AI5L6_ARATH
ID AI5L6_ARATH Reviewed; 454 AA.
AC Q9M7Q3; O49503; O49504; Q9C5Q1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 6;
DE AltName: Full=Abscisic acid responsive elements-binding factor 3;
DE Short=ABRE-binding factor 3;
DE AltName: Full=Dc3 promoter-binding factor 5;
DE Short=AtDPBF5;
DE AltName: Full=bZIP transcription factor 37;
DE Short=AtbZIP37;
GN Name=ABF3; Synonyms=BZIP37, DPBF5; OrderedLocusNames=At4g34000/At4g34010;
GN ORFNames=F17I5.190/F17I5.200, F28A23.230;
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] (ISOFORM 1), 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] (ISOFORM 2).
RX PubMed=12376636; DOI=10.1104/pp.003566;
RA Kim S.Y., Ma J., Perret P., Li Z., Thomas T.L.;
RT "Arabidopsis ABI5 subfamily members have distinct DNA-binding and
RT transcriptional activities.";
RL Plant Physiol. 130:688-697(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP INTERACTION WITH ABI3.
RX PubMed=16247556; DOI=10.1007/s11103-005-8767-2;
RA Finkelstein R.R., Gampala S.S., Lynch T.J., Thomas T.L., Rock C.D.;
RT "Redundant and distinct functions of the ABA response loci ABA-
RT INSENSITIVE(ABI)5 and ABRE-BINDING FACTOR (ABF)3.";
RL Plant Mol. Biol. 59:253-267(2005).
RN [12]
RP INTERACTION WITH AFP1; AFP2; AFP3 AND AFP4.
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).
CC -!- FUNCTION: Binds to the ABA-responsive element (ABRE). Mediates stress-
CC responsive ABA signaling. {ECO:0000269|PubMed:11884679,
CC ECO:0000269|PubMed:15361142}.
CC -!- SUBUNIT: DNA-binding heterodimer (By similarity). Interacts with ABI3
CC and the AFP proteins AFP1, AFP2, AFP3 and AFP4. {ECO:0000250,
CC ECO:0000269|PubMed:16247556, ECO:0000269|PubMed:18484180}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M7Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M7Q3-2; Sequence=VSP_036886;
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:11884679}.
CC -!- INDUCTION: Up-regulated by drought, salt, abscisic acid (ABA).
CC {ECO:0000269|PubMed:10636868, ECO:0000269|PubMed:16284313}.
CC -!- DISRUPTION PHENOTYPE: Defective in ABA and stress responses.
CC {ECO:0000269|PubMed:15361142}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17571.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g34000 and At4g34010.; Evidence={ECO:0000305};
CC Sequence=CAA19882.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g34000 and At4g34010.; Evidence={ECO:0000305};
CC Sequence=CAA19883.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g34000 and At4g34010.; Evidence={ECO:0000305};
CC Sequence=CAB80117.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g34000 and At4g34010.; Evidence={ECO:0000305};
CC Sequence=CAB80118.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g34000 and At4g34010.; Evidence={ECO:0000305};
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DR EMBL; AF093546; AAF27181.1; -; mRNA.
DR EMBL; AF334210; AAK19603.1; -; mRNA.
DR EMBL; AL021961; CAA17571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031032; CAA19882.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031032; CAA19883.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80117.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80118.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86307.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86308.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86309.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67065.1; -; Genomic_DNA.
DR EMBL; AY054605; AAK96796.1; -; mRNA.
DR EMBL; AY081467; AAM10029.1; -; mRNA.
DR EMBL; AK175851; BAD43614.1; -; mRNA.
DR PIR; T05228; T05228.
DR PIR; T05229; T05229.
DR RefSeq; NP_001031785.2; NM_001036708.3. [Q9M7Q3-2]
DR RefSeq; NP_001320130.1; NM_001342246.1. [Q9M7Q3-1]
DR RefSeq; NP_567949.1; NM_119562.5. [Q9M7Q3-1]
DR RefSeq; NP_849490.2; NM_179159.4. [Q9M7Q3-1]
DR AlphaFoldDB; Q9M7Q3; -.
DR SMR; Q9M7Q3; -.
DR BioGRID; 14829; 24.
DR IntAct; Q9M7Q3; 9.
DR STRING; 3702.AT4G34000.1; -.
DR iPTMnet; Q9M7Q3; -.
DR PaxDb; Q9M7Q3; -.
DR PRIDE; Q9M7Q3; -.
DR ProteomicsDB; 244804; -. [Q9M7Q3-1]
DR EnsemblPlants; AT4G34000.1; AT4G34000.1; AT4G34000. [Q9M7Q3-1]
DR EnsemblPlants; AT4G34000.2; AT4G34000.2; AT4G34000. [Q9M7Q3-1]
DR EnsemblPlants; AT4G34000.3; AT4G34000.3; AT4G34000. [Q9M7Q3-2]
DR EnsemblPlants; AT4G34000.4; AT4G34000.4; AT4G34000. [Q9M7Q3-1]
DR GeneID; 829547; -.
DR Gramene; AT4G34000.1; AT4G34000.1; AT4G34000. [Q9M7Q3-1]
DR Gramene; AT4G34000.2; AT4G34000.2; AT4G34000. [Q9M7Q3-1]
DR Gramene; AT4G34000.3; AT4G34000.3; AT4G34000. [Q9M7Q3-2]
DR Gramene; AT4G34000.4; AT4G34000.4; AT4G34000. [Q9M7Q3-1]
DR KEGG; ath:AT4G34000; -.
DR Araport; AT4G34000; -.
DR TAIR; locus:2118969; AT4G34000.
DR eggNOG; ENOG502QPP6; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR InParanoid; Q9M7Q3; -.
DR OMA; RKQVEIM; -.
DR OrthoDB; 822545at2759; -.
DR PhylomeDB; Q9M7Q3; -.
DR PRO; PR:Q9M7Q3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M7Q3; baseline and differential.
DR Genevisible; Q9M7Q3; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; 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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..454
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 6"
FT /id="PRO_0000369611"
FT DOMAIN 372..435
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 374..393
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 400..414
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 420..454
FT /note="EIMEKQKNQLLEPLRQPWGMGCKRQCLRRTLTGPW -> CLASSLSQLRISR
FT FSYFLEVVFTDQMFHAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12376636"
FT /id="VSP_036886"
SQ SEQUENCE 454 AA; 49677 MW; B0428D39183374EF CRC64;
MGSRLNFKSF VDGVSEQQPT VGTSLPLTRQ NSVFSLTFDE FQNSWGGGIG KDFGSMNMDE
LLKNIWTAEE SHSMMGNNTS YTNISNGNSG NTVINGGGNN IGGLAVGVGG ESGGFFTGGS
LQRQGSLTLP RTISQKRVDD VWKELMKEDD IGNGVVNGGT SGIPQRQQTL GEMTLEEFLV
RAGVVREEPQ PVESVTNFNG GFYGFGSNGG LGTASNGFVA NQPQDLSGNG VAVRQDLLTA
QTQPLQMQQP QMVQQPQMVQ QPQQLIQTQE RPFPKQTTIA FSNTVDVVNR SQPATQCQEV
KPSILGIHNH PMNNNLLQAV DFKTGVTVAA VSPGSQMSPD LTPKSALDAS LSPVPYMFGR
VRKTGAVLEK VIERRQKRMI KNRESAARSR ARKQAYTMEL EAEIAQLKEL NEELQKKQVE
IMEKQKNQLL EPLRQPWGMG CKRQCLRRTL TGPW
