AI5L1_ARATH
ID AI5L1_ARATH Reviewed; 331 AA.
AC Q8RYD6; Q9C5Q4; Q9LXP1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 1;
DE AltName: Full=Dc3 promoter-binding factor 2;
DE Short=AtDPBF2;
DE AltName: Full=bZIP transcription factor 67;
DE Short=AtbZIP67;
GN Name=DPBF2; Synonyms=BZIP67; OrderedLocusNames=At3g44460;
GN ORFNames=F14L2.10;
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=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 [2]
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 [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 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).
CC -!- FUNCTION: Could participate in abscisic acid-regulated gene expression
CC during seed development. {ECO:0000250}.
CC -!- SUBUNIT: DNA-binding heterodimer with AREB3/DPBF3 or EEL/DPBF4.
CC Interacts with the AFP proteins AFP1, AFP2 and AFP3.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88528.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ419600; CAD11867.1; -; mRNA.
DR EMBL; AF334207; AAK19600.1; -; mRNA.
DR EMBL; AL353818; CAB88528.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77905.1; -; Genomic_DNA.
DR EMBL; BT002923; AAO22739.1; -; mRNA.
DR EMBL; BT004342; AAO42336.1; -; mRNA.
DR PIR; T48926; T48926.
DR RefSeq; NP_566870.1; NM_114314.5.
DR AlphaFoldDB; Q8RYD6; -.
DR SMR; Q8RYD6; -.
DR BioGRID; 8891; 12.
DR IntAct; Q8RYD6; 9.
DR STRING; 3702.AT3G44460.1; -.
DR PaxDb; Q8RYD6; -.
DR PRIDE; Q8RYD6; -.
DR ProteomicsDB; 244918; -.
DR EnsemblPlants; AT3G44460.1; AT3G44460.1; AT3G44460.
DR GeneID; 823571; -.
DR Gramene; AT3G44460.1; AT3G44460.1; AT3G44460.
DR KEGG; ath:AT3G44460; -.
DR Araport; AT3G44460; -.
DR TAIR; locus:2076018; AT3G44460.
DR eggNOG; ENOG502QV9T; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR InParanoid; Q8RYD6; -.
DR OMA; YNENRPF; -.
DR OrthoDB; 961244at2759; -.
DR PhylomeDB; Q8RYD6; -.
DR PRO; PR:Q8RYD6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RYD6; baseline and differential.
DR Genevisible; Q8RYD6; 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; IDA: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..331
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 1"
FT /id="PRO_0000369606"
FT DOMAIN 247..310
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 249..268
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 275..289
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 296..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 135
FT /note="A -> D (in Ref. 2; AAK19600)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="V -> M (in Ref. 2; AAK19600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37665 MW; 4113F8E24188E3F1 CRC64;
MSVFESETSN FHVYNNHEIQ TQPQMQTFLS EEEPVGRQNS ILSLTLDEIQ MKSGKSFGAM
NMDEFLANLW TTVEENDNEG GGAHNDGEKP AVLPRQGSLS LPVPLCKKTV DEVWLEIQNG
VQQHPPSSNS GQNSAENIRR QQTLGEITLE DFLVKAGVVQ EPLKTTMRMS SSDFGYNPEF
GVGLHCQNQN NYGDNRSVYS ENRPFYSVLG ESSSCMTGNG RSNQYLTGLD AFRIKKRIID
GPPEILMERR QRRMIKNRES AARSRARRQA YTVELELELN NLTEENTKLK EIVEENEKKR
RQEIISRSKQ VTKEKSGDKL RKIRRMASAG W
