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Database: UniProt
Entry: B3S2Y5_TRIAD
LinkDB: B3S2Y5_TRIAD
Original site: B3S2Y5_TRIAD 
ID   B3S2Y5_TRIAD            Unreviewed;       940 AA.
AC   B3S2Y5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_28404 {ECO:0000313|EMBL:EDV22870.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22870.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV22870.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22870.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; DS985248; EDV22870.1; -; Genomic_DNA.
DR   RefSeq; XP_002114736.1; XM_002114700.1.
DR   AlphaFoldDB; B3S2Y5; -.
DR   STRING; 10228.B3S2Y5; -.
DR   MEROPS; M16.008; -.
DR   EnsemblMetazoa; TriadT28404; TriadP28404; TriadG28404.
DR   GeneID; 6755781; -.
DR   KEGG; tad:TRIADDRAFT_28404; -.
DR   CTD; 6755781; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; B3S2Y5; -.
DR   OMA; WIFDEMK; -.
DR   OrthoDB; 129328at2759; -.
DR   PhylomeDB; B3S2Y5; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          36..173
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          200..378
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          384..664
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          669..851
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   940 AA;  108532 MW;  4ABF5C32798BD3A8 CRC64;
     MEKVIDPRVL RASDNIIRSA EDKRLYRSLQ LSNHIKVILV QDDKADKAAA SLDVHIGHLM
     DPPELPGLAH FCEHMLFLGT EKYPLENGFS QFLSEHSGSS NAFTSAEHTN YYFEVATQYL
     QEALDRFSQF FIAPLFNADS KDREVKAINS ENDNNKKSDL WRLSQLDKST CKPSHPFSKF
     GTGNLYTLGT RALEKKIDVR EELLKFHSQY YSANLMTLAI VSKESLDDLS KIAIECFSSI
     VDKNILKPEF NDHPYGADEL QTKFCVVPIK DTPIIELLFP LPDMSEHYTS KPCHYIAHLV
     GHEGSGSLLS LLKSKGWINT LQAGAKHGAK GFMFFMISCK LTEEGFNHLN EIISYIFQYL
     TLLRNSGPQE WIFTECQNLG EMNFRFKDRE RPQGYAVYLA SSLQKYPLEE VLCAQFLMQS
     YSPDIIKEVL DHLRPESFRL FVISPKFEDI ADKTEEWYGT RYKEEKIPLD LIQSWAEVGE
     TDGLNLPRRN EFIPTDFDIK KSSDKPTQYP TIIKEDSLSK TWFKQDNSFF LPKACFCFDI
     TSPFTYVDPA HFNMTRLFVT LVMDSLNEFA YDAEIAGISY ILHATFYGIQ LIIRGYNDKQ
     KVLLSKILNE VAQFKIDPKR FLIIKNEYKR QLLNFKAEKP YMHAAYYVNY LLEDTFWTND
     DLSDALDDIS CEQVQAFIPL FLSRLYIEAL LMGNLTQEEA IEISTLVCSV FRDCAGTKAL
     LPSQRMKHRQ IQLQDGCSYL FEVVNDVHPS SCIEVYYQYG LQSTTTNSLI ELFCQVINEP
     CFDILRTKEQ LGYIVFSGVR RAHGAQGLRV LVQSDHNPAF VESRIEAFMV SMKEHLELLT
     EENFRKHLNA LIIRKSEKPK KLNEECHRYF SEIVSRQYNF DRDNIEINYL KTVNKTELLQ
     FYMDLIEKDA PKRKKLSVRV VSRKVAGKSA YVHFSVCNIS
//
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