BZP28_ARATH
ID BZP28_ARATH Reviewed; 675 AA.
AC Q9SG86; Q0WV49; Q8GUH4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=bZIP transcription factor 28 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP28 {ECO:0000303|PubMed:11906833};
GN Name=BZIP28 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g10800 {ECO:0000312|Araport:AT3G10800};
GN ORFNames=T7M13.12 {ECO:0000312|EMBL:AAF19569.1};
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=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 [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].
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 [LARGE SCALE MRNA].
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 [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, AND SUBCELLULAR LOCATION.
RX PubMed=18156219; DOI=10.1105/tpc.106.050021;
RA Liu J.X., Srivastava R., Che P., Howell S.H.;
RT "An endoplasmic reticulum stress response in Arabidopsis is mediated by
RT proteolytic processing and nuclear relocation of a membrane-associated
RT transcription factor, bZIP28.";
RL Plant Cell 19:4111-4119(2007).
RN [7]
RP CLEAVAGE BY SBT6.1.
RX PubMed=17662035; DOI=10.1111/j.1365-313x.2007.03195.x;
RA Liu J.X., Srivastava R., Che P., Howell S.H.;
RT "Salt stress responses in Arabidopsis utilize a signal transduction pathway
RT related to endoplasmic reticulum stress signaling.";
RL Plant J. 51:897-909(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18634751; DOI=10.1016/j.bbrc.2008.07.021;
RA Tajima H., Iwata Y., Iwano M., Takayama S., Koizumi N.;
RT "Identification of an Arabidopsis transmembrane bZIP transcription factor
RT involved in the endoplasmic reticulum stress response.";
RL Biochem. Biophys. Res. Commun. 374:242-247(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT SHOCK, AND TOPOLOGY.
RX PubMed=18849477; DOI=10.1073/pnas.0808463105;
RA Gao H., Brandizzi F., Benning C., Larkin R.M.;
RT "A membrane-tethered transcription factor defines a branch of the heat
RT stress response in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16398-16403(2008).
RN [10]
RP SUBUNIT.
RX PubMed=20207753; DOI=10.1105/tpc.109.072173;
RA Liu J.X., Howell S.H.;
RT "bZIP28 and NF-Y transcription factors are activated by ER stress and
RT assemble into a transcriptional complex to regulate stress response genes
RT in Arabidopsis.";
RL Plant Cell 22:782-796(2010).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20876872; DOI=10.1126/scisignal.2001140;
RA Che P., Bussell J.D., Zhou W., Estavillo G.M., Pogson B.J., Smith S.M.;
RT "Signaling from the endoplasmic reticulum activates brassinosteroid
RT signaling and promotes acclimation to stress in Arabidopsis.";
RL Sci. Signal. 3:RA69-RA69(2010).
RN [12]
RP INTERACTION WITH SAR1B AND STL2P, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 311-LYS-LYS-312; 320-LYS-LYS-321; 322-VAL--SER-324 AND GLY-329.
RX PubMed=22335396; DOI=10.1111/j.1365-313x.2012.04943.x;
RA Srivastava R., Chen Y., Deng Y., Brandizzi F., Howell S.H.;
RT "Elements proximal to and within the transmembrane domain mediate the
RT organelle-to-organelle movement of bZIP28 under ER stress conditions.";
RL Plant J. 70:1033-1042(2012).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=23558471; DOI=10.1093/mp/sst059;
RA Sun L., Lu S.J., Zhang S.S., Zhou S.F., Sun L., Liu J.X.;
RT "The lumen-facing domain is important for the biological function and
RT organelle-to-organelle movement of bZIP28 during ER stress in
RT Arabidopsis.";
RL Mol. Plant 6:1605-1615(2013).
RN [14]
RP INTERACTION WITH MED37A/BIP1 AND MED37B/BIP3, AND SUBCELLULAR LOCATION.
