AI5L2_ARATH
ID AI5L2_ARATH Reviewed; 297 AA.
AC Q9LES3; Q9C5Q3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 2;
DE AltName: Full=ABA-responsive element-binding protein 3;
DE AltName: Full=Dc3 promoter-binding factor 3;
DE Short=AtDPBF3;
DE AltName: Full=bZIP transcription factor 66;
DE Short=AtbZIP66;
GN Name=DPBF3; Synonyms=AREB3, BZIP66; OrderedLocusNames=At3g56850;
GN ORFNames=T8M16_180;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND HETERODIMERIZATION.
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=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 [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 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 SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15642716; DOI=10.1093/jxb/eri050;
RA Bensmihen S., Giraudat J., Parcy F.;
RT "Characterization of three homologous basic leucine zipper transcription
RT factors (bZIP) of the ABI5 family during Arabidopsis thaliana embryo
RT maturation.";
RL J. Exp. Bot. 56:597-603(2005).
RN [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Binds to the embryo specification element and the ABA-
CC responsive element (ABRE) of the Dc3 gene promoter. Could participate
CC in abscisic acid-regulated gene expression during seed development.
CC -!- SUBUNIT: DNA-binding heterodimer with ABI5/DPBF1, DPBF2 or EEL/DPBF4.
CC Interacts with the AFP proteins AFP1, AFP2, AFP3 and AFP4.
CC {ECO:0000269|PubMed:18484180}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:15642716}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in seeds.
CC {ECO:0000269|PubMed:12376636}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo during the latest stages of
CC seed maturation. {ECO:0000269|PubMed:15642716}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
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DR EMBL; AB017162; BAB12406.1; -; mRNA.
DR EMBL; AF334208; AAK19601.1; -; mRNA.
DR EMBL; AL390921; CAC00748.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79574.1; -; Genomic_DNA.
DR EMBL; AY062448; AAL32526.1; -; mRNA.
DR EMBL; AY081670; AAM10232.1; -; mRNA.
DR PIR; T51273; T51273.
DR RefSeq; NP_191244.1; NM_115544.3.
DR AlphaFoldDB; Q9LES3; -.
DR SMR; Q9LES3; -.
DR BioGRID; 10168; 10.
DR IntAct; Q9LES3; 13.
DR STRING; 3702.AT3G56850.1; -.
DR iPTMnet; Q9LES3; -.
DR MetOSite; Q9LES3; -.
DR PaxDb; Q9LES3; -.
DR PRIDE; Q9LES3; -.
DR ProteomicsDB; 244758; -.
DR EnsemblPlants; AT3G56850.1; AT3G56850.1; AT3G56850.
DR GeneID; 824852; -.
DR Gramene; AT3G56850.1; AT3G56850.1; AT3G56850.
DR KEGG; ath:AT3G56850; -.
DR Araport; AT3G56850; -.
DR TAIR; locus:2103665; AT3G56850.
DR eggNOG; ENOG502QR11; Eukaryota.
DR HOGENOM; CLU_043238_0_1_1; -.
DR InParanoid; Q9LES3; -.
DR OMA; DPIYSDG; -.
DR OrthoDB; 1266458at2759; -.
DR PhylomeDB; Q9LES3; -.
DR PRO; PR:Q9LES3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LES3; baseline and differential.
DR Genevisible; Q9LES3; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
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; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..297
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 2"
FT /id="PRO_0000369607"
FT DOMAIN 225..288
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..246
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 253..267
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 272..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 209
FT /note="T -> I (in Ref. 2; AAK19601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 32419 MW; 1A60F9D6742E6310 CRC64;
MDSQRGIVEQ AKSQSLNRQS SLYSLTLDEV QNHLGSSGKA LGSMNLDELL KSVCSVEANQ
PSSMAVNGGA AAQEGLSRQG SLTLPRDLSK KTVDEVWKDI QQNKNGGSAH ERRDKQPTLG
EMTLEDLLLK AGVVTETIPG SNHDGPVGGG SAGSGAGLGQ NITQVGPWIQ YHQLPSMPQP
QAFMPYPVSD MQAMVSQSSL MGGLSDTQTP GRKRVASGEV VEKTVERRQK RMIKNRESAA
RSRARKQAYT HELEIKVSRL EEENERLRKQ KEVEKILPSV PPPDPKRQLR RTSSAPF
