ID   A0A2K5TUD6_MACFA        Unreviewed;      1053 AA.
AC   A0A2K5TUD6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Insulin degrading enzyme {ECO:0000313|Ensembl:ENSMFAP00000003672.2};
GN   Name=IDE {ECO:0000313|Ensembl:ENSMFAP00000003672.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000003672.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000003672.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000003672.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   AlphaFoldDB; A0A2K5TUD6; -.
DR   STRING; 9541.ENSMFAP00000003672; -.
DR   Ensembl; ENSMFAT00000022333.2; ENSMFAP00000003672.2; ENSMFAG00000001464.2.
DR   VEuPathDB; HostDB:ENSMFAG00000001464; -.
DR   GeneTree; ENSGT00940000155780; -.
DR   Proteomes; UP000233100; Chromosome 9.
DR   Bgee; ENSMFAG00000001464; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0043559; F:insulin binding; IEA:Ensembl.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0140036; F:ubiquitin-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IEA:Ensembl.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR   GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:Ensembl.
DR   GO; GO:0010815; P:bradykinin catabolic process; IEA:Ensembl.
DR   GO; GO:0042447; P:hormone catabolic process; IEA:Ensembl.
DR   GO; GO:1901143; P:insulin catabolic process; IEA:Ensembl.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:1903715; P:regulation of aerobic respiration; IEA:Ensembl.
DR   GO; GO:0010992; P:ubiquitin recycling; IEA:Ensembl.
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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          74..212
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          238..416
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          422..702
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          706..830
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1053 AA;  121962 MW;  83B10AF7025095EC CRC64;
     MRYRLAWLRH PALPTTFRSV FGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED
     KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK
     YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD
     REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE
     LLKFHSTYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KSVPLPEFPE HPFQEEHLKQ
     LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV
     GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV
     AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI
     VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL
     EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL
     KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE
     IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL
     SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRWFVYQQ
     RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGA GHGKWMLWMV
     LPFEELTVKS GWQACKGIIL VQHGYIVFSG PRRANGIQGL RFIIQSEKPP HYLESRVEAF
     LITMEKSIED MTEEAFQKHI QALAIRRLDK PKKLSAECAK YWGEIISQQY HFDRDNTEVA
     YLKTLTKEDI IKFYKEMLAV DAPRRHKVSV HVLAREMDSC PVVGEFPCQN DINLSQAPAL
     PQPEVIQNMT EFKRGLPLFP LVKPHINFMA AKL
//