ABI3_ARATH
ID ABI3_ARATH Reviewed; 720 AA.
AC Q01593; A6N2M3; A6N2N0; A6N2P3; O23625; Q1EQV9; Q56ZT2; Q570G9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=B3 domain-containing transcription factor ABI3;
DE AltName: Full=Protein ABSCISIC ACID-INSENSITIVE 3;
GN Name=ABI3; OrderedLocusNames=At3g24650; ORFNames=MSD24.2;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Fruit;
RX PubMed=1359917; DOI=10.2307/3869411;
RA Giraudat J., Hauge B.M., Valon C., Smalle J., Parcy F., Goodman H.M.;
RT "Isolation of the Arabidopsis ABI3 gene by positional cloning.";
RL Plant Cell 4:1251-1261(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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;
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-719.
RC STRAIN=cv. Wassilewskija;
RX PubMed=16816409; DOI=10.1093/pcp/pcj078;
RA Tamura N., Yoshida T., Tanaka A., Sasaki R., Bando A., Toh S., Lepiniec L.,
RA Kawakami N.;
RT "Isolation and characterization of high temperature-resistant germination
RT mutants of Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:1081-1094(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-302, AND VARIANTS LEU-225; GLU-231
RP AND THR-248.
RC STRAIN=cv. An-1, cv. Br-0, cv. Ct-1, cv. Cvi-1, cv. Edi-0, cv. Ga-0,
RC cv. Kas-1, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0,
RC cv. Mt-0, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0,
RC cv. Wa-1, and cv. Wassilewskija;
RX PubMed=17435248; DOI=10.1534/genetics.107.071928;
RA Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
RT "The genetic architecture of shoot branching in Arabidopsis thaliana: a
RT comparative assessment of candidate gene associations vs. quantitative
RT trait locus mapping.";
RL Genetics 176:1223-1236(2007).
RN [7]
RP INTERACTION WITH APRR1; AIP2; AIP3 AND AIP4.
RX PubMed=10743655; DOI=10.1046/j.1365-313x.2000.00663.x;
RA Kurup S., Jones H.D., Holdsworth M.J.;
RT "Interactions of the developmental regulator ABI3 with proteins identified
RT from developing Arabidopsis seeds.";
RL Plant J. 21:143-155(2000).
RN [8]
RP INTERACTION WITH ABI5.
RX PubMed=11489176; DOI=10.1046/j.1365-313x.2001.01069.x;
RA Nakamura S., Lynch T.J., Finkelstein R.R.;
RT "Physical interactions between ABA response loci of Arabidopsis.";
RL Plant J. 26:627-635(2001).
RN [9]
RP INTERACTION WITH BZIP10 AND BZIP25, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=12657652; DOI=10.1074/jbc.m210538200;
RA Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I., Carbonero P.,
RA Vicente-Carbajosa J.;
RT "Synergistic activation of seed storage protein gene expression in
RT Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
RL J. Biol. Chem. 278:21003-21011(2003).
RN [10]
RP INTERACTION WITH AIP2, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=15998807; DOI=10.1101/gad.1318705;
RA Zhang X., Garreton V., Chua N.H.;
RT "The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by
RT promoting ABI3 degradation.";
RL Genes Dev. 19:1532-1543(2005).
RN [11]
RP INTERACTION WITH SPK1 AND SCAR3.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
RN [12]
RP GENE FAMILY.
RX PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA Swaminathan K., Peterson K., Jack T.;
RT "The plant B3 superfamily.";
RL Trends Plant Sci. 13:647-655(2008).
RN [13]
RP FUNCTION, AND INTERACTION WITH BZIP10; BZIP25 AND BZIP53.
RX PubMed=19531597; DOI=10.1105/tpc.108.062968;
RA Alonso R., Onate-Sanchez L., Weltmeier F., Ehlert A., Diaz I., Dietrich K.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "A pivotal role of the basic leucine zipper transcription factor bZIP53 in
RT the regulation of Arabidopsis seed maturation gene expression based on
RT heterodimerization and protein complex formation.";
RL Plant Cell 21:1747-1761(2009).
RN [14]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=20525852; DOI=10.1105/tpc.110.074674;
RA Sugliani M., Brambilla V., Clerkx E.J., Koornneef M., Soppe W.J.;
RT "The conserved splicing factor SUA controls alternative splicing of the
RT developmental regulator ABI3 in Arabidopsis.";
RL Plant Cell 22:1936-1946(2010).
RN [15]
RP INDUCTION BY EMF1 AND EMF2.
RX PubMed=19783648; DOI=10.1104/pp.109.143495;
RA Kim S.Y., Zhu T., Sung Z.R.;
RT "Epigenetic regulation of gene programs by EMF1 and EMF2 in Arabidopsis.";
RL Plant Physiol. 152:516-528(2010).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24043799; DOI=10.1073/pnas.1308114110;
RA Delmas F., Sankaranarayanan S., Deb S., Widdup E., Bournonville C.,
RA Bollier N., Northey J.G., McCourt P., Samuel M.A.;
RT "ABI3 controls embryo degreening through Mendel's I locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3888-E3894(2013).
CC -!- FUNCTION: Participates in abscisic acid-regulated gene expression
CC during seed development. Regulates the transcription of SGR1 and SGR2
CC that are involved in leaf and embryo degreening.
CC {ECO:0000269|PubMed:19531597, ECO:0000269|PubMed:24043799}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SPK1, SCAR3, ABI5, APRR1,
CC AIP2, AIP3 and AIP4. Binds to BZIP10 and BZIP25 and forms complexes
CC made of ABI3, BZIP53 and BZIP25 or BZIP10.
CC {ECO:0000269|PubMed:10743655, ECO:0000269|PubMed:11489176,
CC ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:15998807,
CC ECO:0000269|PubMed:17267444, ECO:0000269|PubMed:19531597}.
CC -!- INTERACTION:
CC Q01593; Q8RXD3: AIP2; NbExp=3; IntAct=EBI-1578892, EBI-2312425;
CC Q01593; Q9M4B5: AIP3; NbExp=2; IntAct=EBI-1578892, EBI-2130809;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly found in
CC the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced. Splicing is regulated by
CC SUA. {ECO:0000269|PubMed:20525852};
CC Name=1; Synonyms=ABI3-alpha;
CC IsoId=Q01593-1; Sequence=Displayed;
CC Name=2; Synonyms=ABI3-beta;
CC IsoId=Q01593-2; Sequence=VSP_058192, VSP_058193;
CC -!- TISSUE SPECIFICITY: Isoform 2 accumulates only at the end of seed
CC maturation. {ECO:0000269|PubMed:20525852}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryos, endosperm, and outer
CC teguments of the seed throughout seed development.
CC {ECO:0000269|PubMed:12657652}.
CC -!- INDUCTION: Repressed by silencing mediated by polycomb group (PcG)
CC protein complex containing EMF1 and EMF2.
CC {ECO:0000269|PubMed:19783648}.
CC -!- PTM: Ubiquitinated by AIP2. Ubiquitination probably leads to its
CC subsequent degradation, thus negatively regulating ABA signaling.
CC {ECO:0000269|PubMed:15998807}.
CC -!- MISCELLANEOUS: The truncated abi3-6 mutant lacking the DNA-binding
CC domain is unable to localize to the nucleus and is an embryo stay-green
CC mutant. {ECO:0000305|PubMed:24043799}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a cryptic intron removal.
CC {ECO:0000269|PubMed:20525852}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X68141; CAA48241.1; -; mRNA.
DR EMBL; AJ002473; CAA05484.1; -; Genomic_DNA.
DR EMBL; AP000740; BAB01214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76933.1; -; Genomic_DNA.
DR EMBL; AK220739; BAD93896.1; -; mRNA.
DR EMBL; AK220879; BAD94272.1; -; mRNA.
DR EMBL; AB253328; BAE96106.1; -; Genomic_DNA.
DR EMBL; EF597723; ABR21503.1; -; Genomic_DNA.
DR EMBL; EF597724; ABR21504.1; -; Genomic_DNA.
DR EMBL; EF597725; ABR21505.1; -; Genomic_DNA.
DR EMBL; EF597726; ABR21506.1; -; Genomic_DNA.
DR EMBL; EF597727; ABR21507.1; -; Genomic_DNA.
DR EMBL; EF597728; ABR21508.1; -; Genomic_DNA.
DR EMBL; EF597729; ABR21509.1; -; Genomic_DNA.
DR EMBL; EF597730; ABR21510.1; -; Genomic_DNA.
DR EMBL; EF597731; ABR21511.1; -; Genomic_DNA.
DR EMBL; EF597732; ABR21512.1; -; Genomic_DNA.
DR EMBL; EF597733; ABR21513.1; -; Genomic_DNA.
DR EMBL; EF597734; ABR21514.1; -; Genomic_DNA.
DR EMBL; EF597735; ABR21515.1; -; Genomic_DNA.
DR EMBL; EF597736; ABR21516.1; -; Genomic_DNA.
DR EMBL; EF597737; ABR21517.1; -; Genomic_DNA.
DR EMBL; EF597738; ABR21518.1; -; Genomic_DNA.
DR EMBL; EF597739; ABR21519.1; -; Genomic_DNA.
DR EMBL; EF597740; ABR21520.1; -; Genomic_DNA.
DR EMBL; EF597741; ABR21521.1; -; Genomic_DNA.
DR EMBL; EF597743; ABR21523.1; -; Genomic_DNA.
DR EMBL; EF597744; ABR21524.1; -; Genomic_DNA.
DR PIR; JQ1676; JQ1676.
DR RefSeq; NP_189108.1; NM_113376.4. [Q01593-1]
DR AlphaFoldDB; Q01593; -.
DR SMR; Q01593; -.
DR BioGRID; 7392; 18.
DR IntAct; Q01593; 8.
DR STRING; 3702.AT3G24650.1; -.
DR PaxDb; Q01593; -.
DR PRIDE; Q01593; -.
DR ProteomicsDB; 244535; -. [Q01593-1]
DR EnsemblPlants; AT3G24650.1; AT3G24650.1; AT3G24650. [Q01593-1]
DR GeneID; 822061; -.
DR Gramene; AT3G24650.1; AT3G24650.1; AT3G24650. [Q01593-1]
DR KEGG; ath:AT3G24650; -.
DR Araport; AT3G24650; -.
DR TAIR; locus:2093166; AT3G24650.
DR eggNOG; ENOG502QWRF; Eukaryota.
DR HOGENOM; CLU_023549_0_0_1; -.
DR InParanoid; Q01593; -.
DR OMA; GNMAWPQ; -.
DR OrthoDB; 317013at2759; -.
DR PhylomeDB; Q01593; -.
DR PRO; PR:Q01593; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q01593; baseline and differential.
DR Genevisible; Q01593; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEP:TAIR.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IDA:TAIR.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR Gene3D; 2.40.330.10; -; 1.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR044800; LEC2-like.
DR PANTHER; PTHR31140; PTHR31140; 1.
DR Pfam; PF02362; B3; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; SSF101936; 1.
DR PROSITE; PS50863; B3; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; Alternative splicing;
KW Cytoplasm; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..720
FT /note="B3 domain-containing transcription factor ABI3"
FT /id="PRO_0000111504"
FT DNA_BIND 572..674
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT REGION 122..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 415..429
FT /note="YNQFGDPTGFNGYNM -> TNERSEITPFVFLSN (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:20525852"
FT /id="VSP_058192"
FT VAR_SEQ 430..720
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:20525852"
FT /id="VSP_058193"
FT VARIANT 225
FT /note="M -> L (in strain: cv. An-1, cv. Br-0, cv. Ct-1, cv.
FT Cvi-1, cv. Edi-0, cv. Ga-0, cv. Kas-1, cv. Kin-0, cv.
FT Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0,
FT cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo, cv. Tsu-1, cv.
FT Van-0, cv. Wa-1 and cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:17435248"
FT VARIANT 231
FT /note="G -> E (in strain: cv. Kas-1 and cv. Sorbo)"
FT /evidence="ECO:0000269|PubMed:17435248"
FT VARIANT 248
FT /note="A -> T (in strain: cv. Cvi-1)"
FT /evidence="ECO:0000269|PubMed:17435248"
FT CONFLICT 100
FT /note="S -> P (in Ref. 4; BAD93896/BAD94272)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="D -> V (in Ref. 4; BAD94272)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="Missing (in Ref. 1; CAA05484)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="P -> L (in Ref. 5; BAE96106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 79500 MW; D6A0F740D733060F CRC64;
MKSLHVAANA GDLAEDCGIL GGDADDTVLM DGIDEVGREI WLDDHGGDNN HVHGHQDDDL
IVHHDPSIFY GDLPTLPDFP CMSSSSSSST SPAPVNAIVS SASSSSAASS STSSAASWAI
LRSDGEDPTP NQNQYASGNC DDSSGALQST ASMEIPLDSS QGFGCGEGGG DCIDMMETFG
YMDLLDSNEF FDTSAIFSQD DDTQNPNLMD QTLERQEDQV VVPMMENNSG GDMQMMNSSL
EQDDDLAAVF LEWLKNNKET VSAEDLRKVK IKKATIESAA RRLGGGKEAM KQLLKLILEW
VQTNHLQRRR TTTTTTNLSY QQSFQQDPFQ NPNPNNNNLI PPSDQTCFSP STWVPPPPQQ
QAFVSDPGFG YMPAPNYPPQ PEFLPLLESP PSWPPPPQSG PMPHQQFPMP PTSQYNQFGD
PTGFNGYNMN PYQYPYVPAG QMRDQRLLRL CSSATKEARK KRMARQRRFL SHHHRHNNNN
NNNNNNQQNQ TQIGETCAAV APQLNPVATT ATGGTWMYWP NVPAVPPQLP PVMETQLPTM
DRAGSASAMP RQQVVPDRRQ GWKPEKNLRF LLQKVLKQSD VGNLGRIVLP KKEAETHLPE
LEARDGISLA MEDIGTSRVW NMRYRFWPNN KSRMYLLENT GDFVKTNGLQ EGDFIVIYSD
VKCGKYLIRG VKVRQPSGQK PEAPPSSAAT KRQNKSQRNI NNNSPSANVV VASPTSQTVK
