BZP49_ARATH
ID BZP49_ARATH Reviewed; 620 AA.
AC Q9LXX4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=bZIP transcription factor 49 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP49 {ECO:0000303|PubMed:11906833};
GN Name=BZIP49 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g56660 {ECO:0000312|Araport:AT3G56660};
GN ORFNames=T5P19.310 {ECO:0000312|EMBL:CAB88069.1};
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 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 [4]
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 [5]
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).
CC -!- FUNCTION: Transcriptional activator involved in stress responses.
CC {ECO:0000250|UniProtKB:O22208}.
CC -!- SUBUNIT: Interacts with BZIP28. {ECO:0000269|PubMed:20207753}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O22208}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:O22208}.
CC Note=Translocates to the nucleus following stress response.
CC {ECO:0000250|UniProtKB:O22208}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AL163972; CAB88069.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79549.1; -; Genomic_DNA.
DR PIR; T49067; T49067.
DR RefSeq; NP_191225.1; NM_115525.2.
DR AlphaFoldDB; Q9LXX4; -.
DR SMR; Q9LXX4; -.
DR STRING; 3702.AT3G56660.1; -.
DR PaxDb; Q9LXX4; -.
DR PRIDE; Q9LXX4; -.
DR EnsemblPlants; AT3G56660.1; AT3G56660.1; AT3G56660.
DR GeneID; 824833; -.
DR Gramene; AT3G56660.1; AT3G56660.1; AT3G56660.
DR KEGG; ath:AT3G56660; -.
DR Araport; AT3G56660; -.
DR TAIR; locus:2102564; AT3G56660.
DR eggNOG; ENOG502QQUV; Eukaryota.
DR HOGENOM; CLU_018118_2_0_1; -.
DR InParanoid; Q9LXX4; -.
DR OMA; KHLYSET; -.
DR OrthoDB; 849173at2759; -.
DR PhylomeDB; Q9LXX4; -.
DR PRO; PR:Q9LXX4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXX4; baseline and differential.
DR Genevisible; Q9LXX4; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IBA:GO_Central.
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; Membrane;
KW Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..620
FT /note="bZIP transcription factor 49"
FT /id="PRO_0000431973"
FT TOPO_DOM 1..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9SG86"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..620
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9SG86"
FT DOMAIN 172..235
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 109..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..205
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 211..218
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 526..529
FT /note="RRIL cleavage motif"
FT /evidence="ECO:0000305|PubMed:17662035"
FT COMPBIAS 109..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 620 AA; 68184 MW; E6ECE99EE41B8EC7 CRC64;
MAEPVLEDTY LTFSSDFDYI AIAPSPFDNF CNSNSDQVRN SISDLRFLID DDDSFDDLYF
PSENESFCIP PDATKREMSG DFTPASGISG DCVNEDTEKN TNGVLISTSS CYNRESPTDS
DFSGTSQSLS FSGQDSAKRK TEIEEDSSDE SRRLGKDGFA SVIKVGGEED DEKKKNVRLV
RNRESAHLSR QRKKHYVEEL EDKVKNMHST ISELSSKMSY FVAENVTLRQ QMGTRFSSGP
PMVPIVYPWM QYPAYMVKPQ GSQVALLPIP RLKPKHSVAK VKKFKKVASF SVFGFLFCMF
LFGALVNISY GEYKSNYVTD GVYDQSRGRV LVVDSSRVHC GGDSDQGVGR NVSETENLGP
PRNSSEPLVA SLFVPRNEKL VKIDGNLIIH SVLASEKARD SETKNEEGKS VLATTTKTLS
PALPLPDSTS PRTRDVSKHL YSETGKGLSS SGSDDASNDQ LKSTIANGKM QQWFREGVAG
PMFSSGMCTE VFQFDVSSNS GAIIPASPHT QQCKNTSDTQ KGKKNRRILS GGLPVSDFNL
TKEDHNSSSK DKFRETKPGP SMVVSVLVDP REGGNGDIDG MMGGTKPQSR VFIVVLVDGV
KYITYSCVLP RPDVPHLMTS
