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Database: UniProt
Entry: A0A4S2L249_9HYME
LinkDB: A0A4S2L249_9HYME
Original site: A0A4S2L249_9HYME 
ID   A0A4S2L249_9HYME        Unreviewed;       476 AA.
AC   A0A4S2L249;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Insulin-degrading enzyme {ECO:0000313|EMBL:TGZ56631.1};
DE   Flags: Fragment;
GN   ORFNames=DBV15_12523 {ECO:0000313|EMBL:TGZ56631.1};
OS   Temnothorax longispinosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Temnothorax.
OX   NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ56631.1, ECO:0000313|Proteomes:UP000310200};
RN   [1] {ECO:0000313|EMBL:TGZ56631.1, ECO:0000313|Proteomes:UP000310200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:TGZ56631.1};
RX   PubMed=30967075;
RA   Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA   Bornberg-Bauer E., Foitzik S.;
RT   "Ant behaviour and brain gene expression of defending hosts depend on the
RT   ecological success of the intruding social parasite.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TGZ56631.1}.
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DR   EMBL; QBLH01000312; TGZ56631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2L249; -.
DR   STRING; 300112.A0A4S2L249; -.
DR   Proteomes; UP000310200; 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; 2.
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; 1.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000310200};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          3..130
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          350..471
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   NON_TER         476
FT                   /evidence="ECO:0000313|EMBL:TGZ56631.1"
SQ   SEQUENCE   476 AA;  55713 MW;  696D4F1514B2D017 CRC64;
     MKILLISDSK TDISIAAINV NIGSKHDPDD LPGLAHLCEH MLHMGTEEYP QQNNFAEYVS
     QSGGRINADT HFKFTSYYFN IIPKKLKGAL DRFAQFFIAP FFRKDLIEKE INNIHSEYNE
     RLTDDEWRFE QALVKLSIKP DHPYSKLNIG NKKTLNETPK KDNIDVKDRL KKFYEKYYSA
     NIMSLCILSK DGLNNLKNMV IKRFRNVKNK ELPVYSGCPF KDDDFNTVWL HVPIGYIRKL
     DVTFAFSEKR EDQMSLKYIK HLLRHKSEGS LLSALKAKSL CNNIEAGDYP VDTNIHFFKV
     KFHLTKKGLE DSTDIVEIMF QYINMLKKNE PKKLIYDVIK IQQMSDINNR YNEKIHCLSV
     DDISKITCCM QECPMKEIFS KQRAWQSYLI KDLIKEYFTP QNIRIYIATK ACESETDERE
     EWYNIKYFKG KIPEGHMKSF NRAADAADSS TELKLPLKNT FIPMKFDIKN ETNKII
//
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