ID   IAA1_ARATH              Reviewed;         168 AA.
AC   P49677; O23312;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Auxin-responsive protein IAA1;
DE   AltName: Full=Indoleacetic acid-induced protein 1;
GN   Name=IAA1; OrderedLocusNames=At4g14560; ORFNames=dl3320w, FCAALL.409;
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=8278386; DOI=10.1073/pnas.91.1.326;
RA   Abel S., Oeller P.W., Theologis A.;
RT   "Early auxin-induced genes encode short-lived nuclear proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:326-330(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   TISSUE SPECIFICITY, AND INDUCTION.
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   [7]
RP   DIMERIZATION.
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   [8]
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   [9]
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   [10]
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   [11]
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. Interacts with the auxin-
CC       responsive protein IAA2. Interacts with TPL.
CC       {ECO:0000269|PubMed:18258861}.
CC   -!- INTERACTION:
CC       P49677; Q8RYC8: ARF19; NbExp=4; IntAct=EBI-630505, EBI-529887;
CC       P49677; P93024: ARF5; NbExp=4; IntAct=EBI-630505, EBI-629519;
CC       P49677; P93022: ARF7; NbExp=4; IntAct=EBI-630505, EBI-632284;
CC       P49677; O80533: At1g09500; NbExp=3; IntAct=EBI-630505, EBI-4447439;
CC       P49677; P49677: IAA1; NbExp=10; IntAct=EBI-630505, EBI-630505;
CC       P49677; Q38828: IAA10; NbExp=10; IntAct=EBI-630505, EBI-3946434;
CC       P49677; Q38829: IAA11; NbExp=5; IntAct=EBI-630505, EBI-2367923;
CC       P49677; Q38830: IAA12; NbExp=5; IntAct=EBI-630505, EBI-617608;
CC       P49677; Q38831: IAA13; NbExp=8; IntAct=EBI-630505, EBI-1554143;
CC       P49677; Q38832: IAA14; NbExp=3; IntAct=EBI-630505, EBI-2295562;
CC       P49677; A0A2H1ZEF6: IAA15; NbExp=5; IntAct=EBI-630505, EBI-25524519;
CC       P49677; O24407: IAA16; NbExp=11; IntAct=EBI-630505, EBI-632231;
CC       P49677; P93830: IAA17; NbExp=11; IntAct=EBI-630505, EBI-632243;
CC       P49677; O24408: IAA18; NbExp=6; IntAct=EBI-630505, EBI-2295525;
CC       P49677; O24409: IAA19; NbExp=12; IntAct=EBI-630505, EBI-632257;
CC       P49677; P49678: IAA2; NbExp=13; IntAct=EBI-630505, EBI-632343;
CC       P49677; O24410: IAA20; NbExp=6; IntAct=EBI-630505, EBI-632272;
CC       P49677; Q8LAL2: IAA26; NbExp=14; IntAct=EBI-630505, EBI-3947418;
CC       P49677; Q9ZSY8: IAA27; NbExp=10; IntAct=EBI-630505, EBI-3946677;
CC       P49677; Q9XFM0: IAA28; NbExp=12; IntAct=EBI-630505, EBI-3133404;
CC       P49677; Q38822: IAA3; NbExp=13; IntAct=EBI-630505, EBI-307174;
CC       P49677; Q8RYC6: IAA32; NbExp=3; IntAct=EBI-630505, EBI-3946448;
CC       P49677; Q9C5X0: IAA34; NbExp=6; IntAct=EBI-630505, EBI-3946459;
CC       P49677; P33077: IAA4; NbExp=10; IntAct=EBI-630505, EBI-632187;
CC       P49677; P33078: IAA5; NbExp=6; IntAct=EBI-630505, EBI-3946487;
CC       P49677; Q38824: IAA6; NbExp=9; IntAct=EBI-630505, EBI-1554124;
CC       P49677; Q38825: IAA7; NbExp=3; IntAct=EBI-630505, EBI-602959;
CC       P49677; Q38826: IAA8; NbExp=7; IntAct=EBI-630505, EBI-632200;
CC       P49677; Q38827: IAA9; NbExp=5; IntAct=EBI-630505, EBI-632216;
CC       P49677; Q9LV27: LST8-1; NbExp=4; IntAct=EBI-630505, EBI-4453099;
CC       P49677; O22179: MYB70; NbExp=3; IntAct=EBI-630505, EBI-1238013;
CC       P49677; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-630505, EBI-4426144;
CC       P49677; P49679: IAA4/5; Xeno; NbExp=3; IntAct=EBI-630505, EBI-632357;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in stems, leaves and
CC       flowers. {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}.
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DR   EMBL; L15448; AAA16569.1; -; mRNA.
DR   EMBL; Z97336; CAB10235.1; -; Genomic_DNA.
DR   EMBL; AL161539; CAB78498.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83460.1; -; Genomic_DNA.
DR   EMBL; AY133714; AAM91648.1; -; mRNA.
DR   PIR; A71408; A71408.
DR   RefSeq; NP_193192.1; NM_117536.4.
DR   PDB; 5C7F; X-ray; 2.70 A; E/F/G/H=10-20.
DR   PDBsum; 5C7F; -.
DR   AlphaFoldDB; P49677; -.
DR   SMR; P49677; -.
DR   BioGRID; 12400; 54.
DR   DIP; DIP-34629N; -.
DR   ELM; P49677; -.
DR   IntAct; P49677; 47.
DR   STRING; 3702.P49677; -.
DR   PaxDb; 3702-AT4G14560-1; -.
DR   ProteomicsDB; 232220; -.
DR   DNASU; 827103; -.
DR   EnsemblPlants; AT4G14560.1; AT4G14560.1; AT4G14560.
DR   GeneID; 827103; -.
DR   Gramene; AT4G14560.1; AT4G14560.1; AT4G14560.
DR   KEGG; ath:AT4G14560; -.
DR   Araport; AT4G14560; -.
DR   TAIR; AT4G14560; IAA1.
DR   eggNOG; ENOG502QU81; Eukaryota.
DR   HOGENOM; CLU_049393_0_1_1; -.
DR   InParanoid; P49677; -.
DR   OMA; MFASSCK; -.
DR   OrthoDB; 661114at2759; -.
DR   PhylomeDB; P49677; -.
DR   PRO; PR:P49677; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P49677; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IEP:TAIR.
DR   InterPro; IPR033389; AUX/IAA_dom.
DR   InterPro; IPR003311; AUX_IAA.
DR   InterPro; IPR000270; PB1_dom.
DR   PANTHER; PTHR31734:SF282; AUXIN-RESPONSIVE PROTEIN IAA1; 1.
DR   PANTHER; PTHR31734; AUXIN-RESPONSIVE PROTEIN IAA17; 1.
DR   Pfam; PF02309; AUX_IAA; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   Genevisible; P49677; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Auxin signaling pathway; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..168
FT                   /note="Auxin-responsive protein IAA1"
FT                   /id="PRO_0000112832"
FT   DOMAIN          74..161
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           14..18
FT                   /note="EAR-like (transcriptional repression)"
FT   CONFLICT        52
FT                   /note="A -> T (in Ref. 1; AAA16569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   168 AA;  19032 MW;  17CA9B3BEB7962EE CRC64;
     MEVTNGLNLK DTELRLGLPG AQEEQQLELS CVRSNNKRKN NDSTEESAPP PAKTQIVGWP
     PVRSNRKNNN NKNVSYVKVS MDGAPYLRKI DLKMYKNYPE LLKALENMFK FTVGEYSERE
     GYKGSGFVPT YEDKDGDWML VGDVPWDMFS SSCQKLRIMK GSEAPTAL
//