ARFG_ARATH
ID ARFG_ARATH Reviewed; 1164 AA.
AC P93022; O24411; P93023; Q0WWZ8; Q5IRX8; Q8RXZ7; Q9LCZ5; Q9SBK4; Q9SYQ6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Auxin response factor 7 {ECO:0000303|PubMed:10318972, ECO:0000303|PubMed:10476078, ECO:0000303|PubMed:15659631};
DE AltName: Full=Auxin-responsive protein IAA21/IAA23/IAA25 {ECO:0000303|PubMed:9342315};
DE AltName: Full=Protein BIPOSTO;
DE AltName: Full=Protein MASSUGU 1 {ECO:0000303|PubMed:14729917};
DE AltName: Full=Protein NON-PHOTOTROPIC HYPOCOTYL 4 {ECO:0000303|PubMed:10810148, ECO:0000303|PubMed:15659631};
DE AltName: Full=Protein TRANSPORT INHIBITOR RESPONSE 5 {ECO:0000303|PubMed:14729917, ECO:0000303|PubMed:16461383};
GN Name=ARF7 {ECO:0000303|PubMed:10318972, ECO:0000303|PubMed:10476078,
GN ECO:0000303|PubMed:15659631};
GN Synonyms=BIP, IAA21 {ECO:0000303|PubMed:9342315},
GN IAA23 {ECO:0000303|PubMed:9342315}, IAA25 {ECO:0000303|PubMed:9342315},
GN MSG1 {ECO:0000303|PubMed:14729917}, NPH4 {ECO:0000303|PubMed:10810148,
GN ECO:0000303|PubMed:15659631}, TIR5 {ECO:0000303|PubMed:14729917,
GN ECO:0000303|PubMed:16461383};
GN OrderedLocusNames=At5g20730 {ECO:0000312|Araport:AT5G20730};
GN ORFNames=T1M15.130 {ECO:0000312|EMBL:AF296832};
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] (ISOFORM 1), AND TRANSCRIPTIONAL ACTIVATOR.
RC STRAIN=cv. Columbia;
RX PubMed=10318972; DOI=10.1073/pnas.96.10.5844;
RA Ulmasov T., Hagen G., Guilfoyle T.J.;
RT "Activation and repression of transcription by auxin-response factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5844-5849(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=15659631; DOI=10.1105/tpc.104.028316;
RA Okushima Y., Overvoorde P.J., Arima K., Alonso J.M., Chan A., Chang C.,
RA Ecker J.R., Hughes B., Lui A., Nguyen D., Onodera C., Quach H., Smith A.,
RA Yu G., Theologis A.;
RT "Functional genomic analysis of the AUXIN RESPONSE FACTOR gene family
RT members in Arabidopsis thaliana: unique and overlapping functions of ARF7
RT and ARF19.";
RL Plant Cell 17:444-463(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Hardtke C.S., Berleth T.;
RT "A novel transcription factor, closely related to the Arabidopsis MP
RT protein, interacts genetically with C-terminal domains of the MP product.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10810148; DOI=10.2307/3870999;
RA Harper R.M., Stowe-Evans E.L., Luesse D.R., Muto H., Tatematsu K.,
RA Watahiki M.K., Yamamoto K.T., Liscum E.;
RT "The NPH4 locus encodes the auxin response factor ARF7, a conditional
RT regulator of differential growth in aerial Arabidopsis tissue.";
RL Plant Cell 12:757-770(2000).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-1164 (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 551-966.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-1164 (ISOFORMS 1 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=9342315; DOI=10.1073/pnas.94.22.11786;
RA Kim J., Harter K., Theologis A.;
RT "Protein-protein interactions among the Aux/IAA proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11786-11791(1997).
RN [10]
RP DIMERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=10476078; DOI=10.1046/j.1365-313x.1999.00538.x;
RA Ulmasov T., Hagen G., Guilfoyle T.J.;
RT "Dimerization and DNA binding of auxin response factors.";
RL Plant J. 19:309-319(1999).
RN [11]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=12036261; DOI=10.1023/a:1015207114117;
RA Hagen G., Guilfoyle T.J.;
RT "Auxin-responsive gene expression: genes, promoters and regulatory
RT factors.";
RL Plant Mol. Biol. 49:373-385(2002).
