AI5L7_ARATH
ID AI5L7_ARATH Reviewed; 431 AA.
AC Q9M7Q2; Q9LT88;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 7;
DE AltName: Full=ABA-responsive element-binding protein 2 {ECO:0000303|PubMed:11005831};
DE AltName: Full=Abscisic acid responsive elements-binding factor 4 {ECO:0000303|PubMed:10636868, ECO:0000303|PubMed:11884679};
DE Short=ABRE-binding factor 4 {ECO:0000303|PubMed:10636868, ECO:0000303|PubMed:11884679};
DE AltName: Full=bZIP transcription factor 38 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP38 {ECO:0000303|PubMed:11906833};
GN Name=ABF4 {ECO:0000303|PubMed:10636868, ECO:0000303|PubMed:11884679};
GN Synonyms=AREB2 {ECO:0000303|PubMed:11005831},
GN BZIP38 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g19290 {ECO:0000312|Araport:AT3G19290};
GN ORFNames=MVI11.7 {ECO:0000312|EMBL:BAB02453.1};
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 [MRNA], DNA-BINDING, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10636868; DOI=10.1074/jbc.275.3.1723;
RA Choi H.-I., Hong J.-H., Ha J.-O., Kang J.-Y., Kim S.Y.;
RT "ABFs, a family of ABA-responsive element binding factors.";
RL J. Biol. Chem. 275:1723-1730(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11005831; DOI=10.1073/pnas.190309197;
RA Uno Y., Furihata T., Abe H., Yoshida R., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Arabidopsis basic leucine zipper transcription factors involved in an
RT abscisic acid-dependent signal transduction pathway under drought and high-
RT salinity conditions.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11632-11637(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11884679; DOI=10.1105/tpc.010362;
RA Kang J.-Y., Choi H.-I., Im M.-Y., Kim S.Y.;
RT "Arabidopsis basic leucine zipper proteins that mediate stress-responsive
RT abscisic acid signaling.";
RL Plant Cell 14:343-357(2002).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15361142; DOI=10.1111/j.1365-313x.2004.02192.x;
RA Kim S., Kang J.-Y., Cho D.-I., Park J.H., Kim S.Y.;
RT "ABF2, an ABRE-binding bZIP factor, is an essential component of glucose
RT signaling and its overexpression affects multiple stress tolerance.";
RL Plant J. 40:75-87(2004).
RN [9]
RP INDUCTION.
RX PubMed=16284313; DOI=10.1105/tpc.105.035659;
RA Fujita Y., Fujita M., Satoh R., Maruyama K., Parvez M.M., Seki M.,
RA Hiratsu K., Ohme-Takagi M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "AREB1 is a transcription activator of novel ABRE-dependent ABA signaling
RT that enhances drought stress tolerance in Arabidopsis.";
RL Plant Cell 17:3470-3488(2005).
RN [10]
RP INTERACTION WITH CPK32, AND PHOSPHORYLATION AT SER-110 BY CPK32.
RX PubMed=16299177; DOI=10.1104/pp.105.069757;
RA Choi H.-I., Park H.-J., Park J.H., Kim S., Im M.-Y., Seo H.-H., Kim Y.-W.,
RA Hwang I., Kim S.Y.;
RT "Arabidopsis calcium-dependent protein kinase AtCPK32 interacts with ABF4,
RT a transcriptional regulator of abscisic acid-responsive gene expression,
RT and modulates its activity.";
RL Plant Physiol. 139:1750-1761(2005).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=16463099; DOI=10.1007/s11103-005-2418-5;
RA Nakashima K., Fujita Y., Katsura K., Maruyama K., Narusaka Y., Seki M.,
RA Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Transcriptional regulation of ABI3- and ABA-responsive genes including
RT RD29B and RD29A in seeds, germinating embryos, and seedlings of
RT Arabidopsis.";
RL Plant Mol. Biol. 60:51-68(2006).