RX PubMed=23624714; DOI=10.1105/tpc.113.110684;
RA Srivastava R., Deng Y., Shah S., Rao A.G., Howell S.H.;
RT "BINDING PROTEIN is a master regulator of the endoplasmic reticulum stress
RT sensor/transducer bZIP28 in Arabidopsis.";
RL Plant Cell 25:1416-1429(2013).
CC -!- FUNCTION: Transcriptional activator involved in ER stress responses.
CC Functions as a stress sensor and transducer in ER stress signaling
CC pathway. After proteolysis by SBT6.1 (S1P) and S2P, the N-terminal bZIP
CC component is translocated to the nucleus, where it activates the
CC expression and production of ER chaperones (PubMed:18156219,
CC PubMed:18634751, PubMed:18849477, PubMed:20876872). Following ER
CC stress, activates proteins involved in brassinosteroid (BR) signaling,
CC which is required for stress acclimation and growth (PubMed:20876872).
CC {ECO:0000269|PubMed:18156219, ECO:0000269|PubMed:18634751,
CC ECO:0000269|PubMed:18849477, ECO:0000269|PubMed:20876872}.
CC -!- SUBUNIT: Homodimer. Hetereodimers with BZIP17, BZIP49 or BZIP60. Binds
CC the CCAAT box-binding heterotrimeric factor composed of NFYA4, NFYB3
CC and NFYC2 (PubMed:20207753). Interacts with SAR1B and STL2P
CC (PubMed:22335396). Interacts (via C-terminus) with MED37A/BIP1 and
CC MED37B/BIP3. MED37A/BIP1 and MED37B/BIP3 dissociates from BZIP28 under
CC ER stress (PubMed:23624714). {ECO:0000269|PubMed:20207753,
CC ECO:0000269|PubMed:22335396, ECO:0000269|PubMed:23624714}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:18156219, ECO:0000305|PubMed:18634751,
CC ECO:0000305|PubMed:18849477, ECO:0000305|PubMed:20876872,
CC ECO:0000305|PubMed:22335396, ECO:0000305|PubMed:23558471,
CC ECO:0000305|PubMed:23624714}; Single-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:20876872,
CC ECO:0000305|PubMed:22335396, ECO:0000305|PubMed:23558471,
CC ECO:0000305|PubMed:23624714}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:18156219,
CC ECO:0000269|PubMed:18849477, ECO:0000269|PubMed:20876872,
CC ECO:0000305|PubMed:18634751, ECO:0000305|PubMed:22335396,
CC ECO:0000305|PubMed:23558471, ECO:0000305|PubMed:23624714}.
CC Note=Translocates to the nucleus following heat shock or tunicamycin
CC treatment (ER stress) (PubMed:18156219, PubMed:18634751,
CC PubMed:18849477, PubMed:20876872, PubMed:22335396, PubMed:23558471,
CC PubMed:23624714). Relocation of BZIP28 from ER to the nucleus occurs
CC through the Golgi and is S2P-dependent (PubMed:20876872,
CC PubMed:22335396, PubMed:23558471, PubMed:23624714).
CC {ECO:0000269|PubMed:18156219, ECO:0000269|PubMed:18634751,
CC ECO:0000269|PubMed:18849477, ECO:0000269|PubMed:20876872,
CC ECO:0000269|PubMed:22335396, ECO:0000269|PubMed:23558471,
CC ECO:0000269|PubMed:23624714}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:18849477}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AC011708; AAF19569.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74956.1; -; Genomic_DNA.
DR EMBL; BT002502; AAO00862.1; -; mRNA.
DR EMBL; AK226928; BAE98999.1; -; mRNA.
DR RefSeq; NP_187691.1; NM_111917.5.
DR AlphaFoldDB; Q9SG86; -.
DR SMR; Q9SG86; -.
DR IntAct; Q9SG86; 1.
DR STRING; 3702.AT3G10800.1; -.
DR iPTMnet; Q9SG86; -.
DR PaxDb; Q9SG86; -.
