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Protein

Auxin-responsive protein IAA1

Gene

IAA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Aux/IAA proteins are short-lived transcriptional factors that function as repressors 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.1 Publication

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. sequence-specific DNA binding transcription factor activity Source: TAIR
  3. transcription regulatory region DNA binding Source: TAIR

GO - Biological processi

  1. auxin-activated signaling pathway Source: UniProtKB-KW
  2. response to auxin Source: TAIR
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Auxin signaling pathway, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Auxin-responsive protein IAA1
Alternative name(s):
Indoleacetic acid-induced protein 1
Gene namesi
Name:IAA1
Ordered Locus Names:At4g14560
ORF Names:dl3320w, FCAALL.409
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G14560.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Auxin-responsive protein IAA1PRO_0000112832Add
BLAST

Post-translational modificationi

Phosphorylated by phytochrome A in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP49677.

Expressioni

Tissue specificityi

Preferentially expressed in stems, leaves and flowers.1 Publication

Inductioni

By auxin.1 Publication

Gene expression databases

ExpressionAtlasiP49677. baseline and differential.
GenevestigatoriP49677.

Interactioni

Subunit structurei

Homodimers and heterodimers. Interacts with the auxin-responsive protein IAA2. Interacts with TPL.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-630505,EBI-630505
ARF5P930244EBI-630505,EBI-629519
ARF7P930223EBI-630505,EBI-632284
IAA16O244073EBI-630505,EBI-632231
IAA18O244083EBI-630505,EBI-2295525
IAA2P496783EBI-630505,EBI-632343
IAA3Q388223EBI-630505,EBI-307174
IAA4/5P496793EBI-630505,EBI-632357From a different organism.

Protein-protein interaction databases

BioGridi12400. 12 interactions.
DIPiDIP-34629N.
IntActiP49677. 32 interactions.

Structurei

3D structure databases

ProteinModelPortaliP49677.
SMRiP49677. Positions 76-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 16188PB1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 185EAR-like (transcriptional repression)

Domaini

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.

Sequence similaritiesi

Belongs to the Aux/IAA family.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG329801.
HOGENOMiHOG000238261.
InParanoidiP49677.
KOiK14484.
OMAiQPKKAED.
PhylomeDBiP49677.

Family and domain databases

InterProiIPR003311. AUX_IAA.
IPR011525. AuxIAA_ARF_dimer.
[Graphical view]
PfamiPF02309. AUX_IAA. 1 hit.
[Graphical view]
PROSITEiPS51745. PB1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVTNGLNLK DTELRLGLPG AQEEQQLELS CVRSNNKRKN NDSTEESAPP
60 70 80 90 100
PAKTQIVGWP PVRSNRKNNN NKNVSYVKVS MDGAPYLRKI DLKMYKNYPE
110 120 130 140 150
LLKALENMFK FTVGEYSERE GYKGSGFVPT YEDKDGDWML VGDVPWDMFS
160
SSCQKLRIMK GSEAPTAL
Length:168
Mass (Da):19,032
Last modified:November 30, 2000 - v2
Checksum:i17CA9B3BEB7962EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521A → T in AAA16569 (PubMed:8278386).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15448 mRNA. Translation: AAA16569.1.
Z97336 Genomic DNA. Translation: CAB10235.1.
AL161539 Genomic DNA. Translation: CAB78498.1.
CP002687 Genomic DNA. Translation: AEE83460.1.
AY133714 mRNA. Translation: AAM91648.1.
PIRiA71408.
RefSeqiNP_193192.1. NM_117536.3.
UniGeneiAt.43941.

Genome annotation databases

EnsemblPlantsiAT4G14560.1; AT4G14560.1; AT4G14560.
GeneIDi827103.
KEGGiath:AT4G14560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15448 mRNA. Translation: AAA16569.1.
Z97336 Genomic DNA. Translation: CAB10235.1.
AL161539 Genomic DNA. Translation: CAB78498.1.
CP002687 Genomic DNA. Translation: AEE83460.1.
AY133714 mRNA. Translation: AAM91648.1.
PIRiA71408.
RefSeqiNP_193192.1. NM_117536.3.
UniGeneiAt.43941.

3D structure databases

ProteinModelPortaliP49677.
SMRiP49677. Positions 76-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12400. 12 interactions.
DIPiDIP-34629N.
IntActiP49677. 32 interactions.

Proteomic databases

PRIDEiP49677.

Protocols and materials databases

DNASUi827103.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G14560.1; AT4G14560.1; AT4G14560.
GeneIDi827103.
KEGGiath:AT4G14560.

Organism-specific databases

GeneFarmi3140. 342.
TAIRiAT4G14560.

Phylogenomic databases

eggNOGiNOG329801.
HOGENOMiHOG000238261.
InParanoidiP49677.
KOiK14484.
OMAiQPKKAED.
PhylomeDBiP49677.

Gene expression databases

ExpressionAtlasiP49677. baseline and differential.
GenevestigatoriP49677.

Family and domain databases

InterProiIPR003311. AUX_IAA.
IPR011525. AuxIAA_ARF_dimer.
[Graphical view]
PfamiPF02309. AUX_IAA. 1 hit.
[Graphical view]
PROSITEiPS51745. PB1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Early auxin-induced genes encode short-lived nuclear proteins."
    Abel S., Oeller P.W., Theologis A.
    Proc. Natl. Acad. Sci. U.S.A. 91:326-330(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    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.
    Nature 391:485-488(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The PS-IAA4/5-like family of early auxin-inducible mRNAs in Arabidopsis thaliana."
    Abel S., Nguyen M.D., Theologis A.
    J. Mol. Biol. 251:533-549(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  7. "Protein-protein interactions among the Aux/IAA proteins."
    Kim J., Harter K., Theologis A.
    Proc. Natl. Acad. Sci. U.S.A. 94:11786-11791(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMERIZATION.
  8. "Aux/IAA proteins are phosphorylated by phytochrome in vitro."
    Colon-Carmona A., Chen D.L., Yeh K.-C., Abel S.
    Plant Physiol. 124:1728-1738(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PHYTOCHROME A.
  9. "Genetics of Aux/IAA and ARF action in plant growth and development."
    Liscum E., Reed J.W.
    Plant Mol. Biol. 49:387-400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, FUNCTION.
  10. "Aux/IAA proteins contain a potent transcriptional repression domain."
    Tiwari S.B., Hagen G., Guilfoyle T.J.
    Plant Cell 16:533-543(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REPRESSION DOMAIN.
  11. "TOPLESS mediates auxin-dependent transcriptional repression during Arabidopsis embryogenesis."
    Szemenyei H., Hannon M., Long J.A.
    Science 319:1384-1386(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPL.

Entry informationi

Entry nameiIAA1_ARATH
AccessioniPrimary (citable) accession number: P49677
Secondary accession number(s): O23312
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: November 30, 2000
Last modified: March 31, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.