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Protein

IAA-amino acid hydrolase ILR1-like 2

Gene

ILL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Cofactori

Mn2+Note: The Mn2+ ion enhances activity.

GO - Molecular functioni

  • IAA-Ala conjugate hydrolase activity Source: TAIR
  • IAA-amino acid conjugate hydrolase activity Source: TAIR

GO - Biological processi

  • auxin metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese

Protein family/group databases

MEROPSiM20.014.

Names & Taxonomyi

Protein namesi
Recommended name:
IAA-amino acid hydrolase ILR1-like 2 (EC:3.5.1.-)
Gene namesi
Name:ILL2
Ordered Locus Names:At5g56660
ORF Names:MIK19.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G56660.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 439418IAA-amino acid hydrolase ILR1-like 2PRO_0000001190Add
BLAST

Proteomic databases

PaxDbiP54970.
PRIDEiP54970.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G56660.1.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 436Combined sources
Helixi45 – 6016Combined sources
Helixi69 – 8214Combined sources
Beta strandi86 – 905Combined sources
Turni91 – 933Combined sources
Beta strandi94 – 10411Combined sources
Beta strandi106 – 1127Combined sources
Helixi139 – 15517Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 1699Combined sources
Turni172 – 1754Combined sources
Helixi177 – 1837Combined sources
Turni184 – 1896Combined sources
Beta strandi190 – 20314Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi217 – 22711Combined sources
Helixi240 – 25314Combined sources
Helixi262 – 2643Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi285 – 29612Combined sources
Helixi298 – 31518Combined sources
Beta strandi318 – 3258Combined sources
Helixi326 – 3283Combined sources
Beta strandi335 – 3373Combined sources
Helixi339 – 35315Combined sources
Helixi355 – 3573Combined sources
Beta strandi358 – 3603Combined sources
Helixi370 – 3745Combined sources
Turni375 – 3784Combined sources
Beta strandi379 – 3879Combined sources
Beta strandi396 – 3983Combined sources
Helixi405 – 4073Combined sources
Helixi408 – 42720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XMBX-ray2.00A22-439[»]
2Q43X-ray2.00A22-439[»]
ProteinModelPortaliP54970.
SMRiP54970. Positions 37-428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54970.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi436 – 4394Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the peptidase M20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1473.
HOGENOMiHOG000241403.
InParanoidiP54970.
KOiK14664.
OMAiQVRTWRT.
PhylomeDBiP54970.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01891. amidohydrolases. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54970-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALNKLLSLT FQLLLFLLSV SSESPWIAED TSQIQTKLLE FAKSPEVFDW
60 70 80 90 100
MVKIRRKIHE NPELGYEELE TSKLIRSELE LIGIKYRYPV AITGVIGYIG
110 120 130 140 150
TGEPPFVALR ADMDALPIQE GVEWEHKSKI AGKMHACGHD GHVTMLLGAA
160 170 180 190 200
KILHEHRHHL QGTVVLIFQP AEEGLSGAKK MREEGALKNV EAIFGIHLSA
210 220 230 240 250
RIPFGKAASR AGSFLAGAGV FEAVITGKGG HAAIPQHTID PVVAASSIVL
260 270 280 290 300
SLQQLVSRET DPLDSKVVTV SKVNGGNAFN VIPDSITIGG TLRAFTGFTQ
310 320 330 340 350
LQQRVKEVIT KQAAVHRCNA SVNLTPNGRE PMPPTVNNKD LYKQFKKVVR
360 370 380 390 400
DLLGQEAFVE AAPVMGSEDF SYFAETIPGH FSLLGMQDET NGYASSHSPL
410 420 430
YRINEDVLPY GAAIHASMAV QYLKEKASKG SVSGFHEEL
Length:439
Mass (Da):47,856
Last modified:May 27, 2002 - v2
Checksum:iBFA5F35AF4C4F508
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311A → P in AAC49016 (PubMed:7792599).Curated
Sequence conflicti236 – 2361Q → H in AAC49016 (PubMed:7792599).Curated
Sequence conflicti240 – 2401D → G in AAL59907 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_200477.1. NM_125049.3.
UniGeneiAt.46738.
At.66661.
At.66838.

Genome annotation databases

EnsemblPlantsiAT5G56660.1; AT5G56660.1; AT5G56660.
GeneIDi835767.
KEGGiath:AT5G56660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_200477.1. NM_125049.3.
UniGeneiAt.46738.
At.66661.
At.66838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XMBX-ray2.00A22-439[»]
2Q43X-ray2.00A22-439[»]
ProteinModelPortaliP54970.
SMRiP54970. Positions 37-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G56660.1.

Protein family/group databases

MEROPSiM20.014.

Proteomic databases

PaxDbiP54970.
PRIDEiP54970.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G56660.1; AT5G56660.1; AT5G56660.
GeneIDi835767.
KEGGiath:AT5G56660.

Organism-specific databases

GeneFarmi1960. 187.
TAIRiAT5G56660.

Phylogenomic databases

eggNOGiCOG1473.
HOGENOMiHOG000241403.
InParanoidiP54970.
KOiK14664.
OMAiQVRTWRT.
PhylomeDBiP54970.

Miscellaneous databases

EvolutionaryTraceiP54970.
PROiP54970.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01891. amidohydrolases. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiILL2_ARATH
AccessioniPrimary (citable) accession number: P54970
Secondary accession number(s): O49221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: July 22, 2015
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.