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Protein

IAA-amino acid hydrolase ILR1-like 4

Gene

ILL4

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

GO - Biological processi

  • response to wounding Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-3488-MONOMER.

Protein family/group databases

MEROPSiM20.A04.

Names & Taxonomyi

Protein namesi
Recommended name:
IAA-amino acid hydrolase ILR1-like 4 (EC:3.5.1.-)
Gene namesi
Name:ILL4
Synonyms:IAR3, JR3
Ordered Locus Names:At1g51760
ORF Names:F19C24.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G51760.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2061S → L in iar3-1; reduces activity. 1 Publication
Mutagenesisi224 – 2241G → E in iar3-2; abolishes activity. 1 Publication
Mutagenesisi226 – 2261G → E in iar3-4; reduces activity. 1 Publication
Mutagenesisi230 – 2301A → T in iar3-3; reduces activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 440417IAA-amino acid hydrolase ILR1-like 4PRO_0000045470Add
BLAST

Proteomic databases

PaxDbiO04373.
PRIDEiO04373.

Expressioni

Tissue specificityi

Expressed most strongly in roots, stems, cauline leaves and flowers.1 Publication

Inductioni

By jasmonic acid (JA) and by wounding.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi26827. 1 interaction.
STRINGi3702.AT1G51760.1.

Structurei

3D structure databases

ProteinModelPortaliO04373.
SMRiO04373. Positions 34-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi437 – 4404Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the peptidase M20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1473.
HOGENOMiHOG000241403.
InParanoidiO04373.
KOiK14664.
OMAiKRTRGYP.
PhylomeDBiO04373.

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.

O04373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFFKWVSFV LILHLLNPTL ISCSSNGLSQ IPSKFLTLAK RNDFFDWMVG
60 70 80 90 100
IRRRIHENPE LGYEEVETSK LVRAELEKMG VSYKYPVAVT GVVGYVGTGH
110 120 130 140 150
APFVALRADM DALAMQEMVE WEHKSKVPGK MHACGHDAHT TMLLGAAKLL
160 170 180 190 200
KEHEEELQGT VVLVFQPAEE GGGGAKKIVE AGVLENVSAI FGLHVTNQLA
210 220 230 240 250
LGQVSSREGP MLAGSGFFKA KISGKGGHAA LPQHTIDPIL AASNVIVSLQ
260 270 280 290 300
HLVSREADPL DSQVVTVAKF EGGGAFNVIP DSVTIGGTFR AFSTKSFMQL
310 320 330 340 350
KKRIEQVITR QASVNMCNAT VDFIEEEKPF FPPTVNDKAL HQFFKNVSGD
360 370 380 390 400
MLGIENYVEM QPLMGSEDFS FYQQAIPGHF SFVGMQNKAR SPMASPHSPY
410 420 430 440
FEVNEELLPY GASLHASMAT RYLLELKAST LNKSNKKDEL
Length:440
Mass (Da):48,263
Last modified:January 10, 2006 - v2
Checksum:i8B605EEF67A1746E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111M → I in CAA73905 (PubMed:9342878).Curated
Sequence conflicti291 – 2911A → AFST in CAA73905 (PubMed:9342878).Curated
Sequence conflicti325 – 3295EEEKP → ARGET in CAA73905 (PubMed:9342878).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13577 mRNA. Translation: CAA73905.1.
AF081067 Genomic DNA. Translation: AAC32192.1.
AC025294 Genomic DNA. Translation: AAG50883.1.
CP002684 Genomic DNA. Translation: AEE32712.1.
AF375444 mRNA. Translation: AAK53028.1.
AY143961 mRNA. Translation: AAN28900.1.
PIRiF96556.
RefSeqiNP_175587.1. NM_104055.3.
UniGeneiAt.52138.
At.5375.

Genome annotation databases

EnsemblPlantsiAT1G51760.1; AT1G51760.1; AT1G51760.
GeneIDi841602.
KEGGiath:AT1G51760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13577 mRNA. Translation: CAA73905.1.
AF081067 Genomic DNA. Translation: AAC32192.1.
AC025294 Genomic DNA. Translation: AAG50883.1.
CP002684 Genomic DNA. Translation: AEE32712.1.
AF375444 mRNA. Translation: AAK53028.1.
AY143961 mRNA. Translation: AAN28900.1.
PIRiF96556.
RefSeqiNP_175587.1. NM_104055.3.
UniGeneiAt.52138.
At.5375.

3D structure databases

ProteinModelPortaliO04373.
SMRiO04373. Positions 34-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26827. 1 interaction.
STRINGi3702.AT1G51760.1.

Chemistry

ChEMBLiCHEMBL1687678.

Protein family/group databases

MEROPSiM20.A04.

Proteomic databases

PaxDbiO04373.
PRIDEiO04373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G51760.1; AT1G51760.1; AT1G51760.
GeneIDi841602.
KEGGiath:AT1G51760.

Organism-specific databases

GeneFarmi1917. 187.
TAIRiAT1G51760.

Phylogenomic databases

eggNOGiCOG1473.
HOGENOMiHOG000241403.
InParanoidiO04373.
KOiK14664.
OMAiKRTRGYP.
PhylomeDBiO04373.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-3488-MONOMER.

Miscellaneous databases

PROiO04373.

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. "Jasmonic acid-dependent and -independent signaling pathways control wound-induced gene activation in Arabidopsis thaliana."
    Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.
    Plant Physiol. 115:817-826(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  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], TISSUE SPECIFICITY, MUTAGENESIS OF SER-206; GLY-224; GLY-226 AND ALA-230.
    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] [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.

Entry informationi

Entry nameiILL4_ARATH
AccessioniPrimary (citable) accession number: O04373
Secondary accession number(s): O81642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: July 22, 2015
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.