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P54970

- ILL2_ARATH

UniProt

P54970 - ILL2_ARATH

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Protein

IAA-amino acid hydrolase ILR1-like 2

Gene

ILL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 Mn(2+) ion enhances activity.

GO - Molecular functioni

  1. IAA-Ala conjugate hydrolase activity Source: TAIR
  2. IAA-amino acid conjugate hydrolase activity Source: TAIR

GO - Biological processi

  1. 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: Chromosome 5

Organism-specific databases

TAIRiAT5G56660.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
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.

Expressioni

Gene expression databases

GenevestigatoriP54970.

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.
OMAiRRNLHEH.
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 .
RefSeqi NP_200477.1. NM_125049.3.
UniGenei At.46738.
At.66661.
At.66838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XMB X-ray 2.00 A 22-439 [» ]
2Q43 X-ray 2.00 A 22-439 [» ]
ProteinModelPortali P54970.
SMRi P54970. Positions 37-428.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M20.014.

Proteomic databases

PaxDbi P54970.
PRIDEi P54970.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G56660.1 ; AT5G56660.1 ; AT5G56660 .
GeneIDi 835767.
KEGGi ath:AT5G56660.

Organism-specific databases

GeneFarmi 1960. 187.
TAIRi AT5G56660.

Phylogenomic databases

eggNOGi COG1473.
HOGENOMi HOG000241403.
InParanoidi P54970.
KOi K14664.
OMAi RRNLHEH.
PhylomeDBi P54970.

Miscellaneous databases

EvolutionaryTracei P54970.

Gene expression databases

Genevestigatori P54970.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR017439. Amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF005962. Pept_M20D_amidohydro. 1 hit.
SUPFAMi SSF55031. SSF55031. 1 hit.
TIGRFAMsi TIGR01891. amidohydrolases. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 121 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