AI5L3_ARATH
ID AI5L3_ARATH Reviewed; 262 AA.
AC Q9C5Q2; O80677; Q8GXQ0; Q8LGU9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 3;
DE AltName: Full=Dc3 promoter-binding factor 4;
DE Short=AtDPBF4;
DE AltName: Full=Protein ENHANCED EM LEVEL;
DE AltName: Full=bZIP transcription factor 12;
DE Short=AtbZIP12;
GN Name=DPBF4; Synonyms=BZIP12, EEL; OrderedLocusNames=At2g41070;
GN ORFNames=T3K9.16;
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], TISSUE SPECIFICITY, DNA-BINDING, AND
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-262, IDENTIFICATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12084834; DOI=10.1105/tpc.000869;
RA Bensmihen S., Rippa S., Lambert G., Jublot D., Pautot V., Granier F.,
RA Giraudat J., Parcy F.;
RT "The homologous ABI5 and EEL transcription factors function
RT antagonistically to fine-tune gene expression during late embryogenesis.";
RL Plant Cell 14:1391-1403(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 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 [10]
RP INTERACTION WITH 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 embryo specification element and the ABA-
CC responsive element (ABRE) of the Dc3 gene promoter and to the ABRE of
CC the Em1 gene promoter. Could participate in abscisic acid-regulated
CC gene expression during seed development.
CC -!- SUBUNIT: DNA-binding heterodimer with ABI5/DPBF1, DPBF2 or AREB3/DPBF3.
CC Interacts with the AFP proteins 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 -!- DISRUPTION PHENOTYPE: No visible changes in phenotype.
CC {ECO:0000269|PubMed:12084834}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
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DR EMBL; AF334209; AAK19602.1; -; mRNA.
DR EMBL; AC004261; AAD12004.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09922.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09923.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09924.1; -; Genomic_DNA.
DR EMBL; AK118113; BAC42739.1; -; mRNA.
DR EMBL; BT025175; ABE77413.1; -; mRNA.
DR EMBL; AY084668; AAM61230.1; -; mRNA.
DR EMBL; AJ420881; CAD12766.1; -; mRNA.
DR EMBL; BN000024; CAD29863.1; -; mRNA.
DR PIR; T02112; T02112.
DR RefSeq; NP_565948.1; NM_129672.2.
DR RefSeq; NP_850341.1; NM_180010.1.
DR RefSeq; NP_973655.1; NM_201926.2.
DR AlphaFoldDB; Q9C5Q2; -.
DR SMR; Q9C5Q2; -.
DR BioGRID; 4043; 7.
DR IntAct; Q9C5Q2; 8.
DR STRING; 3702.AT2G41070.3; -.
DR iPTMnet; Q9C5Q2; -.
DR PaxDb; Q9C5Q2; -.
DR PRIDE; Q9C5Q2; -.
DR EnsemblPlants; AT2G41070.1; AT2G41070.1; AT2G41070.
DR EnsemblPlants; AT2G41070.2; AT2G41070.2; AT2G41070.
DR EnsemblPlants; AT2G41070.3; AT2G41070.3; AT2G41070.
DR GeneID; 818706; -.
DR Gramene; AT2G41070.1; AT2G41070.1; AT2G41070.
DR Gramene; AT2G41070.2; AT2G41070.2; AT2G41070.
DR Gramene; AT2G41070.3; AT2G41070.3; AT2G41070.
DR KEGG; ath:AT2G41070; -.
DR Araport; AT2G41070; -.
DR TAIR; locus:2063275; AT2G41070.
DR eggNOG; ENOG502QR11; Eukaryota.
DR HOGENOM; CLU_043238_0_2_1; -.
DR InParanoid; Q9C5Q2; -.
DR OrthoDB; 1266458at2759; -.
DR PhylomeDB; Q9C5Q2; -.
DR PRO; PR:Q9C5Q2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5Q2; baseline and differential.
DR Genevisible; Q9C5Q2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP: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; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..262
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 3"
FT /id="PRO_0000369608"
FT DOMAIN 190..253
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 192..211
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 218..232
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 239..262
FT /note="Disordered"
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:0000250|UniProtKB:Q9LES3"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 121
FT /note="T -> S (in Ref. 4; BAC42739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 29618 MW; ED58DF6B22582B07 CRC64;
MGSIRGNIEE PISQSLTRQN SLYSLKLHEV QTHLGSSGKP LGSMNLDELL KTVLPPAEEG
LVRQGSLTLP RDLSKKTVDE VWRDIQQDKN GNGTSTTTTH KQPTLGEITL EDLLLRAGVV
TETVVPQENV VNIASNGQWV EYHHQPQQQQ GFMTYPVCEM QDMVMMGGLS DTPQAPGRKR
VAGEIVEKTV ERRQKRMIKN RESAARSRAR KQAYTHELEI KVSRLEEENE KLRRLKEVEK
ILPSEPPPDP KWKLRRTNSA SL
