RAV1_ARATH
ID RAV1_ARATH Reviewed; 344 AA.
AC Q9ZWM9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=AP2/ERF and B3 domain-containing transcription factor RAV1;
DE AltName: Full=Ethylene-responsive transcription factor RAV1;
DE AltName: Full=Protein RELATED TO ABI3/VP1 1;
GN Name=RAV1; OrderedLocusNames=At1g13260; ORFNames=T6J4.2;
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, AND TISSUE SPECIFICITY.
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] {ECO:0000312|EMBL:AAL36211.1}
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 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).
RN [6]
RP STRUCTURE BY NMR OF 182-298.
RX PubMed=15548737; DOI=10.1105/tpc.104.026112;
RA Yamasaki K., Kigawa T., Inoue M., Tateno M., Yamasaki T., Yabuki T.,
RA Aoki M., Seki E., Matsuda T., Tomo Y., Hayami N., Terada T., Shirouzu M.,
RA Osanai T., Tanaka A., Seki M., Shinozaki K., Yokoyama S.;
RT "Solution structure of the B3 DNA binding domain of the Arabidopsis cold-
RT responsive transcription factor RAV1.";
RL Plant Cell 16:3448-3459(2004).
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, AND INDUCTION.
RX PubMed=15040885; DOI=10.1038/sj.cr.7290197;
RA Hu Y.X., Wang Y.H., Liu X.F., Li J.Y.;
RT "Arabidopsis RAV1 is down-regulated by brassinosteroid and may act as a
RT negative regulator during plant development.";
RL Cell Res. 14:8-15(2004).
CC -!- FUNCTION: Binds specifically to bipartite recognition sequences
CC composed of two unrelated motifs, 5'-CAACA-3' and 5'-CACCTG-3'. May
CC function as negative regulator of plant growth and development.
CC {ECO:0000269|PubMed:15040885, ECO:0000269|PubMed:9862967}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined: Roots, rosette
CC leaves, cauline leaves, inflorescence stems, flowers and siliques.
CC Highest expression in roots and rosette leaves. Very low expression in
CC flowers. {ECO:0000269|PubMed:9862967}.
CC -!- INDUCTION: Down-regulated by brassinosteroid and zeatin.
CC {ECO:0000269|PubMed:15040885}.
CC -!- DOMAIN: Contains two distinct DNA-binding domains. One is located in
CC the N-terminal region and binds to the 5'-CAACA-3' motif. The second is
CC located in the C-terminal region and binds to the 5'-CACCTG-3' motif.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. RAV
CC subfamily. {ECO:0000305}.
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DR EMBL; AB013886; BAA34250.1; -; mRNA.
DR EMBL; AC011810; AAG09554.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28991.1; -; Genomic_DNA.
DR EMBL; AY063855; AAL36211.1; -; mRNA.
DR EMBL; AY091291; AAM14230.1; -; mRNA.
DR PIR; T51329; T51329.
DR RefSeq; NP_172784.1; NM_101197.4.
DR PDB; 1WID; NMR; -; A=182-298.
DR PDBsum; 1WID; -.
DR AlphaFoldDB; Q9ZWM9; -.
DR SMR; Q9ZWM9; -.
DR BioGRID; 23126; 16.
DR IntAct; Q9ZWM9; 8.
DR STRING; 3702.AT1G13260.1; -.
DR iPTMnet; Q9ZWM9; -.
DR PaxDb; Q9ZWM9; -.
DR PRIDE; Q9ZWM9; -.
DR ProteomicsDB; 236987; -.
DR EnsemblPlants; AT1G13260.1; AT1G13260.1; AT1G13260.
DR GeneID; 837886; -.
DR Gramene; AT1G13260.1; AT1G13260.1; AT1G13260.
DR KEGG; ath:AT1G13260; -.
DR Araport; AT1G13260; -.
DR TAIR; locus:2205319; AT1G13260.
DR eggNOG; ENOG502QRVI; Eukaryota.
DR HOGENOM; CLU_038898_0_0_1; -.
DR OMA; MAFLNTH; -.
DR OrthoDB; 810704at2759; -.
DR PhylomeDB; Q9ZWM9; -.
DR EvolutionaryTrace; Q9ZWM9; -.
DR PRO; PR:Q9ZWM9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWM9; baseline and differential.
DR Genevisible; Q9ZWM9; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; 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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IEP: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 3D-structure; DNA-binding; Ethylene signaling pathway; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..344
FT /note="AP2/ERF and B3 domain-containing transcription
FT factor RAV1"
FT /id="PRO_0000112571"
FT DNA_BIND 61..116
FT /note="AP2/ERF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT DNA_BIND 188..292
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1WID"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1WID"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1WID"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1WID"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1WID"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1WID"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1WID"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1WID"
SQ SEQUENCE 344 AA; 38597 MW; 7349B640B3505823 CRC64;
MESSSVDEST TSTGSICETP AITPAKKSSV GNLYRMGSGS SVVLDSENGV EAESRKLPSS
KYKGVVPQPN GRWGAQIYEK HQRVWLGTFN EEDEAARAYD VAVHRFRRRD AVTNFKDVKM
DEDEVDFLNS HSKSEIVDML RKHTYNEELE QSKRRRNGNG NMTRTLLTSG LSNDGVSTTG
FRSAEALFEK AVTPSDVGKL NRLVIPKHHA EKHFPLPSSN VSVKGVLLNF EDVNGKVWRF
RYSYWNSSQS YVLTKGWSRF VKEKNLRAGD VVSFSRSNGQ DQQLYIGWKS RSGSDLDAGR
VLRLFGVNIS PESSRNDVVG NKRVNDTEML SLVCSKKQRI FHAS
