ID A0A4S2KXE9_9HYME Unreviewed; 1766 AA.
AC A0A4S2KXE9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=DBV15_09984 {ECO:0000313|EMBL:TGZ52919.1};
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:TGZ52919.1, ECO:0000313|Proteomes:UP000310200};
RN [1] {ECO:0000313|EMBL:TGZ52919.1, ECO:0000313|Proteomes:UP000310200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:TGZ52919.1};
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}.
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:TGZ52919.1}.
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DR EMBL; QBLH01001145; TGZ52919.1; -; Genomic_DNA.
DR STRING; 300112.A0A4S2KXE9; -.
DR Proteomes; UP000310200; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 8.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
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; 4.
DR Pfam; PF16187; Peptidase_M16_M; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 8.
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 386..514
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 536..818
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 823..987
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 1026..1126
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 1167..1344
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 1361..1467
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 1519..1634
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1766 AA; 207070 MW; 5D6FF458EE1C016D CRC64;
MLLTEQHWLN DELLKSTAHL SDXELKDELK LFIRKLFSQM HIECLIYGNV SEEEATENKV
LKTSSTIVYY ETGLQSKWML SLLLNQIIKQ PCVDFLKTTK KLGYTVFSEI CRMMNRTQYL
KIFVRGDHPP QYVEEQIDLF MDFMLNHISA MSEEQFGKHK ESLKLYLHLT APNTISSQGS
LYWEEIERQE YNFNRLNTEV PYLMNEITQQ QLLQFFTVXT YFYKRTISFN EKEKENILSK
LTRRKLSVHV MPTAIAKEKN LPDTSRRITV TSSNNEIKKF DNLMSFKLSQ SLYPLLKPID
KNVVRKGICS SMINNIFESA ALVTNMSNHN CVEEQFDNIH PDNDSRSYRG LVLTNKMRIF
LISDPSTDIS FASMDVNAEN KEVELPMYSE YPFKDEDFNT IWYYVPIHDT ITQLVISFAL
PEMQREYRMP LDYIAHLFKH KSEGLLVSAL KARGWCNTII AGKDSADTSI HYFKVIFELT
EKGIKHXEDI ILIMFQYINM LKKNGPMKWI YDEHLHIWNM CNRYKNSKIH SWNPNNIATI
AYLLHIYPME NIISLLRDFP KWRPDLINEL MEYFTPQNIR IYVAAKAYES IANKTEKWFG
TKYMKEKISE KTMKMWNHAG YKLPDLKLPS KNEFIATKFD IKTKINDQKF PLRVVKDTSF
VKVWYKEDNV FRLPHATMIF HFVSPFAYMD PLSSNLTNMF VNLLCDFLDE YACIVNIHKH
EFMHTVDITS LEWKITTTKY GITLKIDGFD DKQRVLLEKI MDQMTNFKLN PKRFEVLKET
HIKYLKNFAA ILQTPKHAKE YLHILLSERH WSNDELLAST AHLSIDRLEL FIPKLFSKMH
VECLMYGNVT EMEATNIGEL IESNLKTRMP HIVPMLQEQL VLYRQIKIDD GCHILYEEEN
KVHENSCTIV NYATGLRSTE SNMLLLLLAQ IISGPCYDIL RTTEQLGYII LGDVCTINET
QYLTVVIQGE RNPQNVEERI DSFMENMFSE RAKSCTRQLA APVPVARVAS LANHEAQYIG
RKSFKHDPDD LPGLAHLCEH MLLLGTKEYP QQNDYNEYLS QYGGWDNATT KLNCTNYYFN
IIPKKLEGAL DIFAQFFIAP LFSETLIEKV INGAIHPEHE EYLTKDIQLL YQLHKLSVKP
DHPYSKFSTG TRETLSKIPK EKNINVRNRL LEFYDIYYSA NIMSLCILSK DGLDDLENMV
VKRFRNVKNK EVELPVYSEY PFKDEDFNTI WYYIPIHDIR YLDISFALPE KQHEHRMPLK
YIKHLLAHES KGSLSSALKA KGWCDYVGNR DVSADTSVHF FTVVFNLTEE GINHVEDIVQ
IMFQYINMLK KNGPIKWIYD EIQQISNINN TYNENIHRLS HEHISKIAYR LHECPMEEIF
LKQRAWRPDL IEELMEYFTP QNIRIYVAAK AYESITNKTE KWYDVKYKKE KISQKAIEIW
NHAGYNTDLK LPPKNEFIAA KFDIKTETNT GLIYGNVTKM EATDIGELIE CNLKTRMPHI
VPLWQKQLVL YREIKLEDGC HVLFEEESKV QKTFSTIVYY ATGLRSTESN MLLSLLNQII
DQPCFDILRT TEELGYEVFS RICAINETQY LTVVVQGDHR PQNVEQRIDS FMDSMFDHIS
TMSEEHFDNH KKSLVSLYLK APKTISSQGS LYWEEIGSQV YNFNRVNIEK EYLNTITQQQ
LLQFFKENVH SNLTRRKLSV HVMPTAMAAE RNLPDTFRKI TVTSSDNKIK KFDNLMSFKL
SQSLYPLLEP IDKNVIRKGI RCSSKV
//
