EF115_ARATH
ID EF115_ARATH Reviewed; 263 AA.
AC Q9LY29; A0MFE2; C0SVN8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ethylene-responsive transcription factor ERF115;
GN Name=ERF115; OrderedLocusNames=At5g07310; ORFNames=T2I1.20;
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].
RA Pan Y., Gong W., Liu D., Fu Q., Mei W.-Q., Song W.-Q., Ma L.-G., Luo J.-C.,
RA Deng X.-W., Zhu Y.-X.;
RT "Molecular cloning, expression, phylogenetic and functional
RT characterization of the Arabidopsis AP2/EREBP transcription factor
RT family.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, MUTAGENESIS OF 115-ARG--LEU-118 AND 150-ARG--LEU-153, TISSUE
RP SPECIFICITY, INDUCTION BY ETHYLENE AND BRASSINOSTEROID, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=24158907; DOI=10.1126/science.1240667;
RA Heyman J., Cools T., Vandenbussche F., Heyndrickx K.S., Van Leene J.,
RA Vercauteren I., Vanderauwera S., Vandepoele K., De Jaeger G.,
RA Van Der Straeten D., De Veylder L.;
RT "ERF115 controls root quiescent center cell division and stem cell
RT replenishment.";
RL Science 342:860-863(2013).
CC -!- FUNCTION: Acts as a transcriptional activator of the phytosulfokine
CC PSK5 peptide hormone. Binds to the GCC-box pathogenesis-related
CC promoter element. Rate-limiting factor of quiescent center cell
CC division active when surrounding stem cells are damaged. Is a
CC proteolytic target of APC/C-FZR1 complex.
CC {ECO:0000269|PubMed:24158907}.
CC -!- INTERACTION:
CC Q9LY29; Q9LDL7: PAT1; NbExp=3; IntAct=EBI-2130977, EBI-25514815;
CC Q9LY29; Q9S7H5: SCL21; NbExp=3; IntAct=EBI-2130977, EBI-1238472;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Restricted to dividing quiescent center cells.
CC {ECO:0000269|PubMed:24158907}.
CC -!- INDUCTION: Up-regulated by brassinosteroid, but not regulated by
CC ethylene. {ECO:0000269|PubMed:24158907}.
CC -!- PTM: Cleaved by the APC/C-FZR1 complex.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28684.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY560885; AAT44952.1; -; mRNA.
DR EMBL; AL163912; CAB87920.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91135.1; -; Genomic_DNA.
DR EMBL; DQ653268; ABK28684.1; ALT_SEQ; mRNA.
DR EMBL; BT025717; ABF82620.1; -; mRNA.
DR EMBL; AB493741; BAH30579.1; -; mRNA.
DR PIR; T49870; T49870.
DR RefSeq; NP_196348.1; NM_120813.2.
DR AlphaFoldDB; Q9LY29; -.
DR SMR; Q9LY29; -.
DR BioGRID; 15901; 9.
DR IntAct; Q9LY29; 8.
DR STRING; 3702.AT5G07310.1; -.
DR PaxDb; Q9LY29; -.
DR PRIDE; Q9LY29; -.
DR EnsemblPlants; AT5G07310.1; AT5G07310.1; AT5G07310.
DR GeneID; 830622; -.
DR Gramene; AT5G07310.1; AT5G07310.1; AT5G07310.
DR KEGG; ath:AT5G07310; -.
DR Araport; AT5G07310; -.
DR TAIR; locus:2183304; AT5G07310.
DR eggNOG; ENOG502RZR5; Eukaryota.
DR HOGENOM; CLU_042594_0_2_1; -.
DR InParanoid; Q9LY29; -.
DR OMA; NYGKRPF; -.
DR OrthoDB; 1525125at2759; -.
DR PhylomeDB; Q9LY29; -.
DR PRO; PR:Q9LY29; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY29; baseline and differential.
DR Genevisible; Q9LY29; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1990110; P:callus formation; IGI:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR CDD; cd00018; AP2; 1.
DR Gene3D; 3.30.730.10; -; 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; PTHR31190; 1.
DR Pfam; PF00847; AP2; 1.
DR PRINTS; PR00367; ETHRSPELEMNT.
DR SMART; SM00380; AP2; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS51032; AP2_ERF; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Ethylene signaling pathway; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..263
FT /note="Ethylene-responsive transcription factor ERF115"
FT /id="PRO_0000290426"
FT DNA_BIND 91..148
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..118
FT /note="Destruction-box D1"
FT /evidence="ECO:0000255"
FT MOTIF 150..153
FT /note="Destruction-box D2"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 115..118
FT /note="RVWL->AVWA: Increased stability of the protein.
FT Further increase of the stability of the protein; when
FT associated with 150-AAQA-153."
FT /evidence="ECO:0000269|PubMed:24158907"
FT MUTAGEN 150..153
FT /note="RAQL->AAQA: No effect on the stability of the
FT protein. Increased stability of the protein; when
FT associated with 115-AVWA-118."
FT /evidence="ECO:0000269|PubMed:24158907"
SQ SEQUENCE 263 AA; 29406 MW; 240033D9087A233C CRC64;
MANSGNYGKR PFRGDESDEK KEADDDENIF PFFSARSQYD MRAMVSALTQ VIGNQSSSHD
NNQHQPVVYN QQDPNPPAPP TQDQGLLRKR HYRGVRQRPW GKWAAEIRDP QKAARVWLGT
FETAEAAALA YDNAALKFKG SKAKLNFPER AQLASNTSTT TGPPNYYSSN NQIYYSNPQT
NPQTIPYFNQ YYYNQYLHQG GNSNDALSYS LAGGETGGSM YNHQTLSTTN SSSSGGSSRQ
QDDEQDYARY LRFGDSSPPN SGF
