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Database: UniProt
Entry: A0A3M0KEE0_HIRRU
LinkDB: A0A3M0KEE0_HIRRU
Original site: A0A3M0KEE0_HIRRU 
ID   A0A3M0KEE0_HIRRU        Unreviewed;      1021 AA.
AC   A0A3M0KEE0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Insulin-degrading enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DUI87_11652 {ECO:0000313|EMBL:RMC11532.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC11532.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC11532.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC11532.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC11532.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RMC11532.1}.
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DR   EMBL; QRBI01000108; RMC11532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0KEE0; -.
DR   STRING; 333673.A0A3M0KEE0; -.
DR   Proteomes; UP000269221; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          80..216
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          243..421
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          427..629
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          632..751
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          755..938
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1021 AA;  118501 MW;  4C083A7C3DA7177A CRC64;
     MRQRLFPVLS RALPGWTRPW AAPASRSFPQ GRRRSSLGFQ KETNNKMNNP AIKRITNEII
     KSPEDKREYR GLELANGIKA LLISDPTTDK SSAALDVHIG SLSDPPNIAG LSHFCEHMLF
     LGTKKYPKEN EYSQFLSEHA GSSNAFTSGE HTNYYFDVSH EHLEGALDRF AQFFLCPLFD
     ESCKDREVNA VDSEHEKNLM NDAWRLFQLE KATGNPNHPF SKFGTGNKFT LETRPTQEGI
     DVRQELLKFH STYYSSNLMA ICVLGRESLD ELTCLVMKLF SEVENKNVPI PEFPEHPFQE
     EHLRQLYKVV PIKDIRNLYV TFPIPDLQKY YKSNPGHYLG HLIGHEGPGS LLSELKAKGW
     VNTLVGGQKE GARGFMFFII NVDLTEEGLL HVEDIILHMF QYIQKLRTEG PQEWVFQECK
     DLNAVAFRFK DKERPRGYTS KLGGMLHYYP IEEVLAAEYL LEEFRPDLIE MVLDKLRPEN
     VRVAIVSKSF EGKTDRTEEW YGTQYKQEAI SDEKWQNADL NGKFKLPMKN EFIPTNFEIL
     PLEKDATQYP ALIKDTAMSK LWFKQDDKFF LPKACLNFEF FSPFAYVDPL HCNMAYLYLE
     LLKDSLNEYA YAAELAGLNY DLQNTIYGIR YIYADPLHCN MTYLFIRLLK DDLKