RAP22_ARATH
ID RAP22_ARATH Reviewed; 379 AA.
AC Q9LUM4; A8MRL7; O23104; Q8LE76;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ethylene-responsive transcription factor RAP2-2;
DE Short=AtRAP2.2;
DE AltName: Full=Protein RELATED TO APETALA2 2;
GN Name=RAP2-2; Synonyms=ERF075; OrderedLocusNames=At3g14230;
GN ORFNames=MLN21.1;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-375 (ISOFORM 2), 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 [6]
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 [7]
RP FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, AND INTERACTION WITH SINAT2.
RX PubMed=17873090; DOI=10.1104/pp.107.104828;
RA Welsch R., Maass D., Voegel T., Dellapenna D., Beyer P.;
RT "Transcription factor RAP2.2 and its interacting partner SINAT2: stable
RT elements in the carotenogenesis of Arabidopsis leaves.";
RL Plant Physiol. 145:1073-1085(2007).
RN [8]
RP FUNCTION, INDUCTION BY DARKNESS AND ETHYLENE, AND TISSUE SPECIFICITY.
RX PubMed=20357136; DOI=10.1104/pp.110.155077;
RA Hinz M., Wilson I.W., Yang J., Buerstenbinder K., Llewellyn D.,
RA Dennis E.S., Sauter M., Dolferus R.;
RT "Arabidopsis RAP2.2: an ethylene response transcription factor that is
RT important for hypoxia survival.";
RL Plant Physiol. 153:757-772(2010).
RN [9]
RP INTERACTION WITH MED25.
RX PubMed=21343311; DOI=10.1093/mp/ssr002;
RA Ou B., Yin K.Q., Liu S.N., Yang Y., Gu T., Wing Hui J.M., Zhang L.,
RA Miao J., Kondou Y., Matsui M., Gu H.Y., Qu L.J.;
RT "A high-throughput screening system for Arabidopsis transcription factors
RT and its application to Med25-dependent transcriptional regulation.";
RL Mol. Plant 4:546-555(2011).
RN [10]
RP FUNCTION, AND INDUCTION BY ETHYLENE AND BOTRYTIS CINEREA.
RX PubMed=22530619; DOI=10.1111/j.1469-8137.2012.04160.x;
RA Zhao Y., Wei T., Yin K.Q., Chen Z., Gu H., Qu L.J., Qin G.;
RT "Arabidopsis RAP2.2 plays an important role in plant resistance to Botrytis
RT cinerea and ethylene responses.";
RL New Phytol. 195:450-460(2012).
CC -!- FUNCTION: Transcription factor involved in carotenoid biosynthesis
CC regulation. Binds to the 5'-ATCTA-3' element present in the promoter of
CC phytoene synthase (PSY) and phytoene desaturase (PDS). Involved in
CC ethylene response and resistance to necrotrophic pathogens. Acts as a
CC downstream regulator in the ethylene signaling pathway. Partially
CC redundant with RAP2-12. {ECO:0000269|PubMed:17873090,
CC ECO:0000269|PubMed:20357136, ECO:0000269|PubMed:22530619}.
CC -!- SUBUNIT: Interacts with MED25 and SINAT2. {ECO:0000269|PubMed:17873090,
CC ECO:0000269|PubMed:21343311}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LUM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LUM4-2; Sequence=VSP_027407;
CC Name=3;
CC IsoId=Q9LUM4-3; Sequence=VSP_053957;
CC -!- TISSUE SPECIFICITY: Constitutive in flowers, leaves, stems, and roots.
CC {ECO:0000269|PubMed:20357136, ECO:0000269|PubMed:9192694}.
CC -!- INDUCTION: Up-regulated by darkness, ethylene and Botrytis cinerea.
CC {ECO:0000269|PubMed:20357136, ECO:0000269|PubMed:22530619}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:17873090}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022220; BAB01029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75490.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75491.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75492.1; -; Genomic_DNA.
DR EMBL; AY054539; AAK96730.1; -; mRNA.
DR EMBL; BT000374; AAN15693.1; -; mRNA.
DR EMBL; AY085580; AAM62802.1; -; mRNA.
DR EMBL; AF003095; AAC49768.1; -; mRNA.
DR RefSeq; NP_566482.1; NM_112281.2. [Q9LUM4-1]
DR RefSeq; NP_850582.1; NM_180251.3. [Q9LUM4-2]
DR RefSeq; NP_850583.1; NM_180252.1. [Q9LUM4-3]
DR AlphaFoldDB; Q9LUM4; -.
DR SMR; Q9LUM4; -.
DR BioGRID; 5977; 16.
DR ELM; Q9LUM4; -.
DR IntAct; Q9LUM4; 3.
DR STRING; 3702.AT3G14230.1; -.
DR PaxDb; Q9LUM4; -.
DR PRIDE; Q9LUM4; -.
DR ProteomicsDB; 236863; -. [Q9LUM4-1]
DR EnsemblPlants; AT3G14230.1; AT3G14230.1; AT3G14230. [Q9LUM4-1]
DR EnsemblPlants; AT3G14230.2; AT3G14230.2; AT3G14230. [Q9LUM4-2]
DR EnsemblPlants; AT3G14230.3; AT3G14230.3; AT3G14230. [Q9LUM4-3]
DR GeneID; 820643; -.
DR Gramene; AT3G14230.1; AT3G14230.1; AT3G14230. [Q9LUM4-1]
DR Gramene; AT3G14230.2; AT3G14230.2; AT3G14230. [Q9LUM4-2]
DR Gramene; AT3G14230.3; AT3G14230.3; AT3G14230. [Q9LUM4-3]
DR KEGG; ath:AT3G14230; -.
DR Araport; AT3G14230; -.
DR TAIR; locus:2090975; AT3G14230.
DR eggNOG; ENOG502QV26; Eukaryota.
DR InParanoid; Q9LUM4; -.
DR OMA; IMYNTNA; -.
DR OrthoDB; 786288at2759; -.
DR PhylomeDB; Q9LUM4; -.
DR PRO; PR:Q9LUM4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUM4; baseline and differential.
DR Genevisible; Q9LUM4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IMP: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; Alternative splicing; DNA-binding; Ethylene signaling pathway;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..379
FT /note="Ethylene-responsive transcription factor RAP2-2"
FT /id="PRO_0000297933"
FT DNA_BIND 127..184
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 97..101
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053957"
FT VAR_SEQ 97..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:9192694"
FT /id="VSP_027407"
FT CONFLICT 345
FT /note="E -> K (in Ref. 4; AAM62802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42526 MW; 84874914D1974BEF CRC64;
MCGGAIISDF IPPPRSLRVT NEFIWPDLKN KVKASKKRSN KRSDFFDLDD DFEADFQGFK
DDSAFDCEDD DDVFVNVKPF VFTATTKPVA SAFVSTGIYL VGSAYAKKTV ESAEQAEKSS
KRKRKNQYRG IRQRPWGKWA AEIRDPRKGS REWLGTFDTA EEAARAYDAA ARRIRGTKAK
VNFPEEKNPS VVSQKRPSAK TNNLQKSVAK PNKSVTLVQQ PTHLSQQYCN NSFDNSFGDM
SFMEEKPQMY NNQFGLTNSF DAGGNNGYQY FSSDQGSNSF DCSEFGWSDH GPKTPEISSM
LVNNNEASFV EETNAAKKLK PNSDESDDLM AYLDNALWDT PLEVEAMLGA DAGAVTQEEE
NPVELWSLDE INFMLEGDF
