BZP17_ARATH
ID BZP17_ARATH Reviewed; 721 AA.
AC O22208; Q8L7E7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=bZIP transcription factor 17 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP17 {ECO:0000303|PubMed:11906833};
GN Name=BZIP17 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At2g40950 {ECO:0000312|Araport:AT2G40950};
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].
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 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE BY SBT6.1, AND DISRUPTION
RP PHENOTYPE.
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 [6]
RP INTERACTION WITH BZIP28.
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 [7]
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).
CC -!- FUNCTION: Transcriptional activator involved in salt and osmotic stress
CC responses. Functions as a stress sensor and transducer in a signaling
CC pathway that resembles an ER stress response. Following salt stress,
CC BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the C-terminus and the N-
CC terminal bZIP component is translocated to the nucleus, where it
CC activates the expression of salt stress response genes
CC (PubMed:17662035). Functions as a stress sensor and transducer in ER
CC stress signaling pathway. ER stress induces proteolysis of BZIP17 by
CC SBT6.1 (S1P) and S2P, and the N-terminal bZIP component is translocated
CC to the nucleus, where it activates the expression and production of ER
CC chaperones, as well as protein involved in brassinosteroid (BR)
CC signaling, which is required for stress acclimation and growth
CC (PubMed:20876872). {ECO:0000269|PubMed:17662035,
CC ECO:0000269|PubMed:20876872}.
CC -!- SUBUNIT: Interacts with BZIP28. {ECO:0000269|PubMed:20207753}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20876872, ECO:0000305|PubMed:17662035}; Single-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:20876872}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:17662035,
CC ECO:0000269|PubMed:20876872}. Note=Translocates to the nucleus
CC following salt treatment, heat shock or tunicamycin treatment (ER
CC stress) (PubMed:17662035, PubMed:20876872). Relocation of BZIP17 from
CC ER to the nucleus occurs through the Golgi and is S2P-dependent
CC (PubMed:20876872). {ECO:0000269|PubMed:17662035,
CC ECO:0000269|PubMed:20876872}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased sensitivity to salt-
CC induced osmotic stress. {ECO:0000269|PubMed:17662035}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AC002409; AAB86455.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09905.1; -; Genomic_DNA.
DR EMBL; AY136295; AAM96961.1; -; mRNA.
DR EMBL; BT000408; AAN15727.1; -; mRNA.
DR PIR; T00759; T00759.
DR RefSeq; NP_565946.1; NM_129659.3.
DR AlphaFoldDB; O22208; -.
DR SMR; O22208; -.
DR STRING; 3702.AT2G40950.1; -.
DR iPTMnet; O22208; -.
DR PaxDb; O22208; -.
DR PRIDE; O22208; -.
DR ProteomicsDB; 240513; -.
DR EnsemblPlants; AT2G40950.1; AT2G40950.1; AT2G40950.
DR GeneID; 818694; -.
DR Gramene; AT2G40950.1; AT2G40950.1; AT2G40950.
DR KEGG; ath:AT2G40950; -.
DR Araport; AT2G40950; -.
DR TAIR; locus:2058510; AT2G40950.
DR eggNOG; ENOG502QQUV; Eukaryota.
DR HOGENOM; CLU_018118_1_0_1; -.
DR InParanoid; O22208; -.
DR OMA; FNHNFGM; -.
DR OrthoDB; 849173at2759; -.
DR PhylomeDB; O22208; -.
DR PRO; PR:O22208; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22208; baseline and differential.
DR Genevisible; O22208; AT.
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:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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..721
FT /note="bZIP transcription factor 17"
FT /id="PRO_0000431971"
FT TOPO_DOM 1..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9SG86"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..721
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9SG86"
FT DOMAIN 228..288
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..261
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 267..274
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 337..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..630
FT /note="RRIL cleavage motif"
FT /evidence="ECO:0000305|PubMed:17662035"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 487
FT /note="I -> V (in Ref. 3; AAM96961/AAN15727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 78438 MW; 486193285A74B21B CRC64;
MAEPITKEQP PPPAPDPNST YPPPSDFDSI SIPPLDDHFS DQTPIGELMS DLGFPDGEFE
LTFDGMDDLY FPAENESFLI PINTSNQEQF GDFTPESESS GISGDCIVPK DADKTITTSG
CINRESPRDS DDRCSGADHN LDLPTPLSSQ GSGNCGSDVS EATNESSPKS RNVAVDQKVK
VEEAATTTTS ITKRKKEIDE DLTDESRNSK YRRSGEDADA SAVTGEEDEK KRARLMRNRE
SAQLSRQRKK HYVEELEEKV RNMHSTITDL NGKISYFMAE NATLRQQLGG NGMCPPHLPP
PPMGMYPPMA PMPYPWMPCP PYMVKQQGSQ VPLIPIPRLK PQNTLGTSKA KKSESKKSEA
KTKKVASISF LGLLFCLFLF GALAPIVNVN YGGISGAFYG NYRSNYITDQ IYSQHRDRVL
DTSRSGAGTG VSNSNGMHRG RDSDRGARKN ISATESSVTP GNGSEPLVAS LFVPRNDKLV
KIDGNLIINS ILASEKAVAS RKASESKERK ADLMISKDYT PALPLPDVGR TEELAKHLYR
SKAEKQKALS SGSADTLKDQ VKTKAANGEM QQWFREGVAG PMFSSGMCTE VFQFDVSSTS
GAIIPAATNV SAEHGKNTTD THKQQNRRIL RGLPIPLPGS DFNLTKEHQR NSSSKEIKPA
SSMVVSVLVD PREGGDGDID GMIGGPKSLS RVFVVVLLDS AKYVTYSCVL PRSGAPHLVT
T
