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Protein

Auxin-responsive protein IAA28

Gene

IAA28

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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

  • sequence-specific DNA binding transcription factor activity Source: TAIR

GO - Biological processi

  • auxin-activated signaling pathway Source: UniProtKB-KW
  • lateral root morphogenesis Source: TAIR
  • response to auxin Source: TAIR
  • 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 IAA28
Alternative name(s):
Indoleacetic acid-induced protein 28
Gene namesi
Name:IAA28
Ordered Locus Names:At5g25890
ORF Names:F18A17.6, T1N24.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G25890.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531P → L in iaa28-1; gain of function. Affects auxin-related developmental processes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Auxin-responsive protein IAA28PRO_0000112854Add
BLAST

Expressioni

Tissue specificityi

In roots and inflorescence stems.

Inductioni

Not induced by auxin.

Interactioni

Subunit structurei

Homodimers and heterodimers (By similarity). Interacts with TPL.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARF6Q9ZTX83EBI-3133404,EBI-3946770
ARF9Q9XED83EBI-3133404,EBI-3946762
IAA11Q388293EBI-3133404,EBI-2367923

Protein-protein interaction databases

BioGridi17933. 39 interactions.
IntActiQ9XFM0. 40 interactions.
STRINGi3702.AT5G25890.1.

Structurei

3D structure databases

ProteinModelPortaliQ9XFM0.
SMRiQ9XFM0. Positions 81-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 16182PB1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 115EAR-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

eggNOGiNOG283222.
HOGENOMiHOG000238261.
InParanoidiQ9XFM0.
KOiK14484.
OMAiDLNRQYT.
PhylomeDBiQ9XFM0.

Family and domain databases

InterProiIPR003311. AUX_IAA.
IPR000270. PB1_dom.
[Graphical view]
PfamiPF02309. AUX_IAA. 1 hit.
[Graphical view]
PROSITEiPS51745. PB1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XFM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEEKRLELR LAPPCHQFTS NNNINGSKQK SSTKETSFLS NNRVEVAPVV
60 70 80 90 100
GWPPVRSSRR NLTAQLKEEM KKKESDEEKE LYVKINMEGV PIGRKVNLSA
110 120 130 140 150
YNNYQQLSHA VDQLFSKKDS WDLNRQYTLV YEDTEGDKVL VGDVPWEMFV
160 170
STVKRLHVLK TSHAFSLSPR KHGKE
Length:175
Mass (Da):20,206
Last modified:November 1, 1999 - v1
Checksum:i7A58B615DBC8FB47
GO

Sequence cautioni

The sequence AAD40120.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149816 mRNA. Translation: AAD34019.1.
AC005405 Genomic DNA. No translation available.
AF149413 Genomic DNA. Translation: AAD40120.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93498.1.
BT000427 mRNA. Translation: AAN17404.1.
BT002175 mRNA. Translation: AAN72186.1.
PIRiT52143.
RefSeqiNP_568478.1. NM_122490.3.
UniGeneiAt.11439.

Genome annotation databases

EnsemblPlantsiAT5G25890.1; AT5G25890.1; AT5G25890.
GeneIDi832658.
KEGGiath:AT5G25890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149816 mRNA. Translation: AAD34019.1.
AC005405 Genomic DNA. No translation available.
AF149413 Genomic DNA. Translation: AAD40120.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED93498.1.
BT000427 mRNA. Translation: AAN17404.1.
BT002175 mRNA. Translation: AAN72186.1.
PIRiT52143.
RefSeqiNP_568478.1. NM_122490.3.
UniGeneiAt.11439.

3D structure databases

ProteinModelPortaliQ9XFM0.
SMRiQ9XFM0. Positions 81-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17933. 39 interactions.
IntActiQ9XFM0. 40 interactions.
STRINGi3702.AT5G25890.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G25890.1; AT5G25890.1; AT5G25890.
GeneIDi832658.
KEGGiath:AT5G25890.

Organism-specific databases

GeneFarmi3188. 342.
TAIRiAT5G25890.

Phylogenomic databases

eggNOGiNOG283222.
HOGENOMiHOG000238261.
InParanoidiQ9XFM0.
KOiK14484.
OMAiDLNRQYT.
PhylomeDBiQ9XFM0.

Miscellaneous databases

PROiQ9XFM0.

Family and domain databases

InterProiIPR003311. AUX_IAA.
IPR000270. PB1_dom.
[Graphical view]
PfamiPF02309. AUX_IAA. 1 hit.
[Graphical view]
PROSITEiPS51745. PB1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A gain-of-function mutation in IAA28 suppresses lateral root development."
    Rogg L.E., Lasswell J.E., Bartel B.
    Plant Cell 13:465-480(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTANT IAA28-1.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, FUNCTION.
  6. "Aux/IAA proteins contain a potent transcriptional repression domain."
    Tiwari S.B., Hagen G., Guilfoyle T.J.
    Plant Cell 16:533-543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REPRESSION DOMAIN.
  7. "TOPLESS mediates auxin-dependent transcriptional repression during Arabidopsis embryogenesis."
    Szemenyei H., Hannon M., Long J.A.
    Science 319:1384-1386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPL.

Entry informationi

Entry nameiIAA28_ARATH
AccessioniPrimary (citable) accession number: Q9XFM0
Secondary accession number(s): Q9S9V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 106 of the entry and version 1 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.