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IAA19_ARATH
ID   IAA19_ARATH             Reviewed;         197 AA.
AC   O24409; Q8L8X3; Q9LDL6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Auxin-responsive protein IAA19;
DE   AltName: Full=Indoleacetic acid-induced protein 19;
DE   AltName: Full=Protein MASSUGU 2;
GN   Name=IAA19; Synonyms=MSG2; OrderedLocusNames=At3g15540; ORFNames=MJK13.20;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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 53-197.
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   [6]
RP   MUTANTS MSG2-1; MSG2-2; MSG2-3 AND MSG2-4, AND INDUCTION BY AUXIN.
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   [7]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=12036262; DOI=10.1023/a:1015255030047;
RA   Liscum E., Reed J.W.;
RT   "Genetics of Aux/IAA and ARF action in plant growth and development.";
RL   Plant Mol. Biol. 49:387-400(2002).
RN   [8]
RP   TRANSCRIPTIONAL REPRESSION DOMAIN.
RX   PubMed=14742873; DOI=10.1105/tpc.017384;
RA   Tiwari S.B., Hagen G., Guilfoyle T.J.;
RT   "Aux/IAA proteins contain a potent transcriptional repression domain.";
RL   Plant Cell 16:533-543(2004).
RN   [9]
RP   INDUCTION BY AUXIN.
RX   PubMed=16901781; DOI=10.1016/j.cell.2006.05.050;
RA   Nemhauser J.L., Hong F., Chory J.;
RT   "Different plant hormones regulate similar processes through largely
RT   nonoverlapping transcriptional responses.";
RL   Cell 126:467-475(2006).
RN   [10]
RP   INDUCTION BY PHOTOTROPISM.
RX   DOI=10.1111/j.1399-3054.2007.00898.x;
RA   Saito K., Watahiki M.K., Yamamoto K.T.;
RT   "Differential expression of the auxin primary response gene
RT   MASSUGU2/IAA19during tropic responses of Arabidopsis hypocotyls.";
RL   Physiol. Plantarum 130:146-158(2007).
CC   -!- FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that
CC       function as repressors of early auxin response genes at low auxin
CC       concentrations. Repression is thought to result from the interaction
CC       with auxin response factors (ARFs), proteins that bind to the auxin-
CC       responsive promoter element (AuxRE). Formation of heterodimers with ARF
CC       proteins may alter their ability to modulate early auxin response genes
CC       expression. {ECO:0000269|PubMed:12036262}.
CC   -!- SUBUNIT: Homodimers and heterodimers. Interacts with the auxin response
CC       factor ARF7.
CC   -!- INTERACTION:
CC       O24409; Q9C5W9: ARF18; NbExp=6; IntAct=EBI-632257, EBI-3946783;
CC       O24409; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-632257, EBI-529887;
CC       O24409; Q9ZTX9: ARF4; NbExp=2; IntAct=EBI-632257, EBI-3946495;
CC       O24409; P93024: ARF5; NbExp=4; IntAct=EBI-632257, EBI-629519;
CC       O24409; P93022: ARF7; NbExp=5; IntAct=EBI-632257, EBI-632284;
CC       O24409; Q9FGV1: ARF8; NbExp=4; IntAct=EBI-632257, EBI-1554169;
CC       O24409; Q9XED8: ARF9; NbExp=2; IntAct=EBI-632257, EBI-3946762;
CC       O24409; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-632257, EBI-25523851;
CC       O24409; P49677: IAA1; NbExp=12; IntAct=EBI-632257, EBI-630505;
CC       O24409; Q38828: IAA10; NbExp=9; IntAct=EBI-632257, EBI-3946434;
CC       O24409; Q38829: IAA11; NbExp=7; IntAct=EBI-632257, EBI-2367923;
