Reviewed, UniProtKB/Swiss-Prot P49677 (IAA1_ARATH)

Names and origin

Protein names

Recommended name:
    Auxin-responsive protein IAA1
Alternative name(s):
    Indoleacetic acid-induced protein 1

Gene names

Name:	IAA1
Ordered Locus Names:	At4g14560
ORF Names:	dl3320w, FCAALL.409

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Homo and heterodimers. Interacts with the auxin-responsive protein IAA2.
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.
Post-translational modification	Phosphorylated by phytochrome A in vitro.
Sequence similarities	Belongs to the Aux/IAA family. Contains 1 Aux/IAA-ARF domain.

Ontologies

Keywords
Biological process	Auxin signaling pathway Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	auxin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: InterPro
Molecular function	identical protein binding Ref.6 Inferred from physical interaction. Source: IntAct protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-630505,EBI-630505
ARF5	P93024	2	EBI-630505,EBI-629519
ARF7	P93022	2	EBI-630505,EBI-632284
IAA4/5	P49679	1	EBI-630505,EBI-632357	From a different organism.
TIR1	Q570C0	1	EBI-630505,EBI-307183

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 168	168	Auxin-responsive protein IAA1		PRO_0000112832
Regions
	Domain	75 – 162	88	Aux/IAA-ARF
	Motif	14 – 18	5	EAR-like (transcriptional repression)
Experimental info
	Sequence conflict	52	1	A → T in AAA16569. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49677-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 17CA9B3BEB7962EE	FASTA	168	19,032
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1994) [PubMed: 8278386] [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(1998) [PubMed: 9461215] [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(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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(1995) [PubMed: 7658471] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]	"Protein-protein interactions among the Aux/IAA proteins." Kim J., Harter K., Theologis A. Proc. Natl. Acad. Sci. U.S.A. 94:11786-11791(1997) [PubMed: 9342315] [Abstract] Cited for: DIMERIZATION.
[7]	"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(2000) [PubMed: 11115889] [Abstract] Cited for: PHOSPHORYLATION BY PHYTOCHROME A.
[8]	"Genetics of Aux/IAA and ARF action in plant growth and development." Liscum E., Reed J.W. Plant Mol. Biol. 49:387-400(2002) [PubMed: 12036262] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, FUNCTION.
[9]	"Aux/IAA proteins contain a potent transcriptional repression domain." Tiwari S.B., Hagen G., Guilfoyle T.J. Plant Cell 16:533-543(2004) [PubMed: 14742873] [Abstract] Cited for: TRANSCRIPTIONAL REPRESSION DOMAIN.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L15448 mRNA. Translation: AAA16569.1. Z97336 Genomic DNA. Translation: CAB10235.1. AL161539 Genomic DNA. Translation: CAB78498.1. AY133714 mRNA. Translation: AAM91648.1.
PIR	A71408.
RefSeq	NP_193192.1.
UniGene	At.43941
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P49677.
Genome annotation databases
GeneID	827103.
GenomeReviews	Gene locus AT4G14560 in contig CT486007_GR.
KEGG	ath:AT4G14560.
Organism-specific databases
GeneFarm	3140. 342.
TAIR	At4g14560.
Gene expression databases
ArrayExpress	P49677.
GermOnline	AT4G14560. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR003311. AUX_IAA. IPR011525. AuxIAA_ARF_dimer. [Graphical view]
Pfam	PF02309. AUX_IAA. 1 hit. [Graphical view]
PROSITE	PS50962. IAA_ARF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P49677.

Entry information

Entry name

IAA1_ARATH

Accession

Primary (citable) accession number: P49677
Secondary accession number(s): O23312

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)