ILL6_ARATH
ID ILL6_ARATH Reviewed; 464 AA.
AC Q8VYX0; O81702; Q94LA5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=IAA-amino acid hydrolase ILR1-like 6 {ECO:0000303|PubMed:11923288};
DE EC=3.5.1.- {ECO:0000305};
DE AltName: Full=Protein gr1 {ECO:0000303|Ref.1};
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=ILL6 {ECO:0000303|PubMed:11923288}; Synonyms=GR1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At1g44350 {ECO:0000312|Araport:AT1G44350};
GN ORFNames=T18F15.9 {ECO:0000312|EMBL:AAK43477.1};
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. Wassilewskija;
RA Slusarenko A.J., Gehring T., Kruse C.M., Rempulska Bujas G.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-464, AND GENE FAMILY.
RC STRAIN=cv. Landsberg erecta;
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 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). Also hydrolyzes amino acid
CC conjugates of jasmonic acid and 12-hydroxy jasmonic acid.
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 -!- 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; AJ010735; CAA09330.1; -; Genomic_DNA.
DR EMBL; AC084807; AAK43477.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32032.1; -; Genomic_DNA.
DR EMBL; AY072322; AAL61929.1; -; mRNA.
DR EMBL; AY074380; AAL67076.1; -; mRNA.
DR EMBL; AY117292; AAM51367.1; -; mRNA.
DR EMBL; AY065996; AAL47552.1; -; mRNA.
DR RefSeq; NP_175086.1; NM_103546.4.
DR AlphaFoldDB; Q8VYX0; -.
DR SMR; Q8VYX0; -.
DR STRING; 3702.AT1G44350.1; -.
DR MEROPS; M20.A05; -.
DR PaxDb; Q8VYX0; -.
DR PRIDE; Q8VYX0; -.
DR ProteomicsDB; 228847; -.
DR EnsemblPlants; AT1G44350.1; AT1G44350.1; AT1G44350.
DR GeneID; 841026; -.
DR Gramene; AT1G44350.1; AT1G44350.1; AT1G44350.
DR KEGG; ath:AT1G44350; -.
DR Araport; AT1G44350; -.
DR TAIR; locus:2823614; AT1G44350.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; Q8VYX0; -.
DR OMA; NKGMMHA; -.
DR OrthoDB; 455218at2759; -.
DR PhylomeDB; Q8VYX0; -.
DR BioCyc; ARA:AT1G44350-MON; -.
DR BioCyc; MetaCyc:AT1G44350-MON; -.
DR BRENDA; 3.5.1.127; 399.
DR PRO; PR:Q8VYX0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYX0; baseline and differential.
DR Genevisible; Q8VYX0; AT.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:1990206; F:jasmonyl-Ile conjugate hydrolase activity; IMP: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:0009694; P:jasmonic acid metabolic process; IMP:TAIR.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP: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 1: Evidence at protein level;
KW Hydrolase; Manganese; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..464
FT /note="IAA-amino acid hydrolase ILR1-like 6"
FT /id="PRO_0000045472"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P54970"
FT CONFLICT 66
FT /note="R -> W (in Ref. 5; AAL47552)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="I -> V (in Ref. 1; CAA09330 and 5; AAL47552)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> K (in Ref. 5; AAL47552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50820 MW; F81312BC850D4627 CRC64;
MDNLRKLNLL SVSLTIIFVS LTIATNLPFF EVKYPNNNPF GMLLRPTPIK NQSLGLPAHV
GSDECRVWTK ACSDEILRLT YQPDNVAWLK RVRRTIHENP ELAFEEYETS RLIRSELDRM
GIMYRYPLAK TGIRAWIGSG GPPFVAVRAD MDALPIQEAV EWEHISKVAG KMHACGHDAH
VTMLLGAAHI LKAREHLLKG TVVLLFQPAE EAGNGAKNMI EDGALDDVEA IFAVHVSHIH
PTGVIGSRSG PLLAGCGIFR AVITSEDSRG AANLLLAASS AVISLQGIVS REASPLDSQV
VSVTSFDGGH SLDVAPDTVV LGGTFRAFSN SSFYYLKKRI QEVLMDQVGV FGCQATVNFF
EKQNAIYPPT TNNDATYNHL KKVTIDLLGD SHFTLAPQMM GAEDFAFYSE IIPAAFYFIG
IRNEELGSVH IAHSPHFMID EDSLPVGAAV HAAVAERYLN DKHS
