ARFS_ARATH
ID ARFS_ARATH Reviewed; 1086 AA.
AC Q8RYC8; O49961; Q5IRX3; Q9LMA4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Auxin response factor 19 {ECO:0000303|PubMed:15659631};
DE AltName: Full=Auxin-responsive protein IAA22 {ECO:0000303|PubMed:9342315};
GN Name=ARF19 {ECO:0000303|PubMed:15659631};
GN Synonyms=IAA22 {ECO:0000303|PubMed:9342315};
GN OrderedLocusNames=At1g19220 {ECO:0000312|Araport:AT1G19220};
GN ORFNames=T29M8.9 {ECO:0000312|EMBL:AAF82232.1};
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 [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
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 [2]
RP SEQUENCE REVISION.
RA Arima K., Overvoorde P.J., Theologis A.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 809-1086.
RC STRAIN=cv. Columbia;
RA Ciarbelli A.R., Carabelli M., Ruzza V., Sessa G., Steindler C., Ruberti I.;
RT "Nucleotide sequence of the Arabidopsis IAA22.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP FUNCTION, AND INDUCTION.
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 [10]
RP FUNCTION.
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 [11]
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 [12]
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 [13]
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).
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). Could act as
CC transcriptional activator or repressor. Formation of heterodimers with
CC Aux/IAA proteins may alter their ability to modulate early auxin
CC response genes expression. Involved in ethylene responses. Regulates
CC lateral root formation through direct regulation of LBD16 and/or LBD29
CC (PubMed:29184030). Functionally redundant with ARF7 (PubMed:29184030).
CC Involved in cellular dedifferentiation during callus formation on
CC callus-inducing medium (CIM) and in an ATXR2-dependent manner
CC (PubMed:29184030). {ECO:0000269|PubMed:12036261,
CC ECO:0000269|PubMed:16461383, ECO:0000269|PubMed:17259263,
CC ECO:0000269|PubMed:29184030}.
CC -!- SUBUNIT: Homodimers and heterodimers (PubMed:9342315). Interacts with
CC the auxin-responsive protein IAA1 (PubMed:9342315). Binds to JMJ30
CC (PubMed:29923261). Binds to ATXR2 in the nucleus (PubMed:29184030).
CC {ECO:0000269|PubMed:29184030, ECO:0000269|PubMed:29923261,
CC ECO:0000269|PubMed:9342315}.
CC -!- INTERACTION:
CC Q8RYC8; P49677: IAA1; NbExp=4; IntAct=EBI-529887, EBI-630505;
CC Q8RYC8; Q38828: IAA10; NbExp=7; IntAct=EBI-529887, EBI-3946434;
CC Q8RYC8; Q38829: IAA11; NbExp=3; IntAct=EBI-529887, EBI-2367923;
CC Q8RYC8; Q38831: IAA13; NbExp=3; IntAct=EBI-529887, EBI-1554143;
CC Q8RYC8; Q38832: IAA14; NbExp=4; IntAct=EBI-529887, EBI-2295562;
CC Q8RYC8; O24407: IAA16; NbExp=6; IntAct=EBI-529887, EBI-632231;
CC Q8RYC8; P93830: IAA17; NbExp=6; IntAct=EBI-529887, EBI-632243;
CC Q8RYC8; O24408: IAA18; NbExp=5; IntAct=EBI-529887, EBI-2295525;
CC Q8RYC8; O24409: IAA19; NbExp=4; IntAct=EBI-529887, EBI-632257;
CC Q8RYC8; P49678: IAA2; NbExp=3; IntAct=EBI-529887, EBI-632343;
CC Q8RYC8; Q9XFM0: IAA28; NbExp=3; IntAct=EBI-529887, EBI-3133404;
CC Q8RYC8; Q93WC4: IAA29; NbExp=3; IntAct=EBI-529887, EBI-3946697;
CC Q8RYC8; Q38822: IAA3; NbExp=4; IntAct=EBI-529887, EBI-307174;
CC Q8RYC8; Q8RYC6: IAA32; NbExp=4; IntAct=EBI-529887, EBI-3946448;
CC Q8RYC8; Q9FKM7: IAA33; NbExp=4; IntAct=EBI-529887, EBI-3946739;
CC Q8RYC8; Q9C5X0: IAA34; NbExp=4; IntAct=EBI-529887, EBI-3946459;
CC Q8RYC8; P33077: IAA4; NbExp=3; IntAct=EBI-529887, EBI-632187;
CC Q8RYC8; P33078: IAA5; NbExp=3; IntAct=EBI-529887, EBI-3946487;
CC Q8RYC8; Q38825: IAA7; NbExp=6; IntAct=EBI-529887, EBI-602959;
CC Q8RYC8; Q38826: IAA8; NbExp=4; IntAct=EBI-529887, EBI-632200;
CC Q8RYC8; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-529887, EBI-15193025;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326,
CC ECO:0000269|PubMed:29184030, ECO:0000269|PubMed:9342315}.
CC -!- INDUCTION: By auxin and ethylene. {ECO:0000269|PubMed:16461383}.
CC -!- DOMAIN: Interactions between auxin response factors (ARFs) and Aux/IAA
CC proteins occur through their C-terminal dimerization domains III and
CC IV. {ECO:0000269|PubMed:9342315}.
CC -!- DISRUPTION PHENOTYPE: The arf7-1 arf19-2 double mutant is defective in
CC callus formation. {ECO:0000269|PubMed:29184030}.
CC -!- SIMILARITY: Belongs to the ARF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82232.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U53672; AAB91321.2; -; mRNA.
DR EMBL; AY008390; AAG35176.1; -; Genomic_DNA.
DR EMBL; AY669794; AAT67078.1; -; mRNA.
DR EMBL; AC069143; AAF82232.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29819.1; -; Genomic_DNA.
DR EMBL; AB493467; BAH30305.1; -; mRNA.
DR EMBL; AJ441312; CAD29695.1; -; mRNA.
DR PIR; G86325; G86325.
DR RefSeq; NP_173356.1; NM_101780.4.
DR AlphaFoldDB; Q8RYC8; -.
DR SMR; Q8RYC8; -.
DR BioGRID; 23744; 137.
DR DIP; DIP-33547N; -.
DR IntAct; Q8RYC8; 139.
DR STRING; 3702.AT1G19220.1; -.
DR PaxDb; Q8RYC8; -.
DR PRIDE; Q8RYC8; -.
DR ProteomicsDB; 246596; -.
DR EnsemblPlants; AT1G19220.1; AT1G19220.1; AT1G19220.
DR GeneID; 838505; -.
DR Gramene; AT1G19220.1; AT1G19220.1; AT1G19220.
DR KEGG; ath:AT1G19220; -.
DR Araport; AT1G19220; -.
DR TAIR; locus:2202205; AT1G19220.
DR eggNOG; ENOG502QSK9; Eukaryota.
DR HOGENOM; CLU_002626_1_1_1; -.
DR InParanoid; Q8RYC8; -.
DR OMA; NHISQQM; -.
DR OrthoDB; 116399at2759; -.
DR PhylomeDB; Q8RYC8; -.
DR PRO; PR:Q8RYC8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RYC8; baseline and differential.
DR Genevisible; Q8RYC8; 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:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1990110; P:callus formation; IMP:UniProtKB.
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:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP: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; 1.
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 Auxin signaling pathway; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1086
FT /note="Auxin response factor 19"
FT /id="PRO_0000111523"
FT DOMAIN 958..1051
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DNA_BIND 126..228
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT REGION 454..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 120576 MW; 202C0944581E0545 CRC64;
MKAPSNGFLP SSNEGEKKPI NSQLWHACAG PLVSLPPVGS LVVYFPQGHS EQVAASMQKQ
TDFIPNYPNL PSKLICLLHS VTLHADTETD EVYAQMTLQP VNKYDREALL ASDMGLKLNR
QPTEFFCKTL TASDTSTHGG FSVPRRAAEK IFPPLDFSMQ PPAQEIVAKD LHDTTWTFRH
IYRGQPKRHL LTTGWSVFVS TKRLFAGDSV LFVRDEKSQL MLGIRRANRQ TPTLSSSVIS
SDSMHIGILA AAAHANANSS PFTIFFNPRA SPSEFVVPLA KYNKALYAQV SLGMRFRMMF
ETEDCGVRRY MGTVTGISDL DPVRWKGSQW RNLQVGWDES TAGDRPSRVS IWEIEPVITP
FYICPPPFFR PKYPRQPGMP DDELDMENAF KRAMPWMGED FGMKDAQSSM FPGLSLVQWM
SMQQNNPLSG SATPQLPSAL SSFNLPNNFA SNDPSKLLNF QSPNLSSANS QFNKPNTVNH
ISQQMQAQPA MVKSQQQQQQ QQQQHQHQQQ QLQQQQQLQM SQQQVQQQGI YNNGTIAVAN
QVSCQSPNQP TGFSQSQLQQ QSMLPTGAKM THQNINSMGN KGLSQMTSFA QEMQFQQQLE
MHNSSQLLRN QQEQSSLHSL QQNLSQNPQQ LQMQQQSSKP SPSQQLQLQL LQKLQQQQQQ
QSIPPVSSSL QPQLSALQQT QSHQLQQLLS SQNQQPLAHG NNSFPASTFM QPPQIQVSPQ
QQGQMSNKNL VAAGRSHSGH TDGEAPSCST SPSANNTGHD NVSPTNFLSR NQQQGQAASV
SASDSVFERA SNPVQELYTK TESRISQGMM NMKSAGEHFR FKSAVTDQID VSTAGTTYCP
DVVGPVQQQQ TFPLPSFGFD GDCQSHHPRN NLAFPGNLEA VTSDPLYSQK DFQNLVPNYG
NTPRDIETEL SSAAISSQSF GIPSIPFKPG CSNEVGGIND SGIMNGGGLW PNQTQRMRTY
TKVQKRGSVG RSIDVTRYSG YDELRHDLAR MFGIEGQLED PLTSDWKLVY TDHENDILLV
GDDPWEEFVN CVQNIKILSS VEVQQMSLDG DLAAIPTTNQ ACSETDSGNA WKVHYEDTSA
AASFNR
