IAA16_ARATH
ID IAA16_ARATH Reviewed; 236 AA.
AC O24407;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Auxin-responsive protein IAA16;
DE AltName: Full=Indoleacetic acid-induced protein 16;
GN Name=IAA16; OrderedLocusNames=At3g04730; ORFNames=F7O18.22;
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].
RC STRAIN=cv. Columbia;
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 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].
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 [5]
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 [6]
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 [7]
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 O24407; Q9C5W9: ARF18; NbExp=5; IntAct=EBI-632231, EBI-3946783;
CC O24407; Q8RYC8: ARF19; NbExp=6; IntAct=EBI-632231, EBI-529887;
CC O24407; Q9ZUM0: At2g02160; NbExp=3; IntAct=EBI-632231, EBI-15206592;
CC O24407; P49677: IAA1; NbExp=11; IntAct=EBI-632231, EBI-630505;
CC O24407; Q38828: IAA10; NbExp=11; IntAct=EBI-632231, EBI-3946434;
CC O24407; Q38829: IAA11; NbExp=8; IntAct=EBI-632231, EBI-2367923;
CC O24407; Q38830: IAA12; NbExp=8; IntAct=EBI-632231, EBI-617608;
CC O24407; Q38831: IAA13; NbExp=9; IntAct=EBI-632231, EBI-1554143;
CC O24407; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-632231, EBI-25524519;
CC O24407; O24407: IAA16; NbExp=4; IntAct=EBI-632231, EBI-632231;
CC O24407; P93830: IAA17; NbExp=8; IntAct=EBI-632231, EBI-632243;
CC O24407; O24408: IAA18; NbExp=4; IntAct=EBI-632231, EBI-2295525;
CC O24407; O24409: IAA19; NbExp=11; IntAct=EBI-632231, EBI-632257;
CC O24407; P49678: IAA2; NbExp=10; IntAct=EBI-632231, EBI-632343;
CC O24407; O24410: IAA20; NbExp=5; IntAct=EBI-632231, EBI-632272;
CC O24407; Q8LAL2: IAA26; NbExp=9; IntAct=EBI-632231, EBI-3947418;
CC O24407; Q9ZSY8: IAA27; NbExp=9; IntAct=EBI-632231, EBI-3946677;
CC O24407; Q9XFM0: IAA28; NbExp=10; IntAct=EBI-632231, EBI-3133404;
CC O24407; Q38822: IAA3; NbExp=12; IntAct=EBI-632231, EBI-307174;
CC O24407; Q8H174: IAA31; NbExp=7; IntAct=EBI-632231, EBI-3946408;
CC O24407; Q9FKM7: IAA33; NbExp=3; IntAct=EBI-632231, EBI-3946739;
CC O24407; Q9C5X0: IAA34; NbExp=6; IntAct=EBI-632231, EBI-3946459;
CC O24407; P33077: IAA4; NbExp=9; IntAct=EBI-632231, EBI-632187;
CC O24407; P33078: IAA5; NbExp=7; IntAct=EBI-632231, EBI-3946487;
CC O24407; Q38824: IAA6; NbExp=8; IntAct=EBI-632231, EBI-1554124;
CC O24407; Q38825: IAA7; NbExp=3; IntAct=EBI-632231, EBI-602959;
CC O24407; Q38826: IAA8; NbExp=7; IntAct=EBI-632231, EBI-632200;
CC O24407; Q38827: IAA9; NbExp=4; IntAct=EBI-632231, EBI-632216;
CC O24407; Q9LSI4: MGH6.1; NbExp=3; IntAct=EBI-632231, EBI-15198743;
CC O24407; Q9LTC4: MYB15; NbExp=3; IntAct=EBI-632231, EBI-21497119;
CC O24407; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-632231, EBI-963647;
CC O24407; Q9FUA4: SPT; NbExp=3; IntAct=EBI-632231, EBI-1536703;
CC O24407; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-632231, EBI-4426168;
CC O24407; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-632231, EBI-25522447;
CC O24407; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-632231, EBI-4426557;
CC O24407; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-632231, EBI-4424568;
CC O24407; O64722: ZHD3; NbExp=3; IntAct=EBI-632231, EBI-1806244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: By auxin.
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; U49072; AAB84353.1; -; mRNA.
DR EMBL; AC011437; AAF04899.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74127.1; -; Genomic_DNA.
DR EMBL; AF332400; AAG48764.1; -; mRNA.
DR EMBL; AF375420; AAK53004.1; -; mRNA.
DR EMBL; BT000857; AAN38694.1; -; mRNA.
DR EMBL; AY087195; AAM64751.1; -; mRNA.
DR RefSeq; NP_187124.1; NM_111345.3.
DR AlphaFoldDB; O24407; -.
DR SMR; O24407; -.
DR BioGRID; 4968; 54.
DR ELM; O24407; -.
DR IntAct; O24407; 62.
DR STRING; 3702.AT3G04730.1; -.
DR iPTMnet; O24407; -.
DR PaxDb; O24407; -.
DR PRIDE; O24407; -.
DR ProteomicsDB; 232188; -.
DR DNASU; 819633; -.
DR EnsemblPlants; AT3G04730.1; AT3G04730.1; AT3G04730.
DR GeneID; 819633; -.
DR Gramene; AT3G04730.1; AT3G04730.1; AT3G04730.
DR KEGG; ath:AT3G04730; -.
DR Araport; AT3G04730; -.
DR TAIR; locus:2084933; AT3G04730.
DR eggNOG; ENOG502QPNB; Eukaryota.
DR HOGENOM; CLU_049393_1_5_1; -.
DR InParanoid; O24407; -.
DR OMA; IGNYGPQ; -.
DR OrthoDB; 1203639at2759; -.
DR PhylomeDB; O24407; -.
DR PRO; PR:O24407; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O24407; baseline and differential.
DR Genevisible; O24407; 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: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 Auxin signaling pathway; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..236
FT /note="Auxin-responsive protein IAA16"
FT /id="PRO_0000112847"
FT DOMAIN 118..218
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 82..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..13
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 84..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 236 AA; 25659 MW; 3575B0C2A0AB595E CRC64;
MINFEATELR LGLPGGNHGG EMAGKNNGKR GFSETVDLKL NLSSTAMDSV SKVDLENMKE
KVVKPPAKAQ VVGWPPVRSF RKNVMSGQKP TTGDATEGND KTSGSSGATS SASACATVAY
VKVSMDGAPY LRKIDLKLYK TYQDLSNALS KMFSSFTIGN YGPQGMKDFM NESKLIDLLN
GSDYVPTYED KDGDWMLVGD VPWEMFVDSC KRIRIMKGSE AIGLAPRALE KCKNRS
