ILL4_ARATH
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 03-AUG-2022, entry version 146.
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},
GN JR3 {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=10.2307/3870866;
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=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}.
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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.AT1G51760.1; -.
DR ChEMBL; CHEMBL1687678; -.
DR MEROPS; M20.A04; -.
DR PaxDb; O04373; -.
DR PRIDE; O04373; -.
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; locus:2017607; AT1G51760.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; O04373; -.
DR OMA; EWHHPAF; -.
DR OrthoDB; 455218at2759; -.
DR PhylomeDB; O04373; -.
DR BioCyc; ARA:MON-4141; -.
DR BioCyc; MetaCyc:MON-4141; -.
DR PRO; PR:O04373; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04373; baseline and differential.
DR Genevisible; O04373; AT.
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:0016787; F:hydrolase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEP: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 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..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
