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O04373

- ILL4_ARATH

UniProt

O04373 - ILL4_ARATH

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Protein

IAA-amino acid hydrolase ILR1-like 4

Gene
ILL4, IAR3, JR3, At1g51760, F19C24.4
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Manganese. The ion enhances activity.

GO - Molecular functioni

  1. IAA-Ala conjugate hydrolase activity Source: TAIR

GO - Biological processi

  1. 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: Chromosome 1

Organism-specific databases

TAIRiAT1G51760.

Subcellular locationi

Endoplasmic reticulum lumen Reviewed prediction

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. 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 – 2323 Reviewed predictionAdd
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

Gene expression databases

GenevestigatoriO04373.

Interactioni

Protein-protein interaction databases

BioGridi26827. 1 interaction.
STRINGi3702.AT1G51760.1-P.

Structurei

3D structure databases

ProteinModelPortaliO04373.
SMRiO04373. Positions 34-429.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi437 – 4404Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Belongs to the peptidase M20 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1473.
HOGENOMiHOG000241403.
InParanoidiO04373.
KOiK14664.
OMAiKMLIEPG.
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

MSFFKWVSFV LILHLLNPTL ISCSSNGLSQ IPSKFLTLAK RNDFFDWMVG    50
IRRRIHENPE LGYEEVETSK LVRAELEKMG VSYKYPVAVT GVVGYVGTGH 100
APFVALRADM DALAMQEMVE WEHKSKVPGK MHACGHDAHT TMLLGAAKLL 150
KEHEEELQGT VVLVFQPAEE GGGGAKKIVE AGVLENVSAI FGLHVTNQLA 200
LGQVSSREGP MLAGSGFFKA KISGKGGHAA LPQHTIDPIL AASNVIVSLQ 250
HLVSREADPL DSQVVTVAKF EGGGAFNVIP DSVTIGGTFR AFSTKSFMQL 300
KKRIEQVITR QASVNMCNAT VDFIEEEKPF FPPTVNDKAL HQFFKNVSGD 350
MLGIENYVEM QPLMGSEDFS FYQQAIPGHF SFVGMQNKAR SPMASPHSPY 400
FEVNEELLPY GASLHASMAT RYLLELKAST LNKSNKKDEL 440
Length:440
Mass (Da):48,263
Last modified:January 10, 2006 - v2
Checksum:i8B605EEF67A1746E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111M → I in CAA73905. 1 Publication
Sequence conflicti291 – 2911A → AFST in CAA73905. 1 Publication
Sequence conflicti325 – 3295EEEKP → ARGET in CAA73905. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi F96556.
RefSeqi NP_175587.1. NM_104055.3.
UniGenei At.52138.
At.5375.

3D structure databases

ProteinModelPortali O04373.
SMRi O04373. Positions 34-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 26827. 1 interaction.
STRINGi 3702.AT1G51760.1-P.

Chemistry

ChEMBLi CHEMBL1687678.

Protein family/group databases

MEROPSi M20.A04.

Proteomic databases

PaxDbi O04373.
PRIDEi O04373.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G51760.1 ; AT1G51760.1 ; AT1G51760 .
GeneIDi 841602.
KEGGi ath:AT1G51760.

Organism-specific databases

GeneFarmi 1917. 187.
TAIRi AT1G51760.

Phylogenomic databases

eggNOGi COG1473.
HOGENOMi HOG000241403.
InParanoidi O04373.
KOi K14664.
OMAi KMLIEPG.
PhylomeDBi O04373.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-3488-MONOMER.

Gene expression databases

Genevestigatori O04373.

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. "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 9, 2014
This is version 102 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

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