AI5L5_ARATH
ID AI5L5_ARATH Reviewed; 416 AA.
AC Q9M7Q4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 5;
DE AltName: Full=ABA-responsive element-binding protein 1;
DE AltName: Full=Abscisic acid responsive elements-binding factor 2;
DE Short=ABRE-binding factor 2;
DE AltName: Full=bZIP transcription factor 36;
DE Short=AtbZIP36;
GN Name=ABF2; Synonyms=AREB1, BZIP36; OrderedLocusNames=At1g45249;
GN ORFNames=T2P3;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, 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 [8]
RP INTERACTION WITH ARIA, AND SUBCELLULAR LOCATION.
RX PubMed=15516505; DOI=10.1104/pp.104.049189;
RA Kim S., Choi H.I., Ryu H.J., Park J.H., Kim M.D., Kim S.Y.;
RT "ARIA, an Arabidopsis arm repeat protein interacting with a transcriptional
RT regulator of abscisic acid-responsive gene expression, is a novel abscisic
RT acid signaling component.";
RL Plant Physiol. 136:3639-3648(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
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 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 [11]
RP ACTIVATION BY PHOSPHORYLATION, AND MUTAGENESIS OF SER-26; SER-86; SER-94
RP AND THR-135.
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 [12]
RP PHOSPHORYLATION BY SRK2D AND SRK2I.
RX PubMed=17307925; DOI=10.1105/tpc.106.048538;
RA Fujii H., Verslues P.E., Zhu J.-K.;
RT "Identification of two protein kinases required for abscisic acid
RT regulation of seed germination, root growth, and gene expression in
RT Arabidopsis.";
RL Plant Cell 19:485-494(2007).
CC -!- FUNCTION: Involved in ABA and stress responses and acts as a positive
CC component of glucose signal transduction. Functions as transcriptional
CC activator in the ABA-inducible expression of rd29B. Binds specifically
CC to the ABA-responsive element (ABRE) of the rd29B gene promoter.
CC {ECO:0000269|PubMed:11005831, ECO:0000269|PubMed:15361142,
CC ECO:0000269|PubMed:16284313, ECO:0000269|PubMed:16463099}.
CC -!- SUBUNIT: DNA-binding heterodimer (By similarity). Interacts with ARIA.
CC {ECO:0000250, ECO:0000269|PubMed:15516505}.
CC -!- INTERACTION:
CC Q9M7Q4; Q940H6: SRK2E; NbExp=2; IntAct=EBI-1538369, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15516505, ECO:0000269|PubMed:16284313}.
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=Q9M7Q4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques
CC but not in seeds. {ECO:0000269|PubMed:11005831,
CC ECO:0000269|PubMed:15361142, ECO:0000269|PubMed:16284313}.
CC -!- INDUCTION: Up-regulated by drought, salt, abscisic acid (ABA), cold and
CC glucose. {ECO:0000269|PubMed:10636868, ECO:0000269|PubMed:11005831,
CC ECO:0000269|PubMed:15361142, ECO:0000269|PubMed:16284313,
CC ECO:0000269|PubMed:16463099}.
CC -!- PTM: The activation by phosphorylation is induced by abscisic acid
CC (ABA). Phosphorylated by SRK2C, SRK2D, SRK2E, SRK2F and SRK2I in vitro.
CC {ECO:0000269|PubMed:17307925}.
CC -!- DISRUPTION PHENOTYPE: Defective in glucose response and grows faster.
CC Exhibits abscisic acid (ABA) insensitivity.
CC {ECO:0000269|PubMed:15361142, ECO:0000269|PubMed:16284313}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
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DR EMBL; AF093545; AAF27180.1; -; mRNA.
DR EMBL; AB017160; BAB12404.1; -; mRNA.
DR EMBL; AC084820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE32110.1; -; Genomic_DNA.
DR EMBL; BT026443; ABH04550.1; -; mRNA.
DR RefSeq; NP_849777.1; NM_179446.5. [Q9M7Q4-1]
DR AlphaFoldDB; Q9M7Q4; -.
DR SMR; Q9M7Q4; -.
DR BioGRID; 26320; 26.
DR DIP; DIP-38544N; -.
DR IntAct; Q9M7Q4; 7.
DR STRING; 3702.AT1G45249.3; -.
DR iPTMnet; Q9M7Q4; -.
DR PaxDb; Q9M7Q4; -.
DR ProteomicsDB; 244776; -. [Q9M7Q4-1]
DR EnsemblPlants; AT1G45249.1; AT1G45249.1; AT1G45249. [Q9M7Q4-1]
DR GeneID; 841095; -.
DR Gramene; AT1G45249.1; AT1G45249.1; AT1G45249. [Q9M7Q4-1]
DR KEGG; ath:AT1G45249; -.
DR Araport; AT1G45249; -.
DR eggNOG; ENOG502QPP6; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR PhylomeDB; Q9M7Q4; -.
DR PRO; PR:Q9M7Q4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M7Q4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..416
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 5"
FT /id="PRO_0000369610"
FT DOMAIN 336..399
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..357
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 364..385
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 388..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MUTAGEN 26
FT /note="S->A: Abolishes ABA-dependent phosphorylation."
FT /evidence="ECO:0000269|PubMed:16446457"
FT MUTAGEN 86
FT /note="S->A: Abolishes ABA-dependent phosphorylation; when
FT associated with A-94."
FT /evidence="ECO:0000269|PubMed:16446457"
FT MUTAGEN 94
FT /note="S->A: Abolishes ABA-dependent phosphorylation; when
FT associated with A-86."
FT /evidence="ECO:0000269|PubMed:16446457"
FT MUTAGEN 135
FT /note="T->A: Abolishes ABA-dependent phosphorylation."
FT /evidence="ECO:0000269|PubMed:16446457"
SQ SEQUENCE 416 AA; 44165 MW; F5E77595B355EBF2 CRC64;
MDGSMNLGNE PPGDGGGGGG LTRQGSIYSL TFDEFQSSVG KDFGSMNMDE LLKNIWSAEE
TQAMASGVVP VLGGGQEGLQ LQRQGSLTLP RTLSQKTVDQ VWKDLSKVGS SGVGGSNLSQ
VAQAQSQSQS QRQQTLGEVT LEEFLVRAGV VREEAQVAAR AQIAENNKGG YFGNDANTGF
SVEFQQPSPR VVAAGVMGNL GAETANSLQV QGSSLPLNVN GARTTYQQSQ QQQPIMPKQP
GFGYGTQMGQ LNSPGIRGGG LVGLGDQSLT NNVGFVQGAS AAIPGALGVG AVSPVTPLSS
EGIGKSNGDS SSLSPSPYMF NGGVRGRKSG TVEKVVERRQ RRMIKNRESA ARSRARKQAY
TVELEAEVAK LKEENDELQR KQARIMEMQK NQETEMRNLL QGGPKKKLRR TESGPW