RN [12]
RP INTERACTION WITH IAA19.
RX PubMed=14729917; DOI=10.1105/tpc.018630;
RA Tatematsu K., Kumagai S., Muto H., Sato A., Watahiki M.K., Harper R.M.,
RA Liscum E., Yamamoto K.T.;
RT "MASSUGU2 encodes Aux/IAA19, an auxin-regulated protein that functions
RT together with the transcriptional activator NPH4/ARF7 to regulate
RT differential growth responses of hypocotyl and formation of lateral roots
RT in Arabidopsis thaliana.";
RL Plant Cell 16:379-393(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH IAA12.
RX PubMed=14973283; DOI=10.1242/dev.00925;
RA Hardtke C.S., Ckurshumova W., Vidaurre D.P., Singh S.A., Stamatiou G.,
RA Tiwari S.B., Hagen G., Guilfoyle T.J., Berleth T.;
RT "Overlapping and non-redundant functions of the Arabidopsis auxin response
RT factors MONOPTEROS and NONPHOTOTROPIC HYPOCOTYL 4.";
RL Development 131:1089-1100(2004).
RN [14]
RP FUNCTION.
RX PubMed=16461383; DOI=10.1104/pp.105.070987;
RA Li J., Dai X., Zhao Y.;
RT "A role for auxin response factor 19 in auxin and ethylene signaling in
RT Arabidopsis.";
RL Plant Physiol. 140:899-908(2006).
RN [15]
RP FUNCTION.
RX PubMed=16371470; DOI=10.1073/pnas.0507127103;
RA Esmon C.A., Tinsley A.G., Ljung K., Sandberg G., Hearne L.B., Liscum E.;
RT "A gradient of auxin and auxin-dependent transcription precedes tropic
RT growth responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:236-241(2006).
RN [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH ARF5.
RX PubMed=17259263; DOI=10.1105/tpc.106.047761;
RA Okushima Y., Fukaki H., Onoda M., Theologis A., Tasaka M.;
RT "ARF7 and ARF19 regulate lateral root formation via direct activation of
RT LBD/ASL genes in Arabidopsis.";
RL Plant Cell 19:118-130(2007).
RN [17]
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 [18]
RP INTERACTION.
RX PubMed=21734647; DOI=10.1038/msb.2011.39;
RA Vernoux T., Brunoud G., Farcot E., Morin V., Van den Daele H., Legrand J.,
RA Oliva M., Das P., Larrieu A., Wells D., Guedon Y., Armitage L., Picard F.,
RA Guyomarc'h S., Cellier C., Parry G., Koumproglou R., Doonan J.H.,
RA Estelle M., Godin C., Kepinski S., Bennett M., De Veylder L., Traas J.;
RT "The auxin signalling network translates dynamic input into robust
RT patterning at the shoot apex.";
RL Mol. Syst. Biol. 7:508-508(2011).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATXR2, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29184030; DOI=10.1126/scisignal.aan0316;
RA Lee K., Park O.S., Seo P.J.;
RT "Arabidopsis ATXR2 deposits H3K36me3 at the promoters of LBD genes to
RT facilitate cellular dedifferentiation.";
RL Sci. Signal. 10:0-0(2017).
RN [20]
RP INTERACTION WITH JMJ30.
RC STRAIN=cv. Columbia;
RX PubMed=29923261; DOI=10.1111/tpj.14002;
RA Lee K., Park O.-S., Seo P.J.;
RT "JMJ30-mediated demethylation of H3K9me3 drives tissue identity changes to
RT promote callus formation in Arabidopsis.";
RL Plant J. 95:961-975(2018).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1036-1126, MUTAGENESIS OF
RP LYS-1041; ASP-1091 AND ASP-1095, INTERACTION WITH IAA17, AND DOMAIN.
RX PubMed=24706860; DOI=10.1073/pnas.1400074111;
RA Korasick D.A., Westfall C.S., Lee S.G., Nanao M.H., Dumas R., Hagen G.,
RA Guilfoyle T.J., Jez J.M., Strader L.C.;
RT "Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the
RT control of auxin response repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5427-5432(2014).
