AI5L8_ARATH
ID AI5L8_ARATH Reviewed; 370 AA.
AC Q9FMM7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 8;
DE AltName: Full=bZIP transcription factor 15;
DE Short=AtbZIP15;
GN Name=BZIP15; OrderedLocusNames=At5g42910; ORFNames=MBD2.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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).
CC -!- FUNCTION: Could participate in abscisic acid-regulated gene expression.
CC {ECO:0000250}.
CC -!- SUBUNIT: DNA-binding heterodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9FMM7; Q8VZI9: At3g11100; NbExp=3; IntAct=EBI-15201762, EBI-1998580;
CC Q9FMM7; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15201762, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ419599; CAD11866.1; -; mRNA.
DR EMBL; AB008264; BAB09193.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94886.1; -; Genomic_DNA.
DR RefSeq; NP_199105.1; NM_123656.2.
DR AlphaFoldDB; Q9FMM7; -.
DR SMR; Q9FMM7; -.
DR BioGRID; 19553; 15.
DR IntAct; Q9FMM7; 15.
DR STRING; 3702.AT5G42910.1; -.
DR PaxDb; Q9FMM7; -.
DR PRIDE; Q9FMM7; -.
DR EnsemblPlants; AT5G42910.1; AT5G42910.1; AT5G42910.
DR GeneID; 834303; -.
DR Gramene; AT5G42910.1; AT5G42910.1; AT5G42910.
DR KEGG; ath:AT5G42910; -.
DR Araport; AT5G42910; -.
DR TAIR; locus:2159986; AT5G42910.
DR eggNOG; ENOG502QPP6; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR InParanoid; Q9FMM7; -.
DR OMA; TNGGSIH; -.
DR OrthoDB; 954756at2759; -.
DR PhylomeDB; Q9FMM7; -.
DR PRO; PR:Q9FMM7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMM7; baseline and differential.
DR Genevisible; Q9FMM7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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..370
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 8"
FT /id="PRO_0000369613"
FT DOMAIN 293..356
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 56..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..314
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 328..342
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 41033 MW; 66B36FAA16AA508F CRC64;
MDSYWRLKNL VNDLPVSTSL SRQGSIYSWT VDQFQTSLGL DCGSMNMDEL VKHISSAEET
QEGSQRQGST TLPPTLSKQN VGEVWKSITE EKHTNNNGGV TNITHLQGQQ TLGEITLEEF
FIRAGARGGN TNGGSIHDSS SSISGNPHTS LGVQIQPKAM VSDFMNNMVP RSHDSYLHQN
VNGSMSTYQP QQSIMSMPNG YSYGKQIRFS NGSLGSGNQS LQDTKRSLVP SVATIPSEAI
TCSPVTPFPT LNGKQKINGE SSLLSPSPYI SNGSTSTRGG KINSEITAEK QFVDKKLRRK
IKNRESAARS RARKQAQTME VEVELENLKK DYEELLKQHV ELRKRQMEPG MISLHERPER
KLRRTKSDIK