IAA31_ARATH
ID IAA31_ARATH Reviewed; 158 AA.
AC Q8H174; Q9LUN7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Auxin-responsive protein IAA31;
DE AltName: Full=Indoleacetic acid-induced protein 31;
GN Name=IAA31; OrderedLocusNames=At3g17600; ORFNames=MKP6.16;
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 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;
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 [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 Q8H174; Q9SKN5: ARF10; NbExp=3; IntAct=EBI-3946408, EBI-3947482;
CC Q8H174; Q93YR9: ARF16; NbExp=10; IntAct=EBI-3946408, EBI-3947588;
CC Q8H174; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-3946408, EBI-1100737;
CC Q8H174; Q9LST3: At5g60142; NbExp=3; IntAct=EBI-3946408, EBI-15192745;
CC Q8H174; O80902: CIPK22; NbExp=3; IntAct=EBI-3946408, EBI-4453230;
CC Q8H174; Q38828: IAA10; NbExp=8; IntAct=EBI-3946408, EBI-3946434;
CC Q8H174; Q38829: IAA11; NbExp=8; IntAct=EBI-3946408, EBI-2367923;
CC Q8H174; Q38830: IAA12; NbExp=8; IntAct=EBI-3946408, EBI-617608;
CC Q8H174; Q38831: IAA13; NbExp=9; IntAct=EBI-3946408, EBI-1554143;
CC Q8H174; Q38832: IAA14; NbExp=3; IntAct=EBI-3946408, EBI-2295562;
CC Q8H174; A0A2H1ZEF6: IAA15; NbExp=3; IntAct=EBI-3946408, EBI-25524519;
CC Q8H174; O24407: IAA16; NbExp=7; IntAct=EBI-3946408, EBI-632231;
CC Q8H174; P93830: IAA17; NbExp=8; IntAct=EBI-3946408, EBI-632243;
CC Q8H174; O24408: IAA18; NbExp=5; IntAct=EBI-3946408, EBI-2295525;
CC Q8H174; O24409: IAA19; NbExp=11; IntAct=EBI-3946408, EBI-632257;
CC Q8H174; O24410: IAA20; NbExp=5; IntAct=EBI-3946408, EBI-632272;
CC Q8H174; Q8LAL2: IAA26; NbExp=5; IntAct=EBI-3946408, EBI-3947418;
CC Q8H174; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-3946408, EBI-3946677;
CC Q8H174; Q9XFM0: IAA28; NbExp=8; IntAct=EBI-3946408, EBI-3133404;
CC Q8H174; Q38822: IAA3; NbExp=10; IntAct=EBI-3946408, EBI-307174;
CC Q8H174; Q8H174: IAA31; NbExp=4; IntAct=EBI-3946408, EBI-3946408;
CC Q8H174; Q8RYC6: IAA32; NbExp=3; IntAct=EBI-3946408, EBI-3946448;
CC Q8H174; Q9FKM7: IAA33; NbExp=6; IntAct=EBI-3946408, EBI-3946739;
CC Q8H174; Q9C5X0: IAA34; NbExp=8; IntAct=EBI-3946408, EBI-3946459;
CC Q8H174; P33077: IAA4; NbExp=3; IntAct=EBI-3946408, EBI-632187;
CC Q8H174; P33078: IAA5; NbExp=6; IntAct=EBI-3946408, EBI-3946487;
CC Q8H174; Q38824: IAA6; NbExp=9; IntAct=EBI-3946408, EBI-1554124;
CC Q8H174; Q38827: IAA9; NbExp=3; IntAct=EBI-3946408, EBI-632216;
CC Q8H174; O23160: MYB73; NbExp=3; IntAct=EBI-3946408, EBI-25506855;
CC Q8H174; Q9MAN1: NGA3; NbExp=3; IntAct=EBI-3946408, EBI-15216492;
CC Q8H174; Q9FGM1: PYL8; NbExp=3; IntAct=EBI-3946408, EBI-2429535;
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; AB022219; BAB02050.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75973.1; -; Genomic_DNA.
DR EMBL; AY054274; AAL06933.1; -; mRNA.
DR EMBL; BT000543; AAN18112.1; -; mRNA.
DR RefSeq; NP_188387.1; NM_112640.5.
DR AlphaFoldDB; Q8H174; -.
DR SMR; Q8H174; -.
DR BioGRID; 6359; 57.
DR IntAct; Q8H174; 46.
DR STRING; 3702.AT3G17600.1; -.
DR PaxDb; Q8H174; -.
DR PRIDE; Q8H174; -.
DR EnsemblPlants; AT3G17600.1; AT3G17600.1; AT3G17600.
DR GeneID; 821026; -.
DR Gramene; AT3G17600.1; AT3G17600.1; AT3G17600.
DR KEGG; ath:AT3G17600; -.
DR Araport; AT3G17600; -.
DR TAIR; locus:2090527; AT3G17600.
DR eggNOG; ENOG502S04C; Eukaryota.
DR HOGENOM; CLU_049393_3_1_1; -.
DR InParanoid; Q8H174; -.
DR OMA; MEVSNSC; -.
DR OrthoDB; 1436796at2759; -.
DR PhylomeDB; Q8H174; -.
DR PRO; PR:Q8H174; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H174; baseline and differential.
DR Genevisible; Q8H174; 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: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; TAS:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system 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..158
FT /note="Auxin-responsive protein IAA31"
FT /id="PRO_0000112857"
FT DOMAIN 72..157
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..33
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 153
FT /note="T -> P (in Ref. 3; AAN18112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18155 MW; CFE7F6AC0EA7F7D7 CRC64;
MEVSNSCSSF SSSSVDSTKP SPSESSVNLS LSLTFPSTSP QREARQDWPP IKSRLRDTLK
GRRLLRRGDD TSLFVKVYME GVPIGRKLDL CVFSGYESLL ENLSHMFDTS IICGNRDRKH
HVLTYEDKDG DWMMVGDIPW DMFLETVRRL KITRPERY
