ID   ILL5_ARATH              Reviewed;         435 AA.
AC   Q9SWX9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=IAA-amino acid hydrolase ILR1-like 5 {ECO:0000303|PubMed:10072397};
DE            EC=3.5.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ILL5 {ECO:0000303|PubMed:10072397};
GN   OrderedLocusNames=At1g51780 {ECO:0000312|Araport:AT1G51780};
GN   ORFNames=F19C24.29 {ECO:0000312|EMBL:AAG50869.1};
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. 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   [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   GENE FAMILY.
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).
CC   -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth
CC       regulator indole-3-acetic acid (IAA). {ECO:0000250|UniProtKB:P54968}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; AF085806; AAD48152.1; -; Genomic_DNA.
DR   EMBL; AC025294; AAG50869.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32715.1; -; Genomic_DNA.
DR   PIR; H96556; H96556.
DR   RefSeq; NP_175589.1; NM_104057.1.
DR   AlphaFoldDB; Q9SWX9; -.
DR   SMR; Q9SWX9; -.
DR   STRING; 3702.Q9SWX9; -.
DR   MEROPS; M20.A01; -.
DR   iPTMnet; Q9SWX9; -.
DR   PaxDb; 3702-AT1G51780-1; -.
DR   EnsemblPlants; AT1G51780.1; AT1G51780.1; AT1G51780.
DR   GeneID; 841604; -.
DR   Gramene; AT1G51780.1; AT1G51780.1; AT1G51780.
DR   KEGG; ath:AT1G51780; -.
DR   Araport; AT1G51780; -.
DR   TAIR; AT1G51780; ILL5.
DR   eggNOG; ENOG502QQEM; Eukaryota.
DR   HOGENOM; CLU_023257_0_0_1; -.
DR   InParanoid; Q9SWX9; -.
DR   OMA; KSHSPMA; -.
DR   OrthoDB; 3684955at2759; -.
DR   PhylomeDB; Q9SWX9; -.
DR   BioCyc; ARA:AT1G51780-MONOMER; -.
DR   PRO; PR:Q9SWX9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SWX9; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0010178; F:IAA-amino acid conjugate hydrolase activity; ISS: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:0010112; P:regulation of systemic acquired resistance; 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; Q9SWX9; AT.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..435
FT                   /note="IAA-amino acid hydrolase ILR1-like 5"
FT                   /id="PRO_0000045471"
FT   MOTIF           432..435
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"
SQ   SEQUENCE   435 AA;  47381 MW;  4128504269F23B5A CRC64;
     MSFCKLVSFV LILHLLNSCL ISCSSNDLSQ IPKNFLSLAK REDFFDWMVG IRRRIHENPE
     LGYEEVETSK LVKTELDKMG VSYKNPVAVT GVIGYVGTGH APFVALRADM DALPIQEMVE
     WEHKSKIPGK MHACGHDAHT TMLLGAAKLL KEHQEELQGT VILVFQPAEE GGAGAKKIVE
     AGVLENVGAI FGLHVSNLLG LGQLSSREGL LMAGSGRFKA TISGKGGHAA LPQFAIDPVL
     AASNVILSLQ HLVSREADPL DSQVVTVATF EGSDAFNVIP DSVTIGGTFR ALLPKSFEQL
     KQRIVQVITT QASVNMCNAT VDFLEDETPP FPPTVNNKTL HLFYKNVSVD MLGIENYVET
     LPVMVSEDFA FYQQAIPGHF SFVGMQNKSH SPMANPHSPF FEVNEELLPY GASLLASLAT
     RYLLDSSSSP NKDEL
//