CC       O24409; Q38830: IAA12; NbExp=8; IntAct=EBI-632257, EBI-617608;
CC       O24409; Q38831: IAA13; NbExp=11; IntAct=EBI-632257, EBI-1554143;
CC       O24409; Q38832: IAA14; NbExp=4; IntAct=EBI-632257, EBI-2295562;
CC       O24409; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-632257, EBI-25524519;
CC       O24409; O24407: IAA16; NbExp=11; IntAct=EBI-632257, EBI-632231;
CC       O24409; P93830: IAA17; NbExp=11; IntAct=EBI-632257, EBI-632243;
CC       O24409; O24408: IAA18; NbExp=3; IntAct=EBI-632257, EBI-2295525;
CC       O24409; O24409: IAA19; NbExp=4; IntAct=EBI-632257, EBI-632257;
CC       O24409; P49678: IAA2; NbExp=10; IntAct=EBI-632257, EBI-632343;
CC       O24409; O24410: IAA20; NbExp=5; IntAct=EBI-632257, EBI-632272;
CC       O24409; Q8LAL2: IAA26; NbExp=9; IntAct=EBI-632257, EBI-3947418;
CC       O24409; Q9ZSY8: IAA27; NbExp=10; IntAct=EBI-632257, EBI-3946677;
CC       O24409; Q9XFM0: IAA28; NbExp=9; IntAct=EBI-632257, EBI-3133404;
CC       O24409; Q38822: IAA3; NbExp=11; IntAct=EBI-632257, EBI-307174;
CC       O24409; Q8H174: IAA31; NbExp=11; IntAct=EBI-632257, EBI-3946408;
CC       O24409; Q8RYC6: IAA32; NbExp=3; IntAct=EBI-632257, EBI-3946448;
CC       O24409; Q9FKM7: IAA33; NbExp=3; IntAct=EBI-632257, EBI-3946739;
CC       O24409; Q9C5X0: IAA34; NbExp=8; IntAct=EBI-632257, EBI-3946459;
CC       O24409; P33077: IAA4; NbExp=9; IntAct=EBI-632257, EBI-632187;
CC       O24409; P33078: IAA5; NbExp=6; IntAct=EBI-632257, EBI-3946487;
CC       O24409; Q38824: IAA6; NbExp=8; IntAct=EBI-632257, EBI-1554124;
CC       O24409; Q38825: IAA7; NbExp=7; IntAct=EBI-632257, EBI-602959;
CC       O24409; Q38826: IAA8; NbExp=7; IntAct=EBI-632257, EBI-632200;
CC       O24409; Q38827: IAA9; NbExp=4; IntAct=EBI-632257, EBI-632216;
CC       O24409; Q9LTC4: MYB15; NbExp=3; IntAct=EBI-632257, EBI-21497119;
CC       O24409; O22179: MYB70; NbExp=3; IntAct=EBI-632257, EBI-1238013;
CC       O24409; Q9SN12: MYB77; NbExp=3; IntAct=EBI-632257, EBI-2324225;
CC       O24409; Q9FUA4: SPT; NbExp=3; IntAct=EBI-632257, EBI-1536703;
CC       O24409; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-632257, EBI-25522447;
CC       O24409; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-632257, EBI-4426557;
CC       O24409; O64722: ZHD3; NbExp=3; IntAct=EBI-632257, EBI-1806244;
CC       O24409; Q9SVL0: ZHD7; NbExp=3; IntAct=EBI-632257, EBI-1806382;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by auxin (PubMed:14729917, PubMed:16901781).
CC       Up-regulated by phototropism in hypocotyls, with a higher level on the
CC       shaded side (Ref.10). {ECO:0000269|PubMed:14729917,
CC       ECO:0000269|PubMed:16901781, ECO:0000269|Ref.10}.
CC   -!- DOMAIN: The N-terminal half of the protein contains two conserved
CC       domains I and II. Domain I includes a slightly degenerated ERF-
CC       associated amphiphilic repression (EAR) motif which seems to be
CC       involved in the activity of transcriptional repression. Domain II is
CC       required for the correct degradation of the protein through the SCF-
CC       mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA
CC       proteins and auxin response factors (ARFs) occur through their C-
CC       terminal dimerization domains III and IV.
CC   -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
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DR   EMBL; AB022218; BAB02383.1; -; Genomic_DNA.
DR   EMBL; AC024081; AAF35420.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75690.1; -; Genomic_DNA.
DR   EMBL; AY088753; AAM67069.1; -; mRNA.
DR   EMBL; U49075; AAB84356.1; -; mRNA.
DR   RefSeq; NP_188173.1; NM_112422.4.
DR   AlphaFoldDB; O24409; -.
DR   SMR; O24409; -.
DR   BioGRID; 6127; 60.
DR   DIP; DIP-34946N; -.
DR   ELM; O24409; -.
DR   IntAct; O24409; 52.
DR   STRING; 3702.AT3G15540.1; -.
DR   PaxDb; O24409; -.
DR   PRIDE; O24409; -.
DR   ProteomicsDB; 228812; -.
DR   EnsemblPlants; AT3G15540.1; AT3G15540.1; AT3G15540.
DR   GeneID; 820793; -.
DR   Gramene; AT3G15540.1; AT3G15540.1; AT3G15540.
DR   KEGG; ath:AT3G15540; -.
DR   Araport; AT3G15540; -.
DR   TAIR; locus:2090141; AT3G15540.
DR   eggNOG; ENOG502RXTN; Eukaryota.
DR   HOGENOM; CLU_049393_0_1_1; -.
DR   InParanoid; O24409; -.
DR   OMA; DKLFGFR; -.
DR   OrthoDB; 1208467at2759; -.
DR   PhylomeDB; O24409; -.
DR   PRO; PR:O24409; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O24409; baseline and differential.
DR   Genevisible; O24409; 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:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009733; P:response to auxin; TAS:TAIR.
DR   GO; GO:0080086; P:stamen filament development; IMP:TAIR.
DR   InterPro; IPR033389; AUX/IAA_dom.
DR   InterPro; IPR003311; AUX_IAA.
DR   InterPro; IPR000270; PB1_dom.
DR   PANTHER; PTHR31734; PTHR31734; 1.
DR   Pfam; PF02309; AUX_IAA; 1.
DR   PROSITE; PS51745; PB1; 1.
PE   1: Evidence at protein level;
KW   Auxin signaling pathway; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..197
FT                   /note="Auxin-responsive protein IAA19"
FT                   /id="PRO_0000112850"
FT   DOMAIN          96..184
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REGION          35..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           13..17
FT                   /note="EAR-like (transcriptional repression)"
FT   COMPBIAS        35..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         73
FT                   /note="G->R: In msg2-2; gain of function. Affects auxin-
FT                   related developmental processes."
FT   MUTAGEN         75
FT                   /note="P->L: In msg2-4; gain of function. Affects auxin-
FT                   related developmental processes."
FT   MUTAGEN         76
FT                   /note="P->L: In msg2-3; gain of function. Affects auxin-
FT                   related developmental processes."
FT   MUTAGEN         76
FT                   /note="P->S: In msg2-1; gain of function. Affects auxin-
FT                   related developmental processes."
FT   CONFLICT        126
FT                   /note="A -> S (in Ref. 4; AAM67069)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   197 AA;  21494 MW;  84B332B780132B53 CRC64;
     MEKEGLGLEI TELRLGLPGR DVAEKMMKKR AFTEMNMTSS GSNSDQCESG VVSSGGDAEK
     VNDSPAAKSQ VVGWPPVCSY RKKNSCKEAS TTKVGLGYVK VSMDGVPYLR KMDLGSSQGY
     DDLAFALDKL FGFRGIGVAL KDGDNCEYVT IYEDKDGDWM LAGDVPWGMF LESCKRLRIM
     KRSDATGFGL QPRGVDE
 
 
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