IAA30_ARATH
ID IAA30_ARATH Reviewed; 172 AA.
AC Q9M1R4; Q2VW99;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Auxin-responsive protein IAA30;
DE AltName: Full=Indoleacetic acid-induced protein 30;
GN Name=IAA30; OrderedLocusNames=At3g62100; ORFNames=T17J13.60;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Yamada K., Chang C.H., Onodera C.S., Yu G., Theologis A.;
RT "Arabidopsis open reading frame (ORF) clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9M1R4; Q9SJN0: ABI5; NbExp=3; IntAct=EBI-3946710, EBI-1778690;
CC Q9M1R4; Q9LKL2: APRR1; NbExp=3; IntAct=EBI-3946710, EBI-618423;
CC Q9M1R4; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-3946710, EBI-1100737;
CC Q9M1R4; Q38825: IAA7; NbExp=4; IntAct=EBI-3946710, EBI-602959;
CC Q9M1R4; Q9SGU3: MYB72; NbExp=3; IntAct=EBI-3946710, EBI-1789562;
CC Q9M1R4; Q9SJA8: WRKY17; NbExp=3; IntAct=EBI-3946710, EBI-2365037;
CC Q9M1R4; O04336: WRKY21; NbExp=3; IntAct=EBI-3946710, EBI-1239118;
CC Q9M1R4; Q8H0Y8: WRKY41; NbExp=3; IntAct=EBI-3946710, EBI-15202502;
CC Q9M1R4; Q9STX0: WRKY7; NbExp=5; IntAct=EBI-3946710, EBI-2364652;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: By auxin. {ECO:0000250}.
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; AL138651; CAB71870.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80310.1; -; Genomic_DNA.
DR EMBL; AY669801; AAT67085.1; -; mRNA.
DR PIR; T48002; T48002.
DR RefSeq; NP_191769.1; NM_116075.3.
DR AlphaFoldDB; Q9M1R4; -.
DR SMR; Q9M1R4; -.
DR BioGRID; 10697; 37.
DR IntAct; Q9M1R4; 32.
DR STRING; 3702.AT3G62100.1; -.
DR PaxDb; Q9M1R4; -.
DR PRIDE; Q9M1R4; -.
DR EnsemblPlants; AT3G62100.1; AT3G62100.1; AT3G62100.
DR GeneID; 825383; -.
DR Gramene; AT3G62100.1; AT3G62100.1; AT3G62100.
DR KEGG; ath:AT3G62100; -.
DR Araport; AT3G62100; -.
DR TAIR; locus:2098023; AT3G62100.
DR eggNOG; ENOG502S04C; Eukaryota.
DR HOGENOM; CLU_049393_3_1_1; -.
DR InParanoid; Q9M1R4; -.
DR OMA; NSQVHAD; -.
DR OrthoDB; 1436796at2759; -.
DR PhylomeDB; Q9M1R4; -.
DR PRO; PR:Q9M1R4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1R4; baseline and differential.
DR Genevisible; Q9M1R4; 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010262; P:somatic embryogenesis; 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..172
FT /note="Auxin-responsive protein IAA30"
FT /id="PRO_0000112856"
FT DOMAIN 82..171
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..39
FT /note="EAR-like (transcriptional repression)"
SQ SEQUENCE 172 AA; 19238 MW; 44124F09674FF4B8 CRC64;
MGRGRSSSSS SIESSCKSNP FGVSSSNTRN LSTDLRLGLS FGSSSGQYYN GGDNHEYDGV
GAAEEMMIME EEEQNECNSV GSFYVKVNME GVPIGRKIDL LSLNGYHDLI TTLDYMFNAS
ILWAEEEDMC SEKSHVLTYA DKEGDWMMVG DVPWEMFLSS VRRLKISRAY HY