DR PRIDE; Q9SG86; -.
DR ProteomicsDB; 240414; -.
DR EnsemblPlants; AT3G10800.1; AT3G10800.1; AT3G10800.
DR GeneID; 820249; -.
DR Gramene; AT3G10800.1; AT3G10800.1; AT3G10800.
DR KEGG; ath:AT3G10800; -.
DR Araport; AT3G10800; -.
DR TAIR; locus:2103192; AT3G10800.
DR eggNOG; ENOG502QQUV; Eukaryota.
DR HOGENOM; CLU_018118_1_0_1; -.
DR InParanoid; Q9SG86; -.
DR OMA; HGERDSC; -.
DR OrthoDB; 849173at2759; -.
DR PRO; PR:Q9SG86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG86; baseline and differential.
DR Genevisible; Q9SG86; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IGI:TAIR.
DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IMP:TAIR.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0006986; P:response to unfolded protein; IMP:TAIR.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Nucleus; Reference proteome; Stress response;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..675
FT /note="bZIP transcription factor 28"
FT /id="PRO_0000431972"
FT TOPO_DOM 1..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18849477"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..675
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:18849477"
FT DOMAIN 190..253
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..223
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 229..236
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 294..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 573..576
FT /note="RRIL cleavage motif"
FT /evidence="ECO:0000305|PubMed:17662035"
FT COMPBIAS 117..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 311..312
FT /note="KK->AA: Decreases binding to SAR1B. Loss of
FT processing by S2P."
FT /evidence="ECO:0000269|PubMed:22335396"
FT MUTAGEN 320..321
FT /note="KK->AA: Decreases binding to SAR1B. Loss of
FT processing by S2P."
FT /evidence="ECO:0000269|PubMed:22335396"
FT MUTAGEN 322..324
FT /note="VAS->AAF: No effect on processing by S2P and
FT translocation to the nucleus."
FT /evidence="ECO:0000269|PubMed:22335396"
FT MUTAGEN 329
FT /note="G->A: Loss of processing by S2P and translocation to
FT the nucleus."
FT /evidence="ECO:0000269|PubMed:22335396"
FT CONFLICT 308
FT /note="A -> V (in Ref. 3; AAO00862)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> I (in Ref. 4; BAE98999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 73432 MW; DAA74401C581C078 CRC64;
MTESTSVVAP PPEIPNLNPS MFSESDLFSI PPLDPLFLSD SDPISMDAPI SDLDFLLDDE
NGDFADFDFS FDNSDDFFDF DLSEPAVVIP EEIGNNRSNL DSSENRSGDG GLEGRSESVH
SQVSSQGSKT FVSDTVDASS SPESSNHQKS SVSKRKKENG DSSGELRSCK YQKSDDKSVA
TNNEGDDDDD KRKLIRQIRN RESAQLSRLR KKQQTEELER KVKSMNATIA ELNGKIAYVM
AENVALRQQM AVASGAPPMN PYMAAPPLPY QWMPYPPYPV RGYGSQTPLV PIPKLNPKPV
SSCRPKKAES KKNEGKSKLK KVASISFIGI LFFVFLFGTL VPFMNVNFGG ERGSFGGLSK
YDGHRYYDEH KGRVLMVGDG SDVRRNSGIS EGNIHSSRIS HGERDSCGGV DYNAHPKVEG
RPSSLSNASD PLFASLYVPR NDGLVKIDGN LIIHSVLASE KARGLGKKNI TETVKTKEPD
LTIPGALSSA LAVPGVRGNA AMLPHSTALS SEGKRLHQWF HEGGSGPLMD YSMCTEVFQF
DIAPGAIVPS SVSSISAEHL QNVTTHGKRM KNRRILEGLP VSLVASELNI TGTQPNKDAQ
NKTFNGNTNK PTSSSSMVVS VLLDPREVVD SETDRVVPPN PKSLSRIFVV VLLDSVKYVT
YSCVLPRSGL HLVAT
