IDE1_ARATH
ID IDE1_ARATH Reviewed; 970 AA.
AC O22941; Q0WVU4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Insulin-degrading enzyme-like 1, peroxisomal;
DE EC=3.4.24.-;
DE AltName: Full=Insulysin-like 1;
DE AltName: Full=Peroxisomal M16 protease;
DE AltName: Full=Zinc-metallopeptidase;
GN Name=PXM16; OrderedLocusNames=At2g41790 {ECO:0000312|Araport:AT2G41790};
GN ORFNames=T11A7.11 {ECO:0000312|EMBL:AAC02769.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15333753; DOI=10.1104/pp.104.043695;
RA Reumann S., Ma C., Lemke S., Babujee L.;
RT "AraPerox. A database of putative Arabidopsis proteins from plant
RT peroxisomes.";
RL Plant Physiol. 136:2587-2608(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17592111; DOI=10.1073/pnas.0704733104;
RA Helm M., Lueck C., Prestele J., Hierl G., Huesgen P.F., Froehlich T.,
RA Arnold G.J., Adamska I., Goerg A., Lottspeich F., Gietl C.;
RT "Dual specificities of the glyoxysomal/peroxisomal processing protease
RT Deg15 in higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11501-11506(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19748917; DOI=10.1104/pp.109.142505;
RA Lingard M.J., Bartel B.;
RT "Arabidopsis LON2 is necessary for peroxisomal function and sustained
RT matrix protein import.";
RL Plant Physiol. 151:1354-1365(2009).
CC -!- FUNCTION: Peptidase that might be involved in pathogen or wound
CC response. Not required for peroxisome biogenesis, indole-3-butyric acid
CC (IBA) metabolism, fatty acid beta-oxidation or degradation of
CC glyoxylate cycle enzymes during seedling development.
CC {ECO:0000269|PubMed:19748917}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15333753}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, and full processing of
CC glyoxysomal precursor proteins. {ECO:0000269|PubMed:17592111,
CC ECO:0000269|PubMed:19748917}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AC002339; AAC02769.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10033.1; -; Genomic_DNA.
DR EMBL; AK226643; BAE98754.1; -; mRNA.
DR PIR; B84846; B84846.
DR RefSeq; NP_181710.1; NM_129743.4.
DR AlphaFoldDB; O22941; -.
DR SMR; O22941; -.
DR IntAct; O22941; 1.
DR STRING; 3702.AT2G41790.1; -.
DR MEROPS; M16.A02; -.
DR iPTMnet; O22941; -.
DR PaxDb; O22941; -.
DR PRIDE; O22941; -.
DR ProteomicsDB; 228791; -.
DR EnsemblPlants; AT2G41790.1; AT2G41790.1; AT2G41790.
DR GeneID; 818778; -.
DR Gramene; AT2G41790.1; AT2G41790.1; AT2G41790.
DR KEGG; ath:AT2G41790; -.
DR Araport; AT2G41790; -.
DR TAIR; locus:2054346; AT2G41790.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_1_1; -.
DR InParanoid; O22941; -.
DR OMA; INQVMEH; -.
DR OrthoDB; 1008844at2759; -.
DR PhylomeDB; O22941; -.
DR PRO; PR:O22941; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22941; baseline and differential.
DR Genevisible; O22941; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Peroxisome; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..970
FT /note="Insulin-degrading enzyme-like 1, peroxisomal"
FT /id="PRO_0000403450"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT ACT_SITE 143
FT /evidence="ECO:0000305"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="H -> R (in Ref. 3; BAE98754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 970 AA; 110995 MW; D37CC2EAD07374E9 CRC64;
MAVEKSNTTV GGVEILKPRT DNREYRMIVL KNLLQVLLIS DPDTDKCAAS MSVSVGSFSD
PQGLEGLAHF LEHMLFYASE KYPEEDSYSK YITEHGGSTN AYTASEETNY HFDVNADCFD
EALDRFAQFF IKPLMSADAT MREIKAVDSE NQKNLLSDGW RIRQLQKHLS KEDHPYHKFS
TGNMDTLHVR PQAKGVDTRS ELIKFYEEHY SANIMHLVVY GKESLDKIQD LVERMFQEIQ
NTNKVVPRFP GQPCTADHLQ ILVKAIPIKQ GHKLGVSWPV TPSIHHYDEA PSQYLGHLIG
HEGEGSLFHA LKTLGWATGL SAGEGEWTLD YSFFKVSIDL TDAGHEHMQE ILGLLFNYIQ
LLQQTGVCQW IFDELSAICE TKFHYQDKIP PMSYIVDIAS NMQIYPTKDW LVGSSLPTKF
NPAIVQKVVD ELSPSNFRIF WESQKFEGQT DKAEPWYNTA YSLEKITSST IQEWVQSAPD
VHLHLPAPNV FIPTDLSLKD ADDKETVPVL LRKTPFSRLW YKPDTMFSKP KAYVKMDFNC
PLAVSSPDAA VLTDIFTRLL MDYLNEYAYY AQVAGLYYGV SLSDNGFELT LLGYNHKLRI
LLETVVGKIA NFEVKPDRFA VIKETVTKEY QNYKFRQPYH QAMYYCSLIL QDQTWPWTEE
LDVLSHLEAE DVAKFVPMLL SRTFIECYIA GNVENNEAES MVKHIEDVLF NDPKPICRPL
FPSQHLTNRV VKLGEGMKYF YHQDGSNPSD ENSALVHYIQ VHRDDFSMNI KLQLFGLVAK
QATFHQLRTV EQLGYITALA QRNDSGIYGV QFIIQSSVKG PGHIDSRVES LLKNFESKLY
EMSNEDFKSN VTALIDMKLE KHKNLKEESR FYWREIQSGT LKFNRKEAEV SALKQLQKQE
LIDFFDEYIK VGAARKKSLS IRVYGSQHLK EMASDKDEVP SPSVEIEDIV GFRKSQPLHG
SFRGCGQPKL
