RAV2_ARATH
ID RAV2_ARATH Reviewed; 352 AA.
AC P82280; O23110; Q8LDM7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=AP2/ERF and B3 domain-containing transcription repressor RAV2;
DE AltName: Full=Ethylene-responsive transcription factor RAV2;
DE AltName: Full=Protein RELATED TO ABI3/VP1 2;
DE AltName: Full=Protein RELATED TO APETALA2 8;
DE AltName: Full=Protein TEMPRANILLO 2;
GN Name=RAV2; Synonyms=RAP2-8, TEM2; OrderedLocusNames=At1g68840;
GN ORFNames=F14K14.5, T6L1.3;
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].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9862967; DOI=10.1093/nar/27.2.470;
RA Kagaya Y., Ohmiya K., Hattori T.;
RT "RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence
RT through two distinct DNA-binding domains uniquely found in higher plants.";
RL Nucleic Acids Res. 27:470-478(1999).
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-352.
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 [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.
RX PubMed=18718758; DOI=10.1016/j.cub.2008.07.075;
RA Castillejo C., Pelaz S.;
RT "The balance between CONSTANS and TEMPRANILLO activities determines FT
RT expression to trigger flowering.";
RL Curr. Biol. 18:1338-1343(2008).
RN [9]
RP GENE FAMILY.
RX PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA Swaminathan K., Peterson K., Jack T.;
RT "The plant B3 superfamily.";
RL Trends Plant Sci. 13:647-655(2008).
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). Transcriptional
CC repressor of flowering time on long day plants. Acts directly on FT
CC expression by binding 5'-CAACA-3' and 5'-CACCTG-3 sequences (Probable).
CC Functionally redundant with TEM1. {ECO:0000250,
CC ECO:0000269|PubMed:18718758, ECO:0000305}.
CC -!- INTERACTION:
CC P82280; Q9SQI2: GI; NbExp=2; IntAct=EBI-15206702, EBI-446380;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. RAV
CC subfamily. {ECO:0000305}.
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DR EMBL; AB013887; BAA34251.1; -; mRNA.
DR EMBL; AC011665; AAG51586.1; -; Genomic_DNA.
DR EMBL; AC011914; AAG52035.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34847.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34848.1; -; Genomic_DNA.
DR EMBL; AF360312; AAK26022.1; -; mRNA.
DR EMBL; AY056361; AAL07247.1; -; mRNA.
DR EMBL; AY085908; AAM63120.1; -; mRNA.
DR EMBL; AF003101; AAC49774.1; -; mRNA.
DR PIR; T51330; T51330.
DR RefSeq; NP_001185352.1; NM_001198423.1.
DR RefSeq; NP_564947.1; NM_105558.3.
DR AlphaFoldDB; P82280; -.
DR SMR; P82280; -.
DR BioGRID; 28437; 6.
DR DIP; DIP-59694N; -.
DR IntAct; P82280; 6.
DR STRING; 3702.AT1G68840.2; -.
DR iPTMnet; P82280; -.
DR PaxDb; P82280; -.
DR PRIDE; P82280; -.
DR ProteomicsDB; 236505; -.
DR EnsemblPlants; AT1G68840.1; AT1G68840.1; AT1G68840.
DR EnsemblPlants; AT1G68840.2; AT1G68840.2; AT1G68840.
DR GeneID; 843216; -.
DR Gramene; AT1G68840.1; AT1G68840.1; AT1G68840.
DR Gramene; AT1G68840.2; AT1G68840.2; AT1G68840.
DR KEGG; ath:AT1G68840; -.
DR Araport; AT1G68840; -.
DR TAIR; locus:2012438; AT1G68840.
DR eggNOG; ENOG502QRVI; Eukaryota.
DR HOGENOM; CLU_038898_0_0_1; -.
DR InParanoid; P82280; -.
DR OMA; SKTSDSM; -.
DR OrthoDB; 810704at2759; -.
DR PhylomeDB; P82280; -.
DR PRO; PR:P82280; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P82280; baseline and differential.
DR Genevisible; P82280; 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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR CDD; cd00018; AP2; 1.
DR CDD; cd10017; B3_DNA; 1.
DR Gene3D; 2.40.330.10; -; 1.
DR Gene3D; 3.30.730.10; -; 1.
DR InterPro; IPR001471; AP2/ERF_dom.
DR InterPro; IPR036955; AP2/ERF_dom_sf.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR044800; LEC2-like.
DR PANTHER; PTHR31140; PTHR31140; 1.
DR Pfam; PF00847; AP2; 1.
DR Pfam; PF02362; B3; 1.
DR SMART; SM00380; AP2; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; SSF101936; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS51032; AP2_ERF; 1.
DR PROSITE; PS50863; B3; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Ethylene signaling pathway; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..352
FT /note="AP2/ERF and B3 domain-containing transcription
FT repressor RAV2"
FT /id="PRO_0000297937"
FT DNA_BIND 64..119
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT DNA_BIND 188..291
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 184
FT /note="R -> C (in Ref. 6; AAC49774)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="K -> N (in Ref. 5; AAM63120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39493 MW; D130DA8DA99ACC75 CRC64;
MDSSCIDEIS SSTSESFSAT TAKKLSPPPA AALRLYRMGS GGSSVVLDPE NGLETESRKL
PSSKYKGVVP QPNGRWGAQI YEKHQRVWLG TFNEQEEAAR SYDIAACRFR GRDAVVNFKN
VLEDGDLAFL EAHSKAEIVD MLRKHTYADE LEQNNKRQLF LSVDANGKRN GSSTTQNDKV
LKTREVLFEK AVTPSDVGKL NRLVIPKQHA EKHFPLPSPS PAVTKGVLIN FEDVNGKVWR
FRYSYWNSSQ SYVLTKGWSR FVKEKNLRAG DVVTFERSTG LERQLYIDWK VRSGPRENPV
QVVVRLFGVD IFNVTTVKPN DVVAVCGGKR SRDVDDMFAL RCSKKQAIIN AL