RN [12]
RP MUTAGENESIS OF SER-39.
RX PubMed=16446457; DOI=10.1073/pnas.0505667103;
RA Furihata T., Maruyama K., Fujita Y., Umezawa T., Yoshida R., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Abscisic acid-dependent multisite phosphorylation regulates the activity
RT of a transcription activator AREB1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1988-1993(2006).
RN [13]
RP PHOSPHORYLATION BY CPK4 AND CPK11.
RX PubMed=17921317; DOI=10.1105/tpc.107.050666;
RA Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y.,
RA Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.;
RT "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic
RT acid signal transduction in Arabidopsis.";
RL Plant Cell 19:3019-3036(2007).
RN [14]
RP INTERACTION WITH AFP1; AFP2 AND AFP3.
RX PubMed=18484180; DOI=10.1007/s11103-008-9344-2;
RA Garcia M.E., Lynch T.J., Peeters J., Snowden C., Finkelstein R.R.;
RT "A small plant-specific protein family of ABI five binding proteins (AFPs)
RT regulates stress response in germinating Arabidopsis seeds and seedlings.";
RL Plant Mol. Biol. 67:643-658(2008).
RN [15]
RP INTERACTION WITH FREE1.
RX PubMed=30962512; DOI=10.1038/s41477-019-0400-5;
RA Li H., Li Y., Zhao Q., Li T., Wei J., Li B., Shen W., Yang C., Zeng Y.,
RA Rodriguez P.L., Zhao Y., Jiang L., Wang X., Gao C.;
RT "The plant ESCRT component FREE1 shuttles to the nucleus to attenuate
RT abscisic acid signalling.";
RL Nat. Plants 5:512-524(2019).
RN [16]
RP FUNCTION.
RX PubMed=32540007; DOI=10.1016/j.plantsci.2020.110489;
RA Pan W., Zheng P., Zhang C., Wang W., Li Y., Fan T., Liu Y., Cao S.;
RT "The effect of ABRE BINDING FACTOR 4-mediated FYVE1 on salt stress
RT tolerance in Arabidopsis.";
RL Plant Sci. 296:110489-110489(2020).
CC -!- FUNCTION: Functions as transcriptional activator in the ABA-inducible
CC expression of LTI65/RD29B (AC Q04980). Binds specifically to the ABA-
CC responsive element (ABRE) of the LTI65/RD29B (AC Q04980) gene promoter
CC (PubMed:11005831, PubMed:11884679, PubMed:15361142, PubMed:16463099).
CC Binds to the promoter of FREE1 and activates its transcription
CC (PubMed:32540007). {ECO:0000269|PubMed:11005831,
CC ECO:0000269|PubMed:11884679, ECO:0000269|PubMed:15361142,
CC ECO:0000269|PubMed:16463099, ECO:0000269|PubMed:32540007}.
CC -!- SUBUNIT: DNA-binding heterodimer (By similarity). Interacts with CPK32
CC and the AFP proteins AFP1, AFP2 and AFP3. Interacts with FREE1 (via C-
CC terminus) (PubMed:30962512). {ECO:0000250, ECO:0000269|PubMed:16299177,
CC ECO:0000269|PubMed:18484180, ECO:0000269|PubMed:30962512}.
CC -!- INTERACTION:
CC Q9M7Q2; Q6NLQ6: CPK32; NbExp=4; IntAct=EBI-1237867, EBI-1538032;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M7Q2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and immatures
CC siliques. {ECO:0000269|PubMed:11005831, ECO:0000269|PubMed:11884679}.
CC -!- INDUCTION: Up-regulated by drought, salt, abscisic acid (ABA) and cold.
CC {ECO:0000269|PubMed:10636868, ECO:0000269|PubMed:11005831,
CC ECO:0000269|PubMed:16284313, ECO:0000269|PubMed:16463099}.
CC -!- PTM: Phosphorylated by CPK4 and CPK11 in vitro.
