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UniProtKB/Swiss-Prot entry P49677


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IAA1_ARATH
Primary accession number P49677
Secondary accession number O23312
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 68)
Name and origin of the protein
Protein name Auxin-responsive protein IAA1
Synonym Indoleacetic acid-induced protein 1
Gene name
Name: IAA1
OrderedLocusNames: At4g14560
ORFNames: dl3320w, FCAALL.409
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=8278386 [NCBI, ExPASy, EBI, Israel, Japan]
Abel S., Oeller P.W., Theologis A.;
"Early auxin-induced genes encode short-lived nuclear proteins.";
Proc. Natl. Acad. Sci. U.S.A. 91:326-330(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35140; PubMed=9461215 [NCBI, ExPASy, EBI, Israel, Japan]
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1006/jmbi.1995.0454; PubMed=7658471 [NCBI, ExPASy, EBI, Israel, Japan]
Abel S., Nguyen M.D., Theologis A.;
"The PS-IAA4/5-like family of early auxin-inducible mRNAs in Arabidopsis thaliana.";
J. Mol. Biol. 251:533-549(1995).
[6]
DIMERIZATION.
DOI=10.1073/pnas.94.22.11786; PubMed=9342315 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J., Harter K., Theologis A.;
"Protein-protein interactions among the Aux/IAA proteins.";
Proc. Natl. Acad. Sci. U.S.A. 94:11786-11791(1997).
[7]
PHOSPHORYLATION BY PHYTOCHROME A.
DOI=10.1104/pp.124.4.1728; PubMed=11115889 [NCBI, ExPASy, EBI, Israel, Japan]
Colon-Carmona A., Chen D.L., Yeh K.-C., Abel S.;
"Aux/IAA proteins are phosphorylated by phytochrome in vitro.";
Plant Physiol. 124:1728-1738(2000).
[8]
GENE FAMILY, NOMENCLATURE, AND FUNCTION.
DOI=10.1023/A:1015255030047; PubMed=12036262 [NCBI, ExPASy, EBI, Israel, Japan]
Liscum E., Reed J.W.;
"Genetics of Aux/IAA and ARF action in plant growth and development.";
Plant Mol. Biol. 49:387-400(2002).
[9]
TRANSCRIPTIONAL REPRESSION DOMAIN.
DOI=10.1105/tpc.017384; PubMed=14742873 [NCBI, ExPASy, EBI, Israel, Japan]
Tiwari S.B., Hagen G., Guilfoyle T.J.;
"Aux/IAA proteins contain a potent transcriptional repression domain.";
Plant Cell 16:533-543(2004).
Comments
  • FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressor of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
  • SUBUNIT: Homo and heterodimers. Interacts with the auxin-responsive protein IAA2.
  • INTERACTION:
    Self; NbExp=2; IntAct=EBI-630505, EBI-630505;
    P93024:ARF5; NbExp=2; IntAct=EBI-630505, EBI-629519;
    P93022:ARF7; NbExp=2; IntAct=EBI-630505, EBI-632284;
    P49679:IAA4/5 (xeno); NbExp=1; IntAct=EBI-630505, EBI-632357;
    Q570C0:TIR1; NbExp=1; IntAct=EBI-630505, EBI-307183;
  • SUBCELLULAR LOCATION: Nucleus.
  • TISSUE SPECIFICITY: Preferentially expressed in stems, leaves and flowers.
  • INDUCTION: By auxin.
  • DOMAIN: The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
  • PTM: Phosphorylated by phytochrome A in vitro.
  • SIMILARITY: Belongs to the Aux/IAA family.
  • SIMILARITY: Contains 1 Aux/IAA-ARF domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L15448; AAA16569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97336; CAB10235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161539; CAB78498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY133714; AAM91648.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A71408; A71408.
RefSeq NP_193192.1; -.
UniGene At.43941
3D structure databases
ModBase P49677.
Protein-protein interaction databases
IntAct P49677; 16.
Organism-specific databases
GeneFarm 3140; 342.
TAIR At4g14560; -.
Gene expression databases
ArrayExpress P49677; -.
GermOnline AT4G14560; Arabidopsis thaliana.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0009734; Biological process: auxin mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003311; AUX_IAA.
IPR011525; AuxIAA_ARF_dimer.
Graphical view of domain structure.
Pfam PF02309; AUX_IAA; 1.
Pfam graphical view of domain structure.
PROSITE PS50962; IAA_ARF; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 827103; -.
GenomeReviews CT486007_GR; AT4G14560.
KEGG ath:AT4G14560; -.
Other
LinkHub P49677; -.
ProtoNet P49677.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Auxin signaling pathway; Complete proteome; Nucleus; Phosphoprotein; Repressor; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   168  168     Auxin-responsive protein IAA1. PRO_0000112832
DOMAIN   75   162  88     Aux/IAA-ARF. 
MOTIF   14    18  5     EAR-like (transcriptional repression). 
CONFLICT   52    52        A -> T (in Ref. 1; AAA16569). 
Sequence information
Length: 168 AA [This is the length of the unprocessed precursor] Molecular weight: 19032 Da [This is the MW of the unprocessed precursor] CRC64: 17CA9B3BEB7962EE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEVTNGLNLK DTELRLGLPG AQEEQQLELS CVRSNNKRKN NDSTEESAPP PAKTQIVGWP 

        70         80         90        100        110        120 
PVRSNRKNNN NKNVSYVKVS MDGAPYLRKI DLKMYKNYPE LLKALENMFK FTVGEYSERE 

       130        140        150        160 
GYKGSGFVPT YEDKDGDWML VGDVPWDMFS SSCQKLRIMK GSEAPTAL 

P49677 in FASTA format

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