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   16-JUN-2009, entry version 71.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=94105161; 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   MEDLINE=98121113; 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.,
RA   Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
RA   Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
RA   Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
RA   Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
RA   Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
RA   Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
RA   Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
RA   Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
RA   Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
RA   Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
RT   Arabidopsis thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   MEDLINE=95387393; 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
RT   Arabidopsis thaliana.";
RL   J. Mol. Biol. 251:533-549(1995).
RN   [6]
RP   DIMERIZATION.
RX   MEDLINE=98004476; 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   [7]
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   [8]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   MEDLINE=22031748; 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   [9]
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
RT   domain.";
RL   Plant Cell 16:533-543(2004).
CC   -!- FUNCTION: Aux/IAA proteins are short-lived transcriptional factors
CC       that function as repressor of early auxin response genes at low
CC       auxin concentrations. Repression is thought to result from the
CC       interaction with auxin response factors (ARFs), proteins that bind
CC       to the auxin-responsive promoter element (AuxRE). Formation of
CC       heterodimers with ARF proteins may alter their ability to modulate
CC       early auxin response genes expression.
CC   -!- SUBUNIT: Homo and heterodimers. Interacts with the auxin-
CC       responsive protein IAA2.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-630505, EBI-630505;
CC       P93024:ARF5; NbExp=2; IntAct=EBI-630505, EBI-629519;
CC       P93022:ARF7; NbExp=2; IntAct=EBI-630505, EBI-632284;
CC       P49679:IAA4/5 (xeno); NbExp=1; IntAct=EBI-630505, EBI-632357;
CC       Q570C0:TIR1; NbExp=1; IntAct=EBI-630505, EBI-307183;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in stems, leaves and
CC       flowers.
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
CC       is required for the correct degradation of the protein through the
CC       SCF-mediated ubiquitin-proteasome pathway. Interactions between
CC       Aux/IAA proteins and auxin response factors (ARFs) occur through
CC       their C-terminal dimerization domains III and IV.
CC   -!- PTM: Phosphorylated by phytochrome A in vitro.
CC   -!- SIMILARITY: Belongs to the Aux/IAA family.
CC   -!- SIMILARITY: Contains 1 Aux/IAA-ARF domain.
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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; AY133714; AAM91648.1; -; mRNA.
DR   IPI; IPI00539077; -.
DR   PIR; A71408; A71408.
DR   RefSeq; NP_193192.1; -.
DR   UniGene; At.43941; -.
DR   IntAct; P49677; 16.
DR   GeneID; 827103; -.
DR   GenomeReviews; CT486007_GR; AT4G14560.
DR   KEGG; ath:AT4G14560; -.
DR   GeneFarm; 3140; 342.
DR   TAIR; At4g14560; -.
DR   OMA; P49677; NNDSTEE.
DR   ArrayExpress; P49677; -.
DR   GermOnline; AT4G14560; Arabidopsis thaliana.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009734; P:auxin mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003311; AUX_IAA.
DR   InterPro; IPR011525; AuxIAA_ARF_dimer.
DR   Pfam; PF02309; AUX_IAA; 1.
DR   PROSITE; PS50962; IAA_ARF; 1.
PE   1: Evidence at protein level;
KW   Auxin signaling pathway; Complete proteome; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    168       Auxin-responsive protein IAA1.
FT                                /FTId=PRO_0000112832.
FT   DOMAIN       75    162       Aux/IAA-ARF.
FT   MOTIF        14     18       EAR-like (transcriptional repression).
FT   CONFLICT     52     52       A -> T (in Ref. 1; AAA16569).
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
//