ILL5_ARATH
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 03-AUG-2022, entry version 134.
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=10.2307/3870866;
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 [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.AT1G51780.1; -.
DR MEROPS; M20.A01; -.
DR iPTMnet; Q9SWX9; -.
DR PaxDb; Q9SWX9; -.
DR PRIDE; Q9SWX9; -.
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; locus:2017577; AT1G51780.
DR eggNOG; ENOG502QQEM; Eukaryota.
DR HOGENOM; CLU_023257_0_0_1; -.
DR InParanoid; Q9SWX9; -.
DR OMA; KSHSPMA; -.
DR OrthoDB; 455218at2759; -.
DR PhylomeDB; Q9SWX9; -.
DR BioCyc; ARA:AT1G51780-MON; -.
DR PRO; PR:Q9SWX9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SWX9; baseline and differential.
DR Genevisible; Q9SWX9; AT.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0010112; P:regulation of systemic acquired resistance; 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 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
