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IAA-amino acid hydrolase ILR1-like 4 (EC 3.5.1.-) (jasmonoyl-L-amino acid hydrolase) (EC 3.5.1.127)

 ILL4_ARATH              Reviewed;         440 AA.
O04373; O81642;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
25-APR-2018, entry version 128.
RecName: Full=IAA-amino acid hydrolase ILR1-like 4 {ECO:0000303|PubMed:10072397};
EC=3.5.1.- {ECO:0000305};
AltName: Full=jasmonoyl-L-amino acid hydrolase {ECO:0000305};
EC=3.5.1.127 {ECO:0000269|PubMed:24052260};
Flags: Precursor;
Name=ILL4 {ECO:0000303|PubMed:10072397};
Synonyms=IAR3 {ECO:0000303|PubMed:10072397},
JR3 {ECO:0000303|PubMed:9342878};
OrderedLocusNames=At1g51760 {ECO:0000312|Araport:AT1G51760};
ORFNames=F19C24.4 {ECO:0000312|EMBL:AAG50883.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=9342878; DOI=10.1104/pp.115.2.817;
Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.;
"Jasmonic acid-dependent and -independent signaling pathways control
wound-induced gene activation in Arabidopsis thaliana.";
Plant Physiol. 115:817-826(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-206; GLY-224; GLY-226 AND
ALA-230.
STRAIN=cv. Columbia;
PubMed=10072397; DOI=10.1105/tpc.11.3.365;
Davies R.T., Goetz D.H., Lasswell J.E., Anderson M.N., Bartel B.;
"IAR3 encodes an auxin conjugate hydrolase from Arabidopsis.";
Plant Cell 11:365-376(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
GENE FAMILY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
SUBSTRATE SPECIFICITY.
PubMed=11923288; DOI=10.1074/jbc.M111955200;
LeClere S., Tellez R., Rampey R.A., Matsuda S.P.T., Bartel B.;
"Characterization of a family of IAA-amino acid conjugate hydrolases
from Arabidopsis.";
J. Biol. Chem. 277:20446-20452(2002).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15155875; DOI=10.1104/pp.104.039677;
Rampey R.A., LeClere S., Kowalczyk M., Ljung K., Sandberg G.,
Bartel B.;
"A family of auxin-conjugate hydrolases that contributes to free
indole-3-acetic acid levels during Arabidopsis germination.";
Plant Physiol. 135:978-988(2004).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24052260; DOI=10.1074/jbc.M113.499228;
Widemann E., Miesch L., Lugan R., Holder E., Heinrich C., Aubert Y.,
Miesch M., Pinot F., Heitz T.;
"The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine
hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in
Arabidopsis leaves.";
J. Biol. Chem. 288:31701-31714(2013).
-!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant
growth regulator indole-3-acetic acid (IAA), including IAA-Ala,
IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly
(PubMed:10072397, PubMed:11923288). Has a lower efficiency with
IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile
(PubMed:10072397, PubMed:11923288). Important for IAA-Leu
hydrolysis in roots (PubMed:15155875). Also hydrolyzes amino acid
conjugates of jasmonic acid and 12-hydroxy jasmonic acid
(PubMed:24052260). {ECO:0000269|PubMed:10072397,
ECO:0000269|PubMed:11923288, ECO:0000269|PubMed:15155875,
ECO:0000269|PubMed:24052260}.
-!- CATALYTIC ACTIVITY: A jasmonoyl-L-amino acid + H(2)O = jasmonate +
an L-amino acid. {ECO:0000269|PubMed:24052260}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11923288};
Note=The Mn(2+) ion enhances activity.
{ECO:0000269|PubMed:11923288};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=90 uM for IAA-Ala {ECO:0000269|PubMed:11923288};
Vmax=20 nmol/min/mg enzyme with IAA-Ala as substrate
{ECO:0000269|PubMed:11923288};
Note=kcat is 0.024 sec(-1) with IAA-Ala as substrate.
{ECO:0000269|PubMed:11923288};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:11923288};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138}.
-!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, siliques
and flowers. Detected in the vascular tissue of cotyledons and
roots, in adult leaves, stems, siliques, petals, hydathodes and in
silique abscission zones and funicles.
{ECO:0000269|PubMed:10072397, ECO:0000269|PubMed:15155875}.
-!- INDUCTION: By jasmonic acid (JA) and by wounding.
{ECO:0000269|PubMed:9342878}.
-!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y13577; CAA73905.1; -; mRNA.
EMBL; AF081067; AAC32192.1; -; Genomic_DNA.
EMBL; AC025294; AAG50883.1; -; Genomic_DNA.
EMBL; CP002684; AEE32712.1; -; Genomic_DNA.
EMBL; AF375444; AAK53028.1; -; mRNA.
EMBL; AY143961; AAN28900.1; -; mRNA.
PIR; F96556; F96556.
RefSeq; NP_175587.1; NM_104055.4.
UniGene; At.52138; -.
UniGene; At.5375; -.
ProteinModelPortal; O04373; -.
SMR; O04373; -.
BioGrid; 26827; 1.
STRING; 3702.AT1G51760.1; -.
ChEMBL; CHEMBL1687678; -.
MEROPS; M20.A04; -.
PaxDb; O04373; -.
PRIDE; O04373; -.
EnsemblPlants; AT1G51760.1; AT1G51760.1; AT1G51760.
GeneID; 841602; -.
Gramene; AT1G51760.1; AT1G51760.1; AT1G51760.
KEGG; ath:AT1G51760; -.
Araport; AT1G51760; -.
TAIR; locus:2017607; AT1G51760.
eggNOG; ENOG410IIRP; Eukaryota.
eggNOG; COG1473; LUCA.
HOGENOM; HOG000241403; -.
InParanoid; O04373; -.
KO; K21604; -.
OMA; LAIRTDM; -.
OrthoDB; EOG09360A3R; -.
PhylomeDB; O04373; -.
BioCyc; ARA:AT1G51760-MONOMER; -.
BioCyc; MetaCyc:MONOMER-4141; -.
PRO; PR:O04373; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; O04373; baseline and differential.
Genevisible; O04373; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
InterPro; IPR017439; Amidohydrolase.
InterPro; IPR036264; Bact_exopeptidase_dim_dom.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
SUPFAM; SSF55031; SSF55031; 1.
TIGRFAMs; TIGR01891; amidohydrolases; 1.
PROSITE; PS00014; ER_TARGET; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Hydrolase; Manganese;
Metal-binding; Reference proteome; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 440 IAA-amino acid hydrolase ILR1-like 4.
/FTId=PRO_0000045470.
MOTIF 437 440 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
METAL 134 134 Manganese 1.
{ECO:0000250|UniProtKB:P54970}.
METAL 134 134 Manganese 2.
{ECO:0000250|UniProtKB:P54970}.
METAL 136 136 Manganese 2.
{ECO:0000250|UniProtKB:P54970}.
METAL 170 170 Manganese 1.
{ECO:0000250|UniProtKB:P54970}.
METAL 194 194 Manganese 2.
{ECO:0000250|UniProtKB:P54970}.
METAL 397 397 Manganese 1.
{ECO:0000250|UniProtKB:P54970}.
MUTAGEN 206 206 S->L: In iar3-1; reduces activity.
{ECO:0000269|PubMed:10072397}.
MUTAGEN 224 224 G->E: In iar3-2; abolishes activity.
{ECO:0000269|PubMed:10072397}.
MUTAGEN 226 226 G->E: In iar3-4; reduces activity.
{ECO:0000269|PubMed:10072397}.
MUTAGEN 230 230 A->T: In iar3-3; reduces activity.
{ECO:0000269|PubMed:10072397}.
CONFLICT 211 211 M -> I (in Ref. 1; CAA73905).
{ECO:0000305}.
CONFLICT 291 291 A -> AFST (in Ref. 1; CAA73905).
{ECO:0000305}.
CONFLICT 325 329 EEEKP -> ARGET (in Ref. 1; CAA73905).
{ECO:0000305}.
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


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