ILL3_ARATH
ID ILL3_ARATH Reviewed; 428 AA.
AC O81641;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=IAA-amino acid hydrolase ILR1-like 3 {ECO:0000303|PubMed:10072397};
DE EC=3.5.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ILL3 {ECO:0000303|PubMed:10072397};
GN OrderedLocusNames=At5g54140 {ECO:0000312|Araport:AT5G54140};
GN ORFNames=MJP23.12 {ECO:0000312|EMBL:BAB11576.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10072397; DOI=10.2307/3870866;
RA Davies R.T., Goetz D.H., Lasswell J.E., Anderson M.N., Bartel B.;
RT "IAR3 encodes an auxin conjugate hydrolase from Arabidopsis.";
RL Plant Cell 11:365-376(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP GENE FAMILY.
RX PubMed=11923288; DOI=10.1074/jbc.m111955200;
RA LeClere S., Tellez R., Rampey R.A., Matsuda S.P.T., Bartel B.;
RT "Characterization of a family of IAA-amino acid conjugate hydrolases from
RT Arabidopsis.";
RL J. Biol. Chem. 277:20446-20452(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15155875; DOI=10.1104/pp.104.039677;
RA Rampey R.A., LeClere S., Kowalczyk M., Ljung K., Sandberg G., Bartel B.;
RT "A family of auxin-conjugate hydrolases that contributes to free indole-3-
RT acetic acid levels during Arabidopsis germination.";
RL Plant Physiol. 135:978-988(2004).
CC -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth
CC regulator indole-3-acetic acid (IAA). {ECO:0000250|UniProtKB:P54968}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, and hypocotyls of
CC seedlings, and in leaves and pollen of mature plants.
CC {ECO:0000269|PubMed:15155875}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; AF081066; AAC31939.1; -; Genomic_DNA.
DR EMBL; AB013387; BAB11576.1; -; Genomic_DNA.
DR EMBL; AB018115; BAB11576.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96456.1; -; Genomic_DNA.
DR RefSeq; NP_200225.1; NM_124794.3.
DR AlphaFoldDB; O81641; -.
DR SMR; O81641; -.
DR BioGRID; 20745; 1.
DR STRING; 3702.AT5G54140.1; -.
DR MEROPS; M20.A06; -.
DR iPTMnet; O81641; -.
DR PaxDb; O81641; -.
DR PRIDE; O81641; -.
DR ProteomicsDB; 228839; -.
DR EnsemblPlants; AT5G54140.1; AT5G54140.1; AT5G54140.
DR GeneID; 835501; -.
DR Gramene; AT5G54140.1; AT5G54140.1; AT5G54140.
DR KEGG; ath:AT5G54140; -.
DR Araport; AT5G54140; -.
DR TAIR; locus:2166557; AT5G54140.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; O81641; -.
DR OMA; RAHACGH; -.
DR OrthoDB; 1022341at2759; -.
DR PhylomeDB; O81641; -.
DR BioCyc; ARA:AT5G54140-MON; -.
DR PRO; PR:O81641; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81641; baseline and differential.
DR Genevisible; O81641; AT.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0010178; F:IAA-amino acid conjugate hydrolase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; ISS:TAIR.
DR CDD; cd08017; M20_IAA_Hyd; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR044757; ILR1-like_Hyd.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Manganese; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..428
FT /note="IAA-amino acid hydrolase ILR1-like 3"
FT /id="PRO_0000045469"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 391
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
SQ SEQUENCE 428 AA; 46791 MW; 8B3A8FB11E958689 CRC64;
MANSSIVALL LLFVIASSVN GGDQEYPNQY LTEALGDKEW LVSVRRQIHE NPELLFELHK
TSALIRRELD ELGVSYSYPV AKTGIVAQIG SGYPPVVALR ADMDALPLQE LVEWDHKSKI
DGKMHACGHD SHTTMLLGAA KLLSKRKRML NGTVRLLFQP AEEGGAGAFH MIKEGALGDS
EAIFGMHVHT GLPTGELATI SGPALASTSI FSVRMSGKSP ASSETYSCVD PVLAASSTIL
ALQLIISREV DPLLSHVLSV TFMKSGGSEF DVIPAYVEFG GTLRSLTTNG INWLIKRLKE
VVEGQAEVQR CKADIDMHED DHPMYPATVN DHKLHEFTEK VLKLLLGPEK VKPANKVMAG
EDFAFYQQKI PGYYIGIGIR NEEIGSVRSV HSPYFFLDEN VLPIGSATFA ALAEMYLQEH
QNQTKSGD
