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P54970 (ILL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
IAA-amino acid hydrolase ILR1-like 2

EC=3.5.1.-
Gene names
Name:ILL2
Ordered Locus Names:At5g56660
ORF Names:MIK19.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala.

Cofactor

Manganese. The ion enhances activity.

Subcellular location

Endoplasmic reticulum lumen Potential.

Sequence similarities

Belongs to the peptidase M20 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 439418IAA-amino acid hydrolase ILR1-like 2
PRO_0000001190

Regions

Motif436 – 4394Prevents secretion from ER Potential

Experimental info

Sequence conflict1311A → P in AAC49016. Ref.1
Sequence conflict2361Q → H in AAC49016. Ref.1
Sequence conflict2401D → G in AAL59907. Ref.5

Secondary structure

............................................................ 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54970 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: BFA5F35AF4C4F508

FASTA43947,856
        10         20         30         40         50         60 
MALNKLLSLT FQLLLFLLSV SSESPWIAED TSQIQTKLLE FAKSPEVFDW MVKIRRKIHE 

        70         80         90        100        110        120 
NPELGYEELE TSKLIRSELE LIGIKYRYPV AITGVIGYIG TGEPPFVALR ADMDALPIQE 

       130        140        150        160        170        180 
GVEWEHKSKI AGKMHACGHD GHVTMLLGAA KILHEHRHHL QGTVVLIFQP AEEGLSGAKK 

       190        200        210        220        230        240 
MREEGALKNV EAIFGIHLSA RIPFGKAASR AGSFLAGAGV FEAVITGKGG HAAIPQHTID 

       250        260        270        280        290        300 
PVVAASSIVL SLQQLVSRET DPLDSKVVTV SKVNGGNAFN VIPDSITIGG TLRAFTGFTQ 

       310        320        330        340        350        360 
LQQRVKEVIT KQAAVHRCNA SVNLTPNGRE PMPPTVNNKD LYKQFKKVVR DLLGQEAFVE 

       370        380        390        400        410        420 
AAPVMGSEDF SYFAETIPGH FSLLGMQDET NGYASSHSPL YRINEDVLPY GAAIHASMAV 

       430 
QYLKEKASKG SVSGFHEEL 

« Hide

References

« Hide 'large scale' references
[1]"ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates."
Bartel B., Fink G.R.
Science 268:1745-1748(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]"IAR3 encodes an auxin conjugate hydrolase from Arabidopsis."
Davies R.T., Goetz D.H., Lasswell J.E., Anderson M.N., Bartel B.
Plant Cell 11:365-376(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-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. expand/collapse author list , 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.
[6]"Characterization of a family of IAA-amino acid conjugate hydrolases from Arabidopsis."
LeClere S., Tellez R., Rampey R.A., Matsuda S.P.T., Bartel B.
J. Biol. Chem. 277:20446-20452(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
[7]"X-ray structure of IAA-aminoacid hydrolase from Arabidopsis thaliana gene At5g56660."
Wesenberg G.E., Smith D.W., Phillips G.N. Jr., Bitto E., Bingman C.A., Allard S.T.M.
Submitted (OCT-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-439.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23796 mRNA. Translation: AAC49016.1.
AF047031 Genomic DNA. Translation: AAC04866.1.
AB013392 Genomic DNA. Translation: BAB09884.1.
CP002688 Genomic DNA. Translation: AED96793.1.
AY072084 mRNA. Translation: AAL59907.1.
RefSeqNP_200477.1. NM_125049.3.
UniGeneAt.46738.
At.66661.
At.66838.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XMBX-ray2.00A22-439[»]
2Q43X-ray2.00A22-439[»]
ProteinModelPortalP54970.
SMRP54970. Positions 37-428.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM20.014.

Proteomic databases

PaxDbP54970.
PRIDEP54970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G56660.1; AT5G56660.1; AT5G56660.
GeneID835767.
KEGGath:AT5G56660.

Organism-specific databases

GeneFarm1960. 187.
TAIRAT5G56660.

Phylogenomic databases

eggNOGCOG1473.
HOGENOMHOG000241403.
InParanoidP54970.
KOK14664.
OMAHASAPHK.
PhylomeDBP54970.
ProtClustDBPLN02693.

Gene expression databases

GenevestigatorP54970.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
InterProIPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01891. amidohydrolases. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54970.

Entry information

Entry nameILL2_ARATH
AccessionPrimary (citable) accession number: P54970
Secondary accession number(s): O49221
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names