ID   RAP23_ARATH             Reviewed;         248 AA.
AC   P42736; O04382; O23105;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Ethylene-responsive transcription factor RAP2-3;
DE   AltName: Full=Cadmium-induced protein AS30;
DE   AltName: Full=Ethylene response factor 72;
DE            Short=ERF72;
DE   AltName: Full=Ethylene-responsive element binding protein;
DE            Short=AtEBP;
DE   AltName: Full=Protein RELATED TO APETALA2 3;
DE            Short=Related to AP2 3;
GN   Name=RAP2-3; Synonyms=EBP, ERF072; OrderedLocusNames=At3g16770;
GN   ORFNames=MGL6.1, MGL6.24;
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], FUNCTION, INTERACTION WITH TGA4/OBF4, AND
RP   INDUCTION BY ETHYLENE.
RC   STRAIN=cv. Columbia; TISSUE=Callus;
RX   PubMed=9159183; DOI=10.1073/pnas.94.11.5961;
RA   Buettner M., Singh K.B.;
RT   "Arabidopsis thaliana ethylene-responsive element binding protein (AtEBP),
RT   an ethylene-inducible, GCC box DNA-binding protein interacts with an ocs
RT   element binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5961-5966(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Choi S., Baek E., Lee S.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9192694; DOI=10.1073/pnas.94.13.7076;
RA   Okamuro J.K., Caster B., Villarroel R., Van Montagu M., Jofuku K.D.;
RT   "The AP2 domain of APETALA2 defines a large new family of DNA binding
RT   proteins in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7076-7081(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ACBP2.
RX   PubMed=15159625; DOI=10.1023/b:plan.0000028790.75090.ab;
RA   Li H.-Y., Chye M.-L.;
RT   "Arabidopsis Acyl-CoA-binding protein ACBP2 interacts with an ethylene-
RT   responsive element-binding protein, AtEBP, via its ankyrin repeats.";
RL   Plant Mol. Biol. 54:233-243(2004).
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16407444; DOI=10.1104/pp.105.073783;
RA   Nakano T., Suzuki K., Fujimura T., Shinshi H.;
RT   "Genome-wide analysis of the ERF gene family in Arabidopsis and rice.";
RL   Plant Physiol. 140:411-432(2006).
RN   [10]
RP   SUBCELLULAR LOCATION, INDUCTION BY ETHYLENE; JASMONATE AND BOTRYTIS
RP   CINEREA, TISSUE SPECIFICITY, AND INTERACTION WITH ACBP4.
RX   PubMed=18836139; DOI=10.1093/jxb/ern241;
RA   Li H.-Y., Xiao S., Chye M.-L.;
RT   "Ethylene- and pathogen-inducible Arabidopsis acyl-CoA-binding protein 4
RT   interacts with an ethylene-responsive element binding protein.";
RL   J. Exp. Bot. 59:3997-4006(2008).
RN   [11]
RP   PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX   PubMed=22631074; DOI=10.1042/bj20111809;
RA   Soerensson C., Lenman M., Veide-Vilg J., Schopper S., Ljungdahl T.,
RA   Groetli M., Tamas M.J., Peck S.C., Andreasson E.;
RT   "Determination of primary sequence specificity of Arabidopsis MAPKs MPK3
RT   and MPK6 leads to identification of new substrates.";
RL   Biochem. J. 446:271-278(2012).
CC   -!- FUNCTION: Probably acts as a transcriptional activator. Binds to the
CC       GCC-box pathogenesis-related promoter element. May be involved in the
CC       regulation of gene expression by stress factors and by components of
CC       stress signal transduction pathways (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:9159183}.
CC   -!- SUBUNIT: Interacts with TGA4/OBF4, ACBP2, and ACBP4.
CC       {ECO:0000269|PubMed:15159625, ECO:0000269|PubMed:18836139,
CC       ECO:0000269|PubMed:9159183}.
CC   -!- INTERACTION:
CC       P42736; Q9STP8: ACBP2; NbExp=3; IntAct=EBI-368243, EBI-368234;
CC       P42736; Q9MA55: ACBP4; NbExp=4; IntAct=EBI-368243, EBI-2009699;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in stems and leaves, and, to a
CC       lower extent, in roots, siliques and flowers.
CC       {ECO:0000269|PubMed:18836139, ECO:0000269|PubMed:9192694}.
CC   -!- INDUCTION: By 1-aminocyclopropane-1-carboxylic acid (ACC, ethylene
CC       precursor), methyl jasmonate (MeJA), and Botrytis cinerea. Also induced
CC       by cadmium. {ECO:0000269|PubMed:18836139, ECO:0000269|PubMed:9159183}.
CC   -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA71073.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC       Sequence=CAA85734.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA85734.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to an insertion into the sequence.; Evidence={ECO:0000305};
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DR   EMBL; Y09942; CAA71073.1; ALT_SEQ; mRNA.
DR   EMBL; Z37504; CAA85734.1; ALT_SEQ; mRNA.
DR   EMBL; AF003096; AAC49769.1; -; mRNA.
DR   EMBL; AB022217; BAB02769.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75863.1; -; Genomic_DNA.
DR   EMBL; AY059917; AAL24399.1; -; mRNA.
DR   EMBL; AY035100; AAK59605.1; -; mRNA.
DR   EMBL; AY142562; AAN13131.1; -; mRNA.
DR   EMBL; AY087488; AAM65031.1; -; mRNA.
DR   RefSeq; NP_188299.1; NM_112550.5.
DR   AlphaFoldDB; P42736; -.
DR   SMR; P42736; -.
DR   BioGRID; 6263; 10.
DR   ELM; P42736; -.
DR   IntAct; P42736; 6.
DR   STRING; 3702.P42736; -.
DR   iPTMnet; P42736; -.
DR   PaxDb; 3702-AT3G16770-1; -.
DR   EnsemblPlants; AT3G16770.1; AT3G16770.1; AT3G16770.
DR   GeneID; 820929; -.
DR   Gramene; AT3G16770.1; AT3G16770.1; AT3G16770.
DR   KEGG; ath:AT3G16770; -.
DR   Araport; AT3G16770; -.
DR   TAIR; AT3G16770; EBP.
DR   eggNOG; ENOG502RZT8; Eukaryota.
DR   HOGENOM; CLU_054468_4_0_1; -.
DR   InParanoid; P42736; -.
DR   OMA; DMWMLDD; -.
DR   OrthoDB; 1216145at2759; -.
DR   PhylomeDB; P42736; -.
DR   PRO; PR:P42736; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P42736; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0008219; P:cell death; IMP:TAIR.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; TAS:TAIR.
DR   GO; GO:0010286; P:heat acclimation; IMP:TAIR.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:TAIR.
DR   GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR   CDD; cd00018; AP2; 1.
DR   Gene3D; 3.30.730.10; AP2/ERF domain; 1.
DR   InterPro; IPR001471; AP2/ERF_dom.
DR   InterPro; IPR036955; AP2/ERF_dom_sf.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR044808; ERF_plant.
DR   PANTHER; PTHR31190; DNA-BINDING DOMAIN; 1.
DR   PANTHER; PTHR31190:SF436; ETHYLENE-RESPONSIVE TRANSCRIPTION FACTOR RAP2-3; 1.
DR   Pfam; PF00847; AP2; 1.
DR   PRINTS; PR00367; ETHRSPELEMNT.
DR   SMART; SM00380; AP2; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   PROSITE; PS51032; AP2_ERF; 1.
DR   Genevisible; P42736; AT.
PE   1: Evidence at protein level;
KW   Cadmium; Cell membrane; Cytoplasm; DNA-binding; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..248
FT                   /note="Ethylene-responsive transcription factor RAP2-3"
FT                   /id="PRO_0000112523"
FT   DNA_BIND        78..135
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          60..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Phosphoserine; by MAPK6"
FT                   /evidence="ECO:0000269|PubMed:22631074"
FT   MUTAGEN         151
FT                   /note="S->A: Loss of phosphorylation by MAPK6."
FT                   /evidence="ECO:0000269|PubMed:22631074"
FT   CONFLICT        42
FT                   /note="F -> N (in Ref. 2; CAA85734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="A -> P (in Ref. 2; CAA85734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223..224
FT                   /note="EQ -> AR (in Ref. 1; CAA71073)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  27758 MW;  317D50CC514782F1 CRC64;
     MCGGAIISDY APLVTKAKGR KLTAEELWSE LDASAADDFW GFYSTSKLHP TNQVNVKEEA
     VKKEQATEPG KRRKRKNVYR GIRKRPWGKW AAEIRDPRKG VRVWLGTFNT AEEAAMAYDV
     AAKQIRGDKA KLNFPDLHHP PPPNYTPPPS SPRSTDQPPA KKVCVVSQSE SELSQPSFPV
     ECIGFGNGDE FQNLSYGFEP DYDLKQQISS LESFLELDGN TAEQPSQLDE SVSEVDMWML
     DDVIASYE
//