AI5L4_ARATH
ID AI5L4_ARATH Reviewed; 392 AA.
AC Q9M7Q5; Q9FX98;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ABSCISIC ACID-INSENSITIVE 5-like protein 4;
DE AltName: Full=Abscisic acid responsive elements-binding factor 1;
DE Short=ABRE-binding factor 1;
DE AltName: Full=bZIP transcription factor 35;
DE Short=AtbZIP35;
GN Name=ABF1; Synonyms=BZIP35; OrderedLocusNames=At1g49720; ORFNames=F14J22.7;
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], DNA-BINDING, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10636868; DOI=10.1074/jbc.275.3.1723;
RA Choi H.-I., Hong J.-H., Ha J.-O., Kang J.-Y., Kim S.Y.;
RT "ABFs, a family of ABA-responsive element binding factors.";
RL J. Biol. Chem. 275:1723-1730(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH ABI3.
RX PubMed=16247556; DOI=10.1007/s11103-005-8767-2;
RA Finkelstein R.R., Gampala S.S., Lynch T.J., Thomas T.L., Rock C.D.;
RT "Redundant and distinct functions of the ABA response loci ABA-
RT INSENSITIVE(ABI)5 and ABRE-BINDING FACTOR (ABF)3.";
RL Plant Mol. Biol. 59:253-267(2005).
RN [8]
RP PHOSPHORYLATION BY SRK2D AND SRK2I.
RX PubMed=17307925; DOI=10.1105/tpc.106.048538;
RA Fujii H., Verslues P.E., Zhu J.-K.;
RT "Identification of two protein kinases required for abscisic acid
RT regulation of seed germination, root growth, and gene expression in
RT Arabidopsis.";
RL Plant Cell 19:485-494(2007).
RN [9]
RP PHOSPHORYLATION BY CPK4 AND CPK11.
RX PubMed=17921317; DOI=10.1105/tpc.107.050666;
RA Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y.,
RA Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.;
RT "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic
RT acid signal transduction in Arabidopsis.";
RL Plant Cell 19:3019-3036(2007).
RN [10]
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).
CC -!- FUNCTION: Binds to the ABA-responsive element (ABRE). Could participate
CC in abscisic acid-regulated gene expression.
CC -!- SUBUNIT: DNA-binding heterodimer (By similarity). Interacts with ABI3
CC and the AFP proteins AFP1, AFP2, AFP3 and AFP4. {ECO:0000250,
CC ECO:0000269|PubMed:16247556, ECO:0000269|PubMed:18484180}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M7Q5-1; Sequence=Displayed;
CC -!- INDUCTION: Up-regulated by abscisic acid (ABA) and cold.
CC {ECO:0000269|PubMed:10636868}.
CC -!- PTM: Phosphorylated by CPK4, CPK11, SRK2D and SRK2I in vitro.
CC {ECO:0000269|PubMed:17307925, ECO:0000269|PubMed:17921317}.
CC -!- SIMILARITY: Belongs to the bZIP family. ABI5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF093544; AAF27179.1; -; mRNA.
DR EMBL; AC011807; AAG13054.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32464.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60265.1; -; Genomic_DNA.
DR EMBL; BT008575; AAP40402.1; -; mRNA.
DR EMBL; BT008647; AAP40462.1; -; mRNA.
DR EMBL; AK226983; BAE99050.1; -; mRNA.
DR PIR; G96533; G96533.
DR RefSeq; NP_001322564.1; NM_001333400.1. [Q9M7Q5-1]
DR RefSeq; NP_564551.1; NM_103859.5. [Q9M7Q5-1]
DR AlphaFoldDB; Q9M7Q5; -.
DR SMR; Q9M7Q5; -.
DR BioGRID; 26620; 22.
DR IntAct; Q9M7Q5; 9.
DR STRING; 3702.AT1G49720.2; -.
DR iPTMnet; Q9M7Q5; -.
DR PaxDb; Q9M7Q5; -.
DR PRIDE; Q9M7Q5; -.
DR ProteomicsDB; 245031; -. [Q9M7Q5-1]
DR EnsemblPlants; AT1G49720.1; AT1G49720.1; AT1G49720. [Q9M7Q5-1]
DR EnsemblPlants; AT1G49720.3; AT1G49720.3; AT1G49720. [Q9M7Q5-1]
DR GeneID; 841395; -.
DR Gramene; AT1G49720.1; AT1G49720.1; AT1G49720. [Q9M7Q5-1]
DR Gramene; AT1G49720.3; AT1G49720.3; AT1G49720. [Q9M7Q5-1]
DR KEGG; ath:AT1G49720; -.
DR Araport; AT1G49720; -.
DR eggNOG; ENOG502QPP6; Eukaryota.
DR HOGENOM; CLU_043238_1_0_1; -.
DR InParanoid; Q9M7Q5; -.
DR OMA; QSKPLGR; -.
DR PhylomeDB; Q9M7Q5; -.
DR PRO; PR:Q9M7Q5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M7Q5; baseline and differential.
DR Genevisible; Q9M7Q5; 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; IEA:InterPro.
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; Alternative splicing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..392
FT /note="ABSCISIC ACID-INSENSITIVE 5-like protein 4"
FT /id="PRO_0000369609"
FT DOMAIN 311..374
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..332
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 339..360
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M7Q2"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 392 AA; 42728 MW; 15F23FD43D021017 CRC64;
MGTHIDINNL GGDTSRGNES KPLARQSSLY SLTFDELQST LGEPGKDFGS MNMDELLKNI
WTAEDTQAFM TTTSSVAAPG PSGFVPGGNG LQRQGSLTLP RTLSQKTVDE VWKYLNSKEG
SNGNTGTDAL ERQQTLGEMT LEDFLLRAGV VKEDNTQQNE NSSSGFYANN GAAGLEFGFG
QPNQNSISFN GNNSSMIMNQ APGLGLKVGG TMQQQQQPHQ QQLQQPHQRL PPTIFPKQAN
VTFAAPVNMV NRGLFETSAD GPANSNMGGA GGTVTATSPG TSSAENNTWS SPVPYVFGRG
RRSNTGLEKV VERRQKRMIK NRESAARSRA RKQAYTLELE AEIESLKLVN QDLQKKQAEI
MKTHNSELKE FSKQPPLLAK RQCLRRTLTG PW
