Reviewed, UniProtKB/Swiss-Prot P93830 (IAA17_ARATH)

Names and origin

Protein names

Recommended name:
    Auxin-responsive protein IAA17
Alternative name(s):
    Indoleacetic acid-induced protein 17
    Auxin response 3

Gene names

Name:	IAA17
Synonyms:	AXR3
Ordered Locus Names:	At1g04250
ORF Names:	F19P19.31

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	229 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. Ref.7
Subunit structure	Homo and heterodimers. Interacts with the auxin response factors ARF1 and IAA24.
Subcellular location	Nucleus.
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. Ref.8
Post-translational modification	Phosphorylated by phytochrome A in vitro. Ref.6
Miscellaneous	Increased auxin response of mutants axr3-1 and axr3-3 may result form an increased stability of AXR3.
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 Traceable author statement. Source: TAIR regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: TAIR
Molecular function	protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIR1	Q570C0	2	EBI-632243,EBI-307183

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	Auxin-responsive protein IAA17		PRO_0000112848
Regions
	Domain	111 – 212	102	Aux/IAA-ARF
	Motif	14 – 18	5	EAR-like (transcriptional repression)
Experimental info
	Mutagenesis	16	1	L → F: Suppresses the axr3-1 phenotype; when associated with L-88. Ref.2
	Mutagenesis	88	1	P → L in axr3-1; gain of function. Affects auxin-related developmental processes. Affects photomorphogenesis.
	Mutagenesis	89	1	V → G in axr3-3; gain of function. Affects auxin-related developmental processes. Affects photomorphogenesis.
	Mutagenesis	118	1	D → N: Suppresses the axr3-1 phenotype; when associated with L-88. Ref.2
	Mutagenesis	121	1	P → S: Suppresses the axr3-1 phenotype; when associated with L-88. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P93830-1 [UniParc]. Last modified January 1, 1998. Version 2. Checksum: ECEA39207476581E	FASTA	229	25,288
	10 20 30 40 50 60 MMGSVELNLR ETELCLGLPG GDTVAPVTGN KRGFSETVDL KLNLNNEPAN KEGSTTHDVV 70 80 90 100 110 120 TFDSKEKSAC PKDPAKPPAK AQVVGWPPVR SYRKNVMVSC QKSSGGPEAA AFVKVSMDGA 130 140 150 160 170 180 PYLRKIDLRM YKSYDELSNA LSNMFSSFTM GKHGGEEGMI DFMNERKLMD LVNSWDYVPS 190 200 210 220 YEDKDGDWML VGDVPWPMFV DTCKRLRLMK GSDAIGLAPR AMEKCKSRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Changes in auxin response from mutations in an AUX/IAA gene." Rouse D., Mackay P., Stirnberg P., Estelle M., Leyser O. Science 279:1371-1373(1998) [PubMed: 9478901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS AXR3-1 AND AXR3-3, MUTAGENESIS OF LEU-16; ASP-118 AND PRO-121. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [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]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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.
[7]	"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.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49073 mRNA. Translation: AAB84354.1. AF040631 Genomic DNA. Translation: AAC39439.1. AF040632 Genomic DNA. Translation: AAC39440.1. AC000104 Genomic DNA. Translation: AAB70451.2. AF336916 mRNA. Translation: AAG53997.1. AY070094 mRNA. Translation: AAL49831.1. AY117183 mRNA. Translation: AAM51258.1. AY087284 mRNA. Translation: AAM64837.1. Different initiation.
IPI	IPI00548274.
PIR	H86173.
RefSeq	NP_171921.1.
UniGene	At.20252 Rra.7128 Rsa.3548
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P93830. 2 interactions.
STRING	P93830.
Genome annotation databases
GeneID	839568.
GenomeReviews	Gene locus AT1G04250 in contig CT485782_GR.
KEGG	ath:AT1G04250.
NMPDR	fig|3702.1.peg.571.
Organism-specific databases
GeneFarm	3180. 342.
TAIR	At1g04250.
Phylogenomic databases
HOGENOM	HBG750482.
InParanoid	P93830.
OMA	KIDLRMY.
Gene expression databases
ArrayExpress	P93830.
Genevestigator	P93830.
GermOnline	AT1G04250. 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...

Entry information

Entry name

IAA17_ARATH

Accession

Primary (citable) accession number: P93830
Secondary accession number(s): O49162

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	December 15, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)