cao K., Wang X.;
RT "A conserved proline residue in the leucine zipper region of AtbZIP34 and
RT AtbZIP61 in Arabidopsis thaliana interferes with the formation of
RT homodimer.";
RL Biochem. Biophys. Res. Commun. 362:425-430(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19449183; DOI=10.1007/s11103-009-9493-y;
RA Gibalova A., Renak D., Matczuk K., Dupl'akova N., Chab D., Twell D.,
RA Honys D.;
RT "AtbZIP34 is required for Arabidopsis pollen wall patterning and the
RT control of several metabolic pathways in developing pollen.";
RL Plant Mol. Biol. 70:581-601(2009).
RN [8]
RP SUBUNIT, AND INTERACTION WITH BZIP18.
RX PubMed=27896439; DOI=10.1007/s00497-016-0295-5;
RA Gibalova A., Steinbachova L., Hafidh S., Blahova V., Gadiou Z.,
RA Michailidis C., Muller K., Pleskot R., Duplakova N., Honys D.;
RT "Characterization of pollen-expressed bZIP protein interactions and the
RT role of ATbZIP18 in the male gametophyte.";
RL Plant Reprod. 30:1-17(2017).
CC -!- FUNCTION: Transcriptional activator involved in the sporophytic control
CC of cell wall patterning and gametophytic control of pollen development.
CC May play a role in the control of metabolic pathways regulating
CC cellular transport and lipid metabolism. {ECO:0000269|PubMed:17719007,
CC ECO:0000269|PubMed:19449183}.
CC -!- SUBUNIT: Forms heterodimers with BZIP18, BZIP43 and VIP1/BZIP51.
CC {ECO:0000269|PubMed:17719007, ECO:0000269|PubMed:27896439}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:17719007}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IN23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IN23-2; Sequence=VSP_056619;
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of leaves, stems and
CC siliques, anthers, filaments, tapetum, mature pollen grains, pistil
CC vascular tissues and papillar cells, and funiculi.
CC {ECO:0000269|PubMed:19449183}.
CC -!- DISRUPTION PHENOTYPE: Pollen morphological defects, reduced pollen
CC germination efficiency and pollen tube growth.
CC {ECO:0000269|PubMed:19449183}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23721.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL69473.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005956; AAD23721.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10113.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10114.1; -; Genomic_DNA.
DR EMBL; AY074657; AAL69473.1; ALT_INIT; mRNA.
DR EMBL; AF401299; AAK84222.1; -; mRNA.
DR PIR; C84853; C84853.
DR RefSeq; NP_565970.2; NM_129800.2. [F4IN23-2]
DR RefSeq; NP_850369.1; NM_180038.2. [F4IN23-1]
DR AlphaFoldDB; F4IN23; -.
DR SMR; F4IN23; -.
DR BioGRID; 4176; 4.
DR IntAct; F4IN23; 3.
DR STRING; 3702.AT2G42380.2; -.
DR PaxDb; F4IN23; -.
DR PRIDE; F4IN23; -.
DR ProteomicsDB; 240556; -. [F4IN23-1]
DR EnsemblPlants; AT2G42380.1; AT2G42380.1; AT2G42380. [F4IN23-2]
DR EnsemblPlants; AT2G42380.2; AT2G42380.2; AT2G42380. [F4IN23-1]
DR GeneID; 818839; -.
DR Gramene; AT2G42380.1; AT2G42380.1; AT2G42380. [F4IN23-2]
DR Gramene; AT2G42380.2; AT2G42380.2; AT2G42380. [F4IN23-1]
DR KEGG; ath:AT2G42380; -.
DR Araport; AT2G42380; -.
DR TAIR; locus:2053761; AT2G42380.
DR eggNOG; ENOG502QQW5; Eukaryota.
DR HOGENOM; CLU_059253_1_0_1; -.
DR InParanoid; F4IN23; -.
DR OMA; KMDNANH; -.
DR OrthoDB; 1069555at2759; -.
DR PRO; PR:F4IN23; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IN23; baseline and differential.
DR Genevisible; F4IN23; AT.
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; ISS:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR CDD; cd14703; bZIP_plant_RF2; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR044759; bZIP_RF2.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..321
FT /note="Basic leucine zipper 34"
FT /id="PRO_0000430352"
FT DOMAIN 186..238
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 97..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..207
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 214..235
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 97..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 216..227
FT /note="RSVTSLQAEVSV -> L (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_056619"
FT MUTAGEN 230
FT /note="P->A: Homodimerization and binding to G-box
FT element."
FT /evidence="ECO:0000269|PubMed:17719007"
SQ SEQUENCE 321 AA; 35806 MW; E6BFAB24CEA69A51 CRC64;
MAQLPPKIPN MTQHWPDFSS QKLSPFSTPT ATAVATATTT VQNPSWVDEF LDFSASRRGN
HRRSISDSIA FLEAPTVSIE DHQFDRFDDE QFMSMFTDDD NLHSNPSHIN NKNNNVGPTG
SSSNTSTPSN SFNDDNKELP PSDHNMNNNI NNNYNDEVQS QCKMEPEDGT ASNNNSGDSS
GNRILDPKRV KRILANRQSA QRSRVRKLQY ISELERSVTS LQAEVSVLSP RVAFLDHQRL
LLNVDNSALK QRIAALSQDK LFKDAHQEAL KREIERLRQV YNQQSLTNVE NANHLSATGA
GATPAVDIKS SVETEQLLNV S