CC -!- FUNCTION: Auxin response factors (ARFs) are transcriptional factors
CC that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the
CC auxin-responsive promoter elements (AuxREs). Acts as a transcriptional
CC activator of several tropic stimulus-induced (TSI) genes, including
CC SAUR50. Formation of heterodimers with Aux/IAA proteins may alter their
CC ability to modulate early auxin response genes expression. Required for
CC differential growth responses of aerial tissues. Involved in ethylene
CC responses. Regulates lateral root formation through direct regulation
CC of LBD16 and/or LBD29 (PubMed:29184030). Functionally redundant with
CC ARF19 (PubMed:29184030). Mediates embryo axis formation and vascular
CC tissues differentiation. Functionally redundant with ARF5. Involved in
CC cellular dedifferentiation during callus formation on callus-inducing
CC medium (CIM) and in an ATXR2-dependent manner (PubMed:29184030).
CC {ECO:0000269|PubMed:12036261, ECO:0000269|PubMed:14973283,
CC ECO:0000269|PubMed:16371470, ECO:0000269|PubMed:16461383,
CC ECO:0000269|PubMed:17259263, ECO:0000269|PubMed:29184030}.
CC -!- SUBUNIT: Homodimers and heterodimers (PubMed:10476078,
CC PubMed:21734647). Interacts with the auxin-responsive proteins IAA1 and
CC IAA12 (BODENLOS)(PubMed:14973283, PubMed:21734647). Interacts (via PB1
CC domain) with IAA17 (via PB1 domain) (PubMed:24706860, PubMed:21734647).
CC Interacts with IAA19 (PubMed:14729917, PubMed:21734647). Interacts with
CC ARF5 (PubMed:17259263, PubMed:21734647). Binds to JMJ30
CC (PubMed:29923261). Binds to ATXR2 in the nucleus (PubMed:29184030).
CC {ECO:0000269|PubMed:10476078, ECO:0000269|PubMed:14729917,
CC ECO:0000269|PubMed:14973283, ECO:0000269|PubMed:17259263,
CC ECO:0000269|PubMed:21734647, ECO:0000269|PubMed:24706860,
CC ECO:0000269|PubMed:29184030, ECO:0000269|PubMed:29923261}.
CC -!- INTERACTION:
CC P93022; Q39011: ASK7; NbExp=2; IntAct=EBI-632284, EBI-1798250;
CC P93022; P49677: IAA1; NbExp=4; IntAct=EBI-632284, EBI-630505;
CC P93022; Q38832: IAA14; NbExp=3; IntAct=EBI-632284, EBI-2295562;
CC P93022; O24408: IAA18; NbExp=3; IntAct=EBI-632284, EBI-2295525;
CC P93022; O24409: IAA19; NbExp=5; IntAct=EBI-632284, EBI-632257;
CC P93022; Q38822: IAA3; NbExp=2; IntAct=EBI-632284, EBI-307174;
CC P93022; Q9SN12: MYB77; NbExp=3; IntAct=EBI-632284, EBI-2324225;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326,
CC ECO:0000269|PubMed:29184030}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P93022-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93022-2; Sequence=VSP_010090;
CC Name=3;
CC IsoId=P93022-3; Sequence=VSP_010091;
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC {ECO:0000269|PubMed:10476078}.
CC -!- DOMAIN: The PB1 domain provides both positive and negative
CC electrostatic interfaces for directional protein interaction.
CC {ECO:0000269|PubMed:24706860}.
CC -!- DISRUPTION PHENOTYPE: The arf7-1 arf19-2 double mutant is defective in
CC callus formation. {ECO:0000269|PubMed:29184030}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. May be due to exon
CC skipping. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ARF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB92474.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF042195; AAD02218.1; -; mRNA.
DR EMBL; AY008392; AAG35177.1; -; Genomic_DNA.
DR EMBL; AY669789; AAT67073.1; -; mRNA.
DR EMBL; AF022368; AAD04807.1; -; mRNA.
DR EMBL; AF186466; AAF71831.1; -; Genomic_DNA.
DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92884.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92885.1; -; Genomic_DNA.
DR EMBL; AY080595; AAL85006.1; -; mRNA.
DR EMBL; U49077; AAB84358.1; -; mRNA.
DR EMBL; U79555; AAB92474.1; ALT_FRAME; mRNA.
DR EMBL; U79556; AAB92475.1; -; mRNA.
DR EMBL; AK226185; BAE98350.1; -; mRNA.
DR RefSeq; NP_851046.1; NM_180715.1. [P93022-2]
DR RefSeq; NP_851047.1; NM_180716.3. [P93022-1]
DR PDB; 4NJ6; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1036-1126.
DR PDB; 4NJ7; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1036-1126.
DR PDBsum; 4NJ6; -.
DR PDBsum; 4NJ7; -.
DR AlphaFoldDB; P93022; -.
DR SMR; P93022; -.
DR BioGRID; 17471; 36.
DR DIP; DIP-34948N; -.
DR IntAct; P93022; 26.
DR STRING; 3702.AT5G20730.1; -.
DR PaxDb; P93022; -.
DR ProteomicsDB; 241021; -. [P93022-1]
DR EnsemblPlants; AT5G20730.1; AT5G20730.1; AT5G20730. [P93022-2]
DR EnsemblPlants; AT5G20730.2; AT5G20730.2; AT5G20730. [P93022-1]
DR GeneID; 832196; -.
DR Gramene; AT5G20730.1; AT5G20730.1; AT5G20730. [P93022-2]
DR Gramene; AT5G20730.2; AT5G20730.2; AT5G20730. [P93022-1]
DR KEGG; ath:AT5G20730; -.
DR Araport; AT5G20730; -.
DR TAIR; locus:2180469; AT5G20730.
DR eggNOG; ENOG502QV9B; Eukaryota.
DR InParanoid; P93022; -.
DR OrthoDB; 116399at2759; -.
DR PRO; PR:P93022; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P93022; baseline and differential.
DR Genevisible; P93022; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:TAIR.
DR GO; GO:1990110; P:callus formation; IMP:UniProtKB.
DR GO; GO:0009630; P:gravitropism; TAS:TAIR.
DR GO; GO:0048527; P:lateral root development; IGI:TAIR.
DR GO; GO:0010311; P:lateral root formation; IGI:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IGI:TAIR.
DR CDD; cd10017; B3_DNA; 1.
DR Gene3D; 2.40.330.10; -; 1.
DR InterPro; IPR010525; ARF_dom.
DR InterPro; IPR044835; ARF_plant.
DR InterPro; IPR033389; AUX/IAA_dom.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR000270; PB1_dom.
DR PANTHER; PTHR31384; PTHR31384; 3.
DR Pfam; PF02309; AUX_IAA; 1.
DR Pfam; PF06507; Auxin_resp; 1.
DR Pfam; PF02362; B3; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; SSF101936; 1.
DR PROSITE; PS50863; B3; 1.
DR PROSITE; PS51745; PB1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Auxin signaling pathway;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1164
FT /note="Auxin response factor 7"
FT /id="PRO_0000111511"
FT DOMAIN 1037..1130
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DNA_BIND 127..229
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT REGION 451..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 270
FT /note="R -> RW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010090"
FT VAR_SEQ 1144..1158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9342315"
FT /id="VSP_010091"
FT MUTAGEN 1041
FT /note="K->A: Loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:24706860"
FT MUTAGEN 1091
FT /note="D->A: Loss of oligomerization; when associated with
FT A-1095. Loss of oligomerization; when associated with A-
FT 1041 and A-1095."
FT /evidence="ECO:0000269|PubMed:24706860"
FT MUTAGEN 1095
FT /note="D->A: Loss of oligomerization; when associated with
FT A-1091. Loss of oligomerization; when associated with A-
FT 1041 and A-1091."
