ID ILL4_ARATH Reviewed; 440 AA. AC O04373; O81642; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=IAA-amino acid hydrolase ILR1-like 4 {ECO:0000303|PubMed:10072397}; DE EC=3.5.1.- {ECO:0000305}; DE AltName: Full=jasmonoyl-L-amino acid hydrolase {ECO:0000305}; DE EC=3.5.1.127 {ECO:0000269|PubMed:24052260}; DE Flags: Precursor; GN Name=ILL4 {ECO:0000303|PubMed:10072397}; GN Synonyms=IAR3 {ECO:0000303|PubMed:10072397}, JR3 GN {ECO:0000303|PubMed:9342878}; GN OrderedLocusNames=At1g51760 {ECO:0000312|Araport:AT1G51760}; GN ORFNames=F19C24.4 {ECO:0000312|EMBL:AAG50883.1}; 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], AND INDUCTION. RX PubMed=9342878; DOI=10.1104/pp.115.2.817; RA Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.; RT "Jasmonic acid-dependent and -independent signaling pathways control wound- RT induced gene activation in Arabidopsis thaliana."; RL Plant Physiol. 115:817-826(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF SER-206; GLY-224; GLY-226 AND ALA-230. RC STRAIN=cv. Columbia; RX PubMed=10072397; DOI=10.1105/tpc.11.3.365; 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] 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 [7] RP FUNCTION, AND 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). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=24052260; DOI=10.1074/jbc.m113.499228; RA Widemann E., Miesch L., Lugan R., Holder E., Heinrich C., Aubert Y., RA Miesch M., Pinot F., Heitz T.; RT "The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine RT hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in RT Arabidopsis leaves."; RL J. Biol. Chem. 288:31701-31714(2013). CC -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth CC regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA- CC Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly (PubMed:10072397, CC PubMed:11923288). Has a lower efficiency with IAA-Phe, IAA-Leu and IAA- CC Val and no activity with IAA-Ile (PubMed:10072397, PubMed:11923288). CC Important for IAA-Leu hydrolysis in roots (PubMed:15155875). Also CC hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy CC jasmonic acid (PubMed:24052260). {ECO:0000269|PubMed:10072397, CC ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:15155875, CC ECO:0000269|PubMed:24052260}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino CC acid; Xref=Rhea:RHEA:52028, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, CC ChEBI:CHEBI:136183, ChEBI:CHEBI:136184; EC=3.5.1.127; CC Evidence={ECO:0000269|PubMed:24052260}; 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 Kinetic parameters: CC KM=90 uM for IAA-Ala {ECO:0000269|PubMed:11923288}; CC Vmax=20 nmol/min/mg enzyme with IAA-Ala as substrate CC {ECO:0000269|PubMed:11923288}; CC Note=kcat is 0.024 sec(-1) with IAA-Ala as substrate. CC {ECO:0000269|PubMed:11923288}; CC pH dependence: CC Optimum pH is 8.0. {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 the vascular tissue of cotyledons and roots, in CC adult leaves, stems, siliques, petals, hydathodes and in silique CC abscission zones and funicles. {ECO:0000269|PubMed:10072397, CC ECO:0000269|PubMed:15155875}. CC -!- INDUCTION: By jasmonic acid (JA) and by wounding. CC {ECO:0000269|PubMed:9342878}. CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y13577; CAA73905.1; -; mRNA. DR EMBL; AF081067; AAC32192.1; -; Genomic_DNA. DR EMBL; AC025294; AAG50883.1; -; Genomic_DNA. DR EMBL; CP002684; AEE32712.1; -; Genomic_DNA. DR EMBL; AF375444; AAK53028.1; -; mRNA. DR EMBL; AY143961; AAN28900.1; -; mRNA. DR PIR; F96556; F96556. DR RefSeq; NP_175587.1; NM_104055.4. DR AlphaFoldDB; O04373; -. DR SMR; O04373; -. DR BioGRID; 26827; 1. DR STRING; 3702.O04373; -. DR ChEMBL; CHEMBL1687678; -. DR MEROPS; M20.A04; -. DR PaxDb; 3702-AT1G51760-1; -. DR ProteomicsDB; 250635; -. DR EnsemblPlants; AT1G51760.1; AT1G51760.1; AT1G51760. DR GeneID; 841602; -. DR Gramene; AT1G51760.1; AT1G51760.1; AT1G51760. DR KEGG; ath:AT1G51760; -. DR Araport; AT1G51760; -. DR TAIR; AT1G51760; IAR3. DR eggNOG; ENOG502QQEM; Eukaryota. DR HOGENOM; CLU_023257_0_0_1; -. DR InParanoid; O04373; -. DR OMA; PECQTMG; -. DR OrthoDB; 3684955at2759; -. DR PhylomeDB; O04373; -. DR BioCyc; ARA:MONOMER-4141; -. DR BioCyc; MetaCyc:MONOMER-4141; -. DR PRO; PR:O04373; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O04373; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009850; P:auxin metabolic process; IEA:InterPro. DR GO; GO:0009611; P:response to wounding; IEP:TAIR. DR CDD; cd08017; M20_IAA_Hyd; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 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 NCBIfam; TIGR01891; amidohydrolases; 1. DR PANTHER; PTHR11014:SF169; IAA-AMINO ACID HYDROLASE ILR1-LIKE 4-RELATED; 1. DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR Genevisible; O04373; AT. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding; KW Reference proteome; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..440 FT /note="IAA-amino acid hydrolase ILR1-like 4" FT /id="PRO_0000045470" FT MOTIF 437..440 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT BINDING 134 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P54970" FT BINDING 134 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" 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 170 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P54970" FT BINDING 194 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P54970" FT BINDING 397 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P54970" FT MUTAGEN 206 FT /note="S->L: In iar3-1; reduces activity." FT /evidence="ECO:0000269|PubMed:10072397" FT MUTAGEN 224 FT /note="G->E: In iar3-2; abolishes activity." FT /evidence="ECO:0000269|PubMed:10072397" FT MUTAGEN 226 FT /note="G->E: In iar3-4; reduces activity." FT /evidence="ECO:0000269|PubMed:10072397" FT MUTAGEN 230 FT /note="A->T: In iar3-3; reduces activity." FT /evidence="ECO:0000269|PubMed:10072397" FT CONFLICT 211 FT /note="M -> I (in Ref. 1; CAA73905)" FT /evidence="ECO:0000305" FT CONFLICT 291 FT /note="A -> AFST (in Ref. 1; CAA73905)" FT /evidence="ECO:0000305" FT CONFLICT 325..329 FT /note="EEEKP -> ARGET (in Ref. 1; CAA73905)" FT /evidence="ECO:0000305" SQ SEQUENCE 440 AA; 48263 MW; 8B605EEF67A1746E CRC64; MSFFKWVSFV LILHLLNPTL ISCSSNGLSQ IPSKFLTLAK RNDFFDWMVG IRRRIHENPE LGYEEVETSK LVRAELEKMG VSYKYPVAVT GVVGYVGTGH APFVALRADM DALAMQEMVE WEHKSKVPGK MHACGHDAHT TMLLGAAKLL KEHEEELQGT VVLVFQPAEE GGGGAKKIVE AGVLENVSAI FGLHVTNQLA LGQVSSREGP MLAGSGFFKA KISGKGGHAA LPQHTIDPIL AASNVIVSLQ HLVSREADPL DSQVVTVAKF EGGGAFNVIP DSVTIGGTFR AFSTKSFMQL KKRIEQVITR QASVNMCNAT VDFIEEEKPF FPPTVNDKAL HQFFKNVSGD MLGIENYVEM QPLMGSEDFS FYQQAIPGHF SFVGMQNKAR SPMASPHSPY FEVNEELLPY GASLHASMAT RYLLELKAST LNKSNKKDEL //