ILL1_ARATH
ID ILL1_ARATH Reviewed; 438 AA.
AC P54969;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=IAA-amino acid hydrolase ILR1-like 1 {ECO:0000303|PubMed:7792599};
DE EC=3.5.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=ILL1 {ECO:0000303|PubMed:7792599};
GN OrderedLocusNames=At5g56650 {ECO:0000312|Araport:AT5G56650};
GN ORFNames=MIK19.10 {ECO:0000312|EMBL:BAB09883.1};
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7792599; DOI=10.1126/science.7792599;
RA Bartel B., Fink G.R.;
RT "ILR1, an amidohydrolase that releases active indole-3-acetic acid from
RT conjugates.";
RL Science 268:1745-1748(1995).
RN [2]
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 [3]
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 [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, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
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), including IAA-Ala, IAA-Asn and
CC IAA-Tyr. {ECO:0000269|PubMed:11923288}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11923288};
CC Note=The Mn(2+) ion enhances activity. {ECO:0000269|PubMed:11923288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11923288};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, siliques and
CC flowers. Detected in pollen. {ECO:0000269|PubMed:15155875}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; U23795; AAC49015.1; -; mRNA.
DR EMBL; AF047031; AAC04865.1; -; Genomic_DNA.
DR EMBL; AB013392; BAB09883.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96792.1; -; Genomic_DNA.
DR RefSeq; NP_200476.1; NM_125048.2.
DR AlphaFoldDB; P54969; -.
DR SMR; P54969; -.
DR BioGRID; 21010; 1.
DR STRING; 3702.AT5G56650.1; -.
DR MEROPS; M20.A03; -.
DR iPTMnet; P54969; -.
DR PaxDb; P54969; -.
DR PRIDE; P54969; -.
DR ProteomicsDB; 228849; -.
DR EnsemblPlants; AT5G56650.1; AT5G56650.1; AT5G56650.
DR GeneID; 835766; -.
DR Gramene; AT5G56650.1; AT5G56650.1; AT5G56650.
DR KEGG; ath:AT5G56650; -.
DR Araport; AT5G56650; -.
DR TAIR; locus:2165076; AT5G56650.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; P54969; -.
DR OMA; MKMHACG; -.
DR OrthoDB; 1022341at2759; -.
DR PhylomeDB; P54969; -.
DR BioCyc; ARA:AT5G56650-MON; -.
DR PRO; PR:P54969; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P54969; baseline and differential.
DR Genevisible; P54969; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; IBA:GO_Central.
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 InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..438
FT /note="IAA-amino acid hydrolase ILR1-like 1"
FT /id="PRO_0000001189"
FT MOTIF 435..438
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 396
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
SQ SEQUENCE 438 AA; 47692 MW; 8EAB21F1E62370B1 CRC64;
MALNNFLTFQ LLLLLLRVSS ESPWIVAGDV SRIPINFLEL AKSPEVFDSM VRIRRKIHEN
PELGYEEFET SKFIRSELDL IGVKYRFPVA ITGIIGYIGT GEPPFVALRA DMDALPIQEA
VEWEHKSKNP GKMHACGHDG HVAMLLGAAK ILQQHRQHLQ GTVVLIFQPA EEGLSGAKMM
REEGALKNVE AIFGIHLSPR TPFGKAASLA GSFMAGAGAF EAVITGKGGH AAIPQHTIDP
VVAASSIVLS LQHLVSRETD PSDSKVVTVT KVNGGNAFNV IPDSITIGGT LRAFTGFTQL
QERIKEIITK QAAVHRCNAS VNLAPNGNQP MPPTVNNMDL YKKFKKVVRD LLGQEAFVEA
VPEMGSEDFS YFAETIPGHF SLLGMQDETQ GYASSHSPHY RINEDVLPYG AAIHATMAVQ
YLKDKASKGS VSGFHDEL