FT /evidence="ECO:0000269|PubMed:24706860"
FT CONFLICT 108
FT /note="D -> N (in Ref. 3; AAD04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> F (in Ref. 3; AAD04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="K -> E (in Ref. 3; AAD04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="H -> D (in Ref. 3; AAD04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="S -> A (in Ref. 1; AAD02218)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="Q -> H (in Ref. 1; AAD02218)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="N -> I (in Ref. 3; AAD04807)"
FT /evidence="ECO:0000305"
FT CONFLICT 839..853
FT /note="Missing (in Ref. 9; AAB92475)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="T -> N (in Ref. 9; AAB92475)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038..1052
FT /note="Missing (in Ref. 9; AAB92475)"
FT /evidence="ECO:0000305"
FT STRAND 1040..1044
FT /evidence="ECO:0007829|PDB:4NJ6"
FT STRAND 1049..1052
FT /evidence="ECO:0007829|PDB:4NJ6"
FT HELIX 1054..1056
FT /evidence="ECO:0007829|PDB:4NJ6"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:4NJ6"
FT HELIX 1060..1070
FT /evidence="ECO:0007829|PDB:4NJ6"
FT TURN 1074..1078
FT /evidence="ECO:0007829|PDB:4NJ6"
FT TURN 1080..1082
FT /evidence="ECO:0007829|PDB:4NJ6"
FT STRAND 1084..1091
FT /evidence="ECO:0007829|PDB:4NJ6"
FT TURN 1092..1094
FT /evidence="ECO:0007829|PDB:4NJ6"
FT STRAND 1095..1098
FT /evidence="ECO:0007829|PDB:4NJ6"
FT HELIX 1104..1110
FT /evidence="ECO:0007829|PDB:4NJ6"
FT STRAND 1113..1117
FT /evidence="ECO:0007829|PDB:4NJ6"
FT HELIX 1119..1123
FT /evidence="ECO:0007829|PDB:4NJ6"
SQ SEQUENCE 1164 AA; 128886 MW; 6A2858510130F5B1 CRC64;
MKAPSSNGVS PNPVEGERRN INSELWHACA GPLISLPPAG SLVVYFPQGH SEQVAASMQK
QTDFIPSYPN LPSKLICMLH NVTLNADPET DEVYAQMTLQ PVNKYDRDAL LASDMGLKLN
RQPNEFFCKT LTASDTSTHG GFSVPRRAAE KIFPALDFSM QPPCQELVAK DIHDNTWTFR
HIYRGQPKRH LLTTGWSVFV STKRLFAGDS VLFIRDGKAQ LLLGIRRANR QQPALSSSVI
SSDSMHIGVL AAAAHANANN SPFTIFYNPR AAPAEFVVPL AKYTKAMYAQ VSLGMRFRMI
FETEECGVRR YMGTVTGISD LDPVRWKNSQ WRNLQIGWDE SAAGDRPSRV SVWDIEPVLT
PFYICPPPFF RPRFSGQPGM PDDETDMESA LKRAMPWLDN SLEMKDPSST IFPGLSLVQW
MNMQQQNGQL PSAAAQPGFF PSMLSPTAAL HNNLGGTDDP SKLLSFQTPH GGISSSNLQF
NKQNQQAPMS QLPQPPTTLS QQQQLQQLLH SSLNHQQQQS QSQQQQQQQQ LLQQQQQLQS
QQHSNNNQSQ SQQQQQLLQQ QQQQQLQQQH QQPLQQQTQQ QQLRTQPLQS HSHPQPQQLQ
QHKLQQLQVP QNQLYNGQQA AQQHQSQQAS THHLQPQLVS GSMASSVITP PSSSLNQSFQ
QQQQQSKQLQ QAHHHLGAST SQSSVIETSK SSSNLMSAPP QETQFSRQVE QQQPPGLNGQ
NQQTLLQQKA HQAQAQQIFQ QSLLEQPHIQ FQLLQRLQQQ QQQQFLSPQS QLPHHQLQSQ
QLQQLPTLSQ GHQFPSSCTN NGLSTLQPPQ MLVSRPQEKQ NPPVGGGVKA YSGITDGGDA
PSSSTSPSTN NCQISSSGFL NRSQSGPAIL IPDAAIDMSG NLVQDLYSKS DMRLKQELVG
QQKSKASLTD HQLEASASGT SYGLDGGENN RQQNFLAPTF GLDGDSRNSL LGGANVDNGF
VPDTLLSRGY DSQKDLQNML SNYGGVTNDI GTEMSTSAVR TQSFGVPNVP AISNDLAVND
AGVLGGGLWP AQTQRMRTYT KVQKRGSVGR SIDVNRYRGY DELRHDLARM FGIEGQLEDP
QTSDWKLVYV DHENDILLVG DDPWEEFVNC VQSIKILSSA EVQQMSLDGN FAGVPVTNQA
CSGGDSGNAW RGHYDDNSAT SFNR
