IAA9_ARATH
ID IAA9_ARATH Reviewed; 338 AA.
AC Q38827; Q8LBP2; Q9FLH4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Auxin-responsive protein IAA9;
DE AltName: Full=Indoleacetic acid-induced protein 9;
GN Name=IAA9; OrderedLocusNames=At5g65670; ORFNames=F6H11.210, MPA24.1;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7658471; DOI=10.1006/jmbi.1995.0454;
RA Abel S., Nguyen M.D., Theologis A.;
RT "The PS-IAA4/5-like family of early auxin-inducible mRNAs in Arabidopsis
RT thaliana.";
RL J. Mol. Biol. 251:533-549(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION BY PHYTOCHROME A.
RX PubMed=11115889; DOI=10.1104/pp.124.4.1728;
RA Colon-Carmona A., Chen D.L., Yeh K.-C., Abel S.;
RT "Aux/IAA proteins are phosphorylated by phytochrome in vitro.";
RL Plant Physiol. 124:1728-1738(2000).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH TPL.
RX PubMed=18258861; DOI=10.1126/science.1151461;
RA Szemenyei H., Hannon M., Long J.A.;
RT "TOPLESS mediates auxin-dependent transcriptional repression during
RT Arabidopsis embryogenesis.";
RL Science 319:1384-1386(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 (By similarity). Interacts with
CC TPL. {ECO:0000250, ECO:0000269|PubMed:18258861}.
CC -!- INTERACTION:
CC Q38827; Q9FIK2: At5g47790; NbExp=3; IntAct=EBI-632216, EBI-25523851;
CC Q38827; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-632216, EBI-15192745;
CC Q38827; P49677: IAA1; NbExp=5; IntAct=EBI-632216, EBI-630505;
CC Q38827; Q38828: IAA10; NbExp=4; IntAct=EBI-632216, EBI-3946434;
CC Q38827; Q38831: IAA13; NbExp=4; IntAct=EBI-632216, EBI-1554143;
CC Q38827; A0A2H1ZEF6: IAA15; NbExp=3; IntAct=EBI-632216, EBI-25524519;
CC Q38827; O24407: IAA16; NbExp=4; IntAct=EBI-632216, EBI-632231;
CC Q38827; P93830: IAA17; NbExp=4; IntAct=EBI-632216, EBI-632243;
CC Q38827; O24409: IAA19; NbExp=4; IntAct=EBI-632216, EBI-632257;
CC Q38827; P49678: IAA2; NbExp=4; IntAct=EBI-632216, EBI-632343;
CC Q38827; O24410: IAA20; NbExp=3; IntAct=EBI-632216, EBI-632272;
CC Q38827; Q8LAL2: IAA26; NbExp=4; IntAct=EBI-632216, EBI-3947418;
CC Q38827; Q9ZSY8: IAA27; NbExp=4; IntAct=EBI-632216, EBI-3946677;
CC Q38827; Q9XFM0: IAA28; NbExp=4; IntAct=EBI-632216, EBI-3133404;
CC Q38827; Q38822: IAA3; NbExp=4; IntAct=EBI-632216, EBI-307174;
CC Q38827; Q8H174: IAA31; NbExp=3; IntAct=EBI-632216, EBI-3946408;
CC Q38827; Q9C5X0: IAA34; NbExp=4; IntAct=EBI-632216, EBI-3946459;
CC Q38827; P33077: IAA4; NbExp=4; IntAct=EBI-632216, EBI-632187;
CC Q38827; Q38824: IAA6; NbExp=3; IntAct=EBI-632216, EBI-1554124;
CC Q38827; Q38826: IAA8; NbExp=4; IntAct=EBI-632216, EBI-632200;
CC Q38827; O65154: KIWI; NbExp=3; IntAct=EBI-632216, EBI-2112286;
CC Q38827; Q9LSI4: MGH6.1; NbExp=3; IntAct=EBI-632216, EBI-15198743;
CC Q38827; O22179: MYB70; NbExp=3; IntAct=EBI-632216, EBI-1238013;
CC Q38827; O23160: MYB73; NbExp=3; IntAct=EBI-632216, EBI-25506855;
CC Q38827; Q84JP1: NFYA7; NbExp=3; IntAct=EBI-632216, EBI-4444640;
CC Q38827; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-632216, EBI-4424877;
CC Q38827; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-632216, EBI-4426144;
CC Q38827; Q9M1U4: TCP16; NbExp=3; IntAct=EBI-632216, EBI-15198627;
CC Q38827; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-632216, EBI-25522447;
CC Q38827; Q9LQW3: ZHD14; NbExp=4; IntAct=EBI-632216, EBI-1806701;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q38827-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in the whole plant.
CC {ECO:0000269|PubMed:7658471}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:7658471}.
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 -!- PTM: Phosphorylated by phytochrome A in vitro.
CC {ECO:0000269|PubMed:11115889}.
CC -!- SIMILARITY: Belongs to the Aux/IAA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10673.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U18411; AAC49050.1; -; mRNA.
DR EMBL; AB010075; BAB10673.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021684; CAA16692.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98084.1; -; Genomic_DNA.
DR EMBL; AF334715; AAG50093.1; -; mRNA.
DR EMBL; AY087089; AAM64650.1; -; mRNA.
DR PIR; T05902; T05902.
DR RefSeq; NP_851275.1; NM_180944.3. [Q38827-1]
DR AlphaFoldDB; Q38827; -.
DR SMR; Q38827; -.
DR BioGRID; 21935; 45.
DR ELM; Q38827; -.
DR IntAct; Q38827; 42.
DR STRING; 3702.AT5G65670.1; -.
DR PaxDb; Q38827; -.
DR PRIDE; Q38827; -.
DR ProteomicsDB; 232161; -. [Q38827-1]
DR EnsemblPlants; AT5G65670.1; AT5G65670.1; AT5G65670. [Q38827-1]
DR GeneID; 836693; -.
DR Gramene; AT5G65670.1; AT5G65670.1; AT5G65670. [Q38827-1]
DR KEGG; ath:AT5G65670; -.
DR Araport; AT5G65670; -.
DR TAIR; locus:2169955; AT5G65670.
DR eggNOG; ENOG502QUQJ; Eukaryota.
DR HOGENOM; CLU_049393_1_2_1; -.
DR InParanoid; Q38827; -.
DR OrthoDB; 1118150at2759; -.
DR PhylomeDB; Q38827; -.
DR PRO; PR:Q38827; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38827; baseline and differential.
DR Genevisible; Q38827; AT.
DR GO; GO:0005634; C:nucleus; ISS: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:0009734; P:auxin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; TAS: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 Alternative splicing; Auxin signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..338
FT /note="Auxin-responsive protein IAA9"
FT /id="PRO_0000112840"
FT DOMAIN 216..318
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 68..72
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 150..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 9
FT /note="S -> T (in Ref. 6; AAM64650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36405 MW; F13BE50C222F6B42 CRC64;
MSPEEELQSN VSVASSSPTS NCISRNTLGG LKEHNYLGLS DCSSVGSSTL SPLAEDDKAT
ISLKATELTL GLPGSQSPAR DTELNLLSPA KLDEKPFFPL LPSKDEICSS SQKNNASGNK
RGFSDTMDQF AEAKSSVYTE KNWMFPEAAA TQSVTKKDVP QNIPKGQSST TNNSSSPPAA
KAQIVGWPPV RSYRKNTLAT TCKNSDEVDG RPGSGALFVK VSMDGAPYLR KVDLRSYTNY
GELSSALEKM FTTFTLGQCG SNGAAGKDML SETKLKDLLN GKDYVLTYED KDGDWMLVGD
VPWEMFIDVC KKLKIMKGCD AIGLAAAPRA MEKSKMRA
