ID   A0A2A3E5Y3_APICC        Unreviewed;      1001 AA.
AC   A0A2A3E5Y3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:PBC27147.1};
GN   ORFNames=APICC_04290 {ECO:0000313|EMBL:PBC27147.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC27147.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC27147.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC27147.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KZ288357; PBC27147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3E5Y3; -.
DR   STRING; 94128.A0A2A3E5Y3; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
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; 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:UP000242457};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          39..176
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          203..381
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          387..668
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          672..836
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1001 AA;  116471 MW;  AA93C80B0F72FF4A CRC64;
     MKITANMANN FIEKQYNNII KSPNDKREYR GLLLNNKMKV LLISDATTDK SAAALNVNIG
     YLSEPDDLLG LAHFCEHMLF LGTEKYPEKN DYNKYLSQNG GSYNASTHMD HTLYYFDVHA
     EKLRDALDRF AQFFIAPLFT EALTDLELNA IHLECEKNIA NDTWRLDQLE KSSADPNHPF
     SRFATGNKET LDIIPKQKGI NVREKLLEFH NKFYSSNIMA LCVLGKESLN ELEKMVVELF
     SQVKNKEIPV PTWPKHPFNE QHFQHKWYIV PIKDIRSLYI IFPIPDLREH YKSAPAHYIS
     HLLGHEGEGS LLSLLKAKGW CNSLGSGKRL GARGFSFFVV FVDLTEEGIQ HIDDIVLLTF
     QYINMLKKNG PIEWIYNEYK DVANINFRFK EKSYPCDYVS GLAQILYDYP IEDILIVEHL
     FLLWKPDLIK CIMEFLKPEN VRIHIVGKLF ENITDETEKW YGVKFKKEKI SPDIINKWIN
     AGLNADLKLP PKNEFIPEKF DIKPIGDKTS KFPVIIEDTS LIRLWFKQDE EFLIPKANLF
     LDFVSPLAYL DPLSYNLTYI FVLLFRDALN EFAYAADIVG LKWELTNSKY GMTLGIVGYD
     DKQRVLLDKI IDKMLNFKVD RKRFAIWKEN YSRSLKNYKA EQPYQHAVYY LAVLLSEQIW
     MKDELLNALS HLTVEKVENF IPQFLSKIHM ECLIHGNMTM SEAIETARLI ESKLSNAIPH
     IIPLLSRQLI LHREIKLEDG CHFLFEVQTK YHSSSCTQIY CQTGLQSTES NMLLELLAQI
     LSEPCFTTLR TKEQLGYIVF SGVRRTNGAQ GLRIIVQSDR HPKYVEQRIH TFLNSMLVKF
     TFKLNIFQQN ISSMTEEEFN AHKESLAIRR LEKPKQMTTL SSIFWNEIVS QQYNFDRANI
     EVAYLRTITK EQILEFYKNI LQNDIQRKLS VHVISTLKDQ NSNNEKAVES NKNTEQSNEI
     NNTIEYKKID DILSFKISQN LYSLPKPFTD VPRKGVHSSK L
//