ID   K1R5G5_CRAGI            Unreviewed;      1019 AA.
AC   K1R5G5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:EKC36445.1};
GN   ORFNames=CGI_10018507 {ECO:0000313|EMBL:EKC36445.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC36445.1};
RN   [1] {ECO:0000313|EMBL:EKC36445.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC36445.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; JH816392; EKC36445.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1R5G5; -.
DR   MEROPS; M16.008; -.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; K1R5G5; -.
DR   OMA; WIFDEMK; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 5.
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; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 5.
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          8..146
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..349
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          356..598
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          600..700
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          705..884
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1019 AA;  117333 MW;  4DE0BBEAFB396736 CRC64;
     MKLNNGLKVV LVSDPDTDKA SAALDVHVGF MKDPKDLPGL AHFCEHMLFL GTKKYEEENA
     YNKFLSEHGG MSNAYTSSEN TNYFFDVRSE NLPGALDRFA QFFLCPLFTP SATDREVNAV
     NSENDKNLQQ DPWRFNMLDK ALGNPDHEFT SYGTGNKDTL DTIPKSKGIN TRDELLKFHS
     KYYSSNIMSL AVLGKESLDE LSEMVAPLFS PVENKSVEIP FWSEGPYGPE HVKKIFYAVP
     VKDLRNLSVS WTIPDLSDYY SSNPGHILGH LIGHEGRGSL LSELKQKGWV NSLCGGQTDG
     ANGFMFFRID FDLSEEGLEH VDDILLMMFQ YIEMLRKEGP QEWVYKECQQ LSDMIFRFKD
     KEKPINYTSF LARRMQKYPL PEVLSGSYLL TEYRPDLITM VLDKLVPETM RIGVIAKKFA
     DIADQKEKWY GTEYKLEDIP DEKIKKWKNC GLTENLHLPP RNEFIPTNFE VVPREKDSSA
     LPEMIKETGL SRLWFKQDDK FLLPKACLSF DISSPIAYTD PLNCNMAGLF TELFKDALNE
     YAYDAELAGL SYDLMNTVCG MVLQVKGYHE KQPVLLRKIL EKLTDFKVDP KRFEIYKEMD
     ALNEYAYDAE LAGLSYDLMN TVCGMVLQVK GYHEKQPVLL RKILEKLTDF KVDPKRFEIY
     KEMYMRGLRN FYAEEPYQHS IYYTNNLMAE IQWTKAELLQ SAAEVTAEKL QEFIPNLLSK
     LFIEALIYGN VTKQQAKEVM EMTEGILKEK CGTKELLPSQ YKRYREVQIP DGCYYLYQTD
     NKVHKSSSIC IYYQCGMQDT LPNMLLELLV QILAEPCFNI LRTKEQLGYI VFSGVRRARG
     VQGLRVIIQS DRPPQYVDDR VEAFLNHMET VIRDMSQEEY DKHVGALATK RMEKTKKINE
     QNMKYWSEII SNTYNFDRDE IEVACLKTVK KDDLIMFFKD FVAINAPHRH KLSIHIMPSS
     EELNTNTVSP EDNGADLLPV PTNLPKPCVV DDIADFKRHL GLYPLPKPFI DIGKAKSKL
//