RA212_ARATH
ID RA212_ARATH Reviewed; 358 AA.
AC Q9SSA8; O23113; Q8L9V3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Ethylene-responsive transcription factor RAP2-12;
DE AltName: Full=Protein RELATED TO APETALA2 12;
GN Name=RAP2-12; Synonyms=ERF074; OrderedLocusNames=At1g53910;
GN ORFNames=T18A20.14;
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=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 [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].
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].
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 42-358.
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, TISSUE SPECIFICITY, INDUCTION BY HYPOXIA, DOMAIN, SUBCELLULAR
RP LOCATION, INTERACTION WITH ACBP1 AND ACBP2, AND MUTAGENESIS OF CYS-2.
RX PubMed=22020282; DOI=10.1038/nature10536;
RA Licausi F., Kosmacz M., Weits D.A., Giuntoli B., Giorgi F.M.,
RA Voesenek L.A., Perata P., van Dongen J.T.;
RT "Oxygen sensing in plants is mediated by an N-end rule pathway for protein
RT destabilization.";
RL Nature 479:419-422(2011).
RN [8]
RP FUNCTION.
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).
RN [9]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-2.
RX PubMed=24599061; DOI=10.1038/ncomms4425;
RA Weits D.A., Giuntoli B., Kosmacz M., Parlanti S., Hubberten H.M.,
RA Riegler H., Hoefgen R., Perata P., van Dongen J.T., Licausi F.;
RT "Plant cysteine oxidases control the oxygen-dependent branch of the N-end-
RT rule pathway.";
RL Nat. Commun. 5:3425-3425(2014).
CC -!- FUNCTION: Transcription factor involved in the activation of hypoxic
CC gene expression and in ethylene response. Partially redundant with
CC RAP2-2. Acts as a downstream regulator in the ethylene signaling
CC pathway. {ECO:0000269|PubMed:22020282, ECO:0000269|PubMed:22530619}.
CC -!- ACTIVITY REGULATION: Ethylene-responsive transcription factor RAP2-12,
CC N-terminally processed: The N-terminal cysteine residue of can be
CC oxidized by PCO1 or PCO2, thus preparing the protein for N-end rule
CC pathway-mediated proteasomal degradation.
CC {ECO:0000269|PubMed:24599061}.
CC -!- SUBUNIT: Interacts with ACBP1 and ACBP2. {ECO:0000269|PubMed:22020282}.
CC -!- INTERACTION:
CC Q9SSA8; Q9SM23: ACBP1; NbExp=3; IntAct=EBI-4441057, EBI-2008643;
CC Q9SSA8; Q9STP8: ACBP2; NbExp=3; IntAct=EBI-4441057, EBI-368234;
CC Q9SSA8; A2RVU3: At2g16030; NbExp=3; IntAct=EBI-4441057, EBI-25519358;
CC Q9SSA8; Q683C9: AUR2; NbExp=3; IntAct=EBI-4441057, EBI-25517163;
CC Q9SSA8; O80902: CIPK22; NbExp=3; IntAct=EBI-4441057, EBI-4453230;
CC Q9SSA8; Q8RWY5: HRA1; NbExp=4; IntAct=EBI-4441057, EBI-16122303;
CC Q9SSA8; Q8VYN2: PVA42; NbExp=3; IntAct=EBI-4441057, EBI-9160824;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22020282}.
CC Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366,
CC ECO:0000269|PubMed:22020282}. Note=Localizes to the plasma membrane
CC under aerobic conditions, but accumulates in the nucleus upon hypoxia.
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=Q9SSA8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings, leaves, flowers,
CC siliques and germinating seeds. {ECO:0000269|PubMed:22020282}.
CC -!- INDUCTION: Up-regulated by hypoxia but not by ethylene.
CC {ECO:0000269|PubMed:22020282}.
CC -!- DOMAIN: The N-terminus (1-13) is important for the regulation of the
CC oxygen-dependent activation of the transcription factor activity, an
CC internal region (123-177) is required for the interactions with ACPB1
CC and ACPB2, while the C-terminus (343-358) is required for positive
CC regulation of gene transcription. {ECO:0000269|PubMed:22020282}.
CC -!- MISCELLANEOUS: The N-terminus qualifies RAP2-12 as candidate substrate
CC of the N-end rule pathway for protein destabilization. The oxygen-
CC dependent oxidation of Cys-2 prevents hypoxic gene expression via the
CC destabilization of RAP2-12 in air. When the oxygen concentration
CC decreases, Cys oxidation is prevented and an active RAP2.12 accumulates
CC in the nucleus.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC subfamily. {ECO:0000305}.
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DR EMBL; AC009324; AAF02863.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33022.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33023.1; -; Genomic_DNA.
DR EMBL; AY037260; AAK59861.1; -; mRNA.
DR EMBL; AY057545; AAL09785.1; -; mRNA.
DR EMBL; AY113051; AAM47359.1; -; mRNA.
DR EMBL; AY088204; AAM65746.1; -; mRNA.
DR EMBL; AF003105; AAC49778.1; -; mRNA.
DR PIR; D96579; D96579.
DR RefSeq; NP_001031185.1; NM_001036108.3. [Q9SSA8-1]
DR RefSeq; NP_175794.1; NM_104269.4. [Q9SSA8-1]
DR AlphaFoldDB; Q9SSA8; -.
DR SMR; Q9SSA8; -.
DR BioGRID; 27054; 12.
DR DIP; DIP-60469N; -.
DR ELM; Q9SSA8; -.
DR IntAct; Q9SSA8; 14.
DR STRING; 3702.AT1G53910.1; -.
DR PaxDb; Q9SSA8; -.
DR EnsemblPlants; AT1G53910.1; AT1G53910.1; AT1G53910. [Q9SSA8-1]
DR EnsemblPlants; AT1G53910.2; AT1G53910.2; AT1G53910. [Q9SSA8-1]
DR GeneID; 841829; -.
DR Gramene; AT1G53910.1; AT1G53910.1; AT1G53910. [Q9SSA8-1]
DR Gramene; AT1G53910.2; AT1G53910.2; AT1G53910. [Q9SSA8-1]
DR KEGG; ath:AT1G53910; -.
DR Araport; AT1G53910; -.
DR TAIR; locus:2197076; AT1G53910.
DR eggNOG; ENOG502QV26; Eukaryota.
DR InParanoid; Q9SSA8; -.
DR OMA; MHAEENS; -.
DR PhylomeDB; Q9SSA8; -.
DR PRO; PR:Q9SSA8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSA8; baseline and differential.
DR Genevisible; Q9SSA8; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0070483; P:detection of hypoxia; IEP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:2000280; P:regulation of root development; IMP: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; Cell membrane; DNA-binding;
KW Ethylene signaling pathway; Membrane; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..358
FT /note="Ethylene-responsive transcription factor RAP2-12"
FT /id="PRO_0000297941"
FT DNA_BIND 124..181
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT MUTAGEN 2
FT /note="C->A: Increased lifetime of the protein and
FT accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:22020282,
FT ECO:0000269|PubMed:24599061"
FT CONFLICT 112
FT /note="D -> E (in Ref. 4; AAM65746)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="M -> L (in Ref. 4; AAM65746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 39801 MW; CF8232CBE3C9FE35 CRC64;
MCGGAIISDF IPPPRSRRVT SEFIWPDLKK NLKGSKKSSK NRSNFFDFDA EFEADFQGFK
DDSSIDCDDD FDVGDVFADV KPFVFTSTPK PAVSAAAEGS VFGKKVTGLD GDAEKSANRK
RKNQYRGIRQ RPWGKWAAEI RDPREGARIW LGTFKTAEEA ARAYDAAARR IRGSKAKVNF
PEENMKANSQ KRSVKANLQK PVAKPNPNPS PALVQNSNIS FENMCFMEEK HQVSNNNNNQ
FGMTNSVDAG CNGYQYFSSD QGSNSFDCSE FGWSDQAPIT PDISSAVINN NNSALFFEEA
NPAKKLKSMD FETPYNNTEW DASLDFLNED AVTTQDNGAN PMDLWSIDEI HSMIGGVF