CC {ECO:0000269|PubMed:16299177, ECO:0000269|PubMed:17921317}.
CC -!- DISRUPTION PHENOTYPE: Defective in ABA and stress responses.
CC {ECO:0000269|PubMed:15361142}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02453.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF093547; AAF27182.1; -; mRNA.
DR EMBL; AB017161; BAB12405.1; -; mRNA.
DR EMBL; AB025624; BAB02453.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76218.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64097.1; -; Genomic_DNA.
DR EMBL; AY050897; AAK92834.1; -; mRNA.
DR EMBL; AY091298; AAM14237.1; -; mRNA.
DR RefSeq; NP_001326147.1; NM_001338391.1. [Q9M7Q2-1]
DR RefSeq; NP_566629.1; NM_112816.3. [Q9M7Q2-1]
DR AlphaFoldDB; Q9M7Q2; -.
DR SMR; Q9M7Q2; -.
DR BioGRID; 6796; 30.
DR IntAct; Q9M7Q2; 21.
DR STRING; 3702.AT3G19290.3; -.
DR iPTMnet; Q9M7Q2; -.
DR PaxDb; Q9M7Q2; -.
DR PRIDE; Q9M7Q2; -.
DR ProteomicsDB; 244932; -. [Q9M7Q2-1]
DR EnsemblPlants; AT3G19290.1; AT3G19290.1; AT3G19290. [Q9M7Q2-1]
DR EnsemblPlants; AT3G19290.5; AT3G19290.5; AT3G19290. [Q9M7Q2-1]
DR GeneID; 821463; -.
DR Gramene; AT3G19290.1; AT3G19290.1; AT3G19290. [Q9M7Q2-1]
DR Gramene; AT3G19290.5; AT3G19290.5; AT3G19290. [Q9M7Q2-1]
DR KEGG; ath:AT3G19290; -.
DR Araport; AT3G19290; -.
DR eggNOG; ENOG502QPP6; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR PhylomeDB; Q9M7Q2; -.
DR PRO; PR:Q9M7Q2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M7Q2; baseline and differential.
DR Genevisible; Q9M7Q2; AT.
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; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043452; BZIP46-like.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR22952; PTHR22952; 1.
DR Pfam; PF00170; bZIP_1; 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 Abscisic acid signaling pathway; Activator; Alternative splicing;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..431
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 7"
FT /id="PRO_0000369612"
FT DOMAIN 351..414
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 379..393
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COILED 372..411
FT /evidence="ECO:0000255"
FT MOTIF 340..347
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 319..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 110
FT /note="Phosphoserine; by CPK32"
FT /evidence="ECO:0000269|PubMed:16299177"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="S->A: Abolishes ABA-dependent phosphorylation."
FT /evidence="ECO:0000269|PubMed:16446457"
SQ SEQUENCE 431 AA; 46492 MW; 562FB52A1B493AF3 CRC64;
MGTHINFNNL GGGGHPGGEG SSNQMKPTGS VMPLARQSSV YSLTFDELQN TLGGPGKDFG
SMNMDELLKS IWTAEEAQAM AMTSAPAATA VAQPGAGIPP PGGNLQRQGS LTLPRTISQK
TVDEVWKCLI TKDGNMEGSS GGGGESNVPP GRQQTLGEMT LEEFLFRAGV VREDNCVQQM
GQVNGNNNNG FYGNSTAAGG LGFGFGQPNQ NSITFNGTND SMILNQPPGL GLKMGGTMQQ
QQQQQQLLQQ QQQQMQQLNQ PHPQQRLPQT IFPKQANVAF SAPVNITNKG FAGAANNSIN
NNNGLASYGG TGVTVAATSP GTSSAENNSL SPVPYVLNRG RRSNTGLEKV IERRQRRMIK
NRESAARSRA RKQAYTLELE AEIEKLKKTN QELQKKQAEM VEMQKNELKE TSKRPWGSKR
QCLRRTLTGP W
