IAA28_ARATH
ID IAA28_ARATH Reviewed; 175 AA.
AC Q9XFM0; Q9S9V6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Auxin-responsive protein IAA28;
DE AltName: Full=Indoleacetic acid-induced protein 28;
GN Name=IAA28; OrderedLocusNames=At5g25890; ORFNames=F18A17.6, T1N24.24;
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], AND MUTANT IAA28-1.
RC STRAIN=cv. Columbia;
RX PubMed=11251090; DOI=10.2307/3871400;
RA Rogg L.E., Lasswell J.E., Bartel B.;
RT "A gain-of-function mutation in IAA28 suppresses lateral root
RT development.";
RL Plant Cell 13:465-480(2001).
RN [2]
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 [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 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 [6]
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 [7]
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).
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 Q9XFM0; Q9C5W9: ARF18; NbExp=11; IntAct=EBI-3133404, EBI-3946783;
CC Q9XFM0; Q8RYC8: ARF19; NbExp=3; IntAct=EBI-3133404, EBI-529887;
CC Q9XFM0; Q9ZTX8: ARF6; NbExp=3; IntAct=EBI-3133404, EBI-3946770;
CC Q9XFM0; Q9XED8: ARF9; NbExp=3; IntAct=EBI-3133404, EBI-3946762;
CC Q9XFM0; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-3133404, EBI-1100737;
CC Q9XFM0; Q9FWS3: CG1; NbExp=3; IntAct=EBI-3133404, EBI-25527280;
CC Q9XFM0; Q9FN91: EXO70H7; NbExp=3; IntAct=EBI-3133404, EBI-25516131;
CC Q9XFM0; Q39103: GA3OX1; NbExp=5; IntAct=EBI-3133404, EBI-4426378;
CC Q9XFM0; Q8H7F6: GRXS16; NbExp=3; IntAct=EBI-3133404, EBI-4424482;
CC Q9XFM0; P49677: IAA1; NbExp=12; IntAct=EBI-3133404, EBI-630505;
CC Q9XFM0; Q38828: IAA10; NbExp=10; IntAct=EBI-3133404, EBI-3946434;
CC Q9XFM0; Q38829: IAA11; NbExp=9; IntAct=EBI-3133404, EBI-2367923;
CC Q9XFM0; Q38830: IAA12; NbExp=6; IntAct=EBI-3133404, EBI-617608;
CC Q9XFM0; Q38831: IAA13; NbExp=8; IntAct=EBI-3133404, EBI-1554143;
CC Q9XFM0; Q38832: IAA14; NbExp=4; IntAct=EBI-3133404, EBI-2295562;
CC Q9XFM0; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-3133404, EBI-25524519;
CC Q9XFM0; O24407: IAA16; NbExp=10; IntAct=EBI-3133404, EBI-632231;
CC Q9XFM0; P93830: IAA17; NbExp=9; IntAct=EBI-3133404, EBI-632243;
CC Q9XFM0; O24408: IAA18; NbExp=7; IntAct=EBI-3133404, EBI-2295525;
CC Q9XFM0; O24409: IAA19; NbExp=9; IntAct=EBI-3133404, EBI-632257;
CC Q9XFM0; P49678: IAA2; NbExp=10; IntAct=EBI-3133404, EBI-632343;
CC Q9XFM0; O24410: IAA20; NbExp=6; IntAct=EBI-3133404, EBI-632272;
CC Q9XFM0; Q8LAL2: IAA26; NbExp=8; IntAct=EBI-3133404, EBI-3947418;
CC Q9XFM0; Q9ZSY8: IAA27; NbExp=8; IntAct=EBI-3133404, EBI-3946677;
CC Q9XFM0; Q9XFM0: IAA28; NbExp=4; IntAct=EBI-3133404, EBI-3133404;
CC Q9XFM0; Q93WC4: IAA29; NbExp=5; IntAct=EBI-3133404, EBI-3946697;
CC Q9XFM0; Q38822: IAA3; NbExp=10; IntAct=EBI-3133404, EBI-307174;
CC Q9XFM0; Q8H174: IAA31; NbExp=8; IntAct=EBI-3133404, EBI-3946408;
CC Q9XFM0; Q8RYC6: IAA32; NbExp=5; IntAct=EBI-3133404, EBI-3946448;
CC Q9XFM0; Q9FKM7: IAA33; NbExp=7; IntAct=EBI-3133404, EBI-3946739;
CC Q9XFM0; Q9C5X0: IAA34; NbExp=8; IntAct=EBI-3133404, EBI-3946459;
CC Q9XFM0; P33077: IAA4; NbExp=9; IntAct=EBI-3133404, EBI-632187;
CC Q9XFM0; P33078: IAA5; NbExp=6; IntAct=EBI-3133404, EBI-3946487;
CC Q9XFM0; Q38824: IAA6; NbExp=9; IntAct=EBI-3133404, EBI-1554124;
CC Q9XFM0; Q38825: IAA7; NbExp=11; IntAct=EBI-3133404, EBI-602959;
CC Q9XFM0; Q38826: IAA8; NbExp=8; IntAct=EBI-3133404, EBI-632200;
CC Q9XFM0; Q38827: IAA9; NbExp=4; IntAct=EBI-3133404, EBI-632216;
CC Q9XFM0; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-3133404, EBI-25522447;
CC Q9XFM0; Q9FEE2: TON2; NbExp=3; IntAct=EBI-3133404, EBI-4452426;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In roots and inflorescence stems.
CC -!- INDUCTION: Not induced 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF149816; AAD34019.1; -; mRNA.
DR EMBL; AC005405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF149413; AAD40120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93498.1; -; Genomic_DNA.
DR EMBL; BT000427; AAN17404.1; -; mRNA.
DR EMBL; BT002175; AAN72186.1; -; mRNA.
DR PIR; T52143; T52143.
DR RefSeq; NP_568478.1; NM_122490.4.
DR AlphaFoldDB; Q9XFM0; -.
DR SMR; Q9XFM0; -.
DR BioGRID; 17933; 58.
DR ELM; Q9XFM0; -.
DR IntAct; Q9XFM0; 55.
DR STRING; 3702.AT5G25890.1; -.
DR PaxDb; Q9XFM0; -.
DR PRIDE; Q9XFM0; -.
DR EnsemblPlants; AT5G25890.1; AT5G25890.1; AT5G25890.
DR GeneID; 832658; -.
DR Gramene; AT5G25890.1; AT5G25890.1; AT5G25890.
DR KEGG; ath:AT5G25890; -.
DR Araport; AT5G25890; -.
DR TAIR; locus:2180557; AT5G25890.
DR eggNOG; ENOG502R4CB; Eukaryota.
DR HOGENOM; CLU_049393_2_2_1; -.
DR InParanoid; Q9XFM0; -.
DR OMA; FSKKDSW; -.
DR OrthoDB; 1365348at2759; -.
DR PhylomeDB; Q9XFM0; -.
DR PRO; PR:Q9XFM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFM0; baseline and differential.
DR Genevisible; Q9XFM0; 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:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; 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; 2.
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..175
FT /note="Auxin-responsive protein IAA28"
FT /id="PRO_0000112854"
FT DOMAIN 80..161
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..11
FT /note="EAR-like (transcriptional repression)"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53
FT /note="P->L: In iaa28-1; gain of function. Affects auxin-
FT related developmental processes."
SQ SEQUENCE 175 AA; 20206 MW; 7A58B615DBC8FB47 CRC64;
MEEEKRLELR LAPPCHQFTS NNNINGSKQK SSTKETSFLS NNRVEVAPVV GWPPVRSSRR
NLTAQLKEEM KKKESDEEKE LYVKINMEGV PIGRKVNLSA YNNYQQLSHA VDQLFSKKDS
WDLNRQYTLV YEDTEGDKVL VGDVPWEMFV STVKRLHVLK TSHAFSLSPR KHGKE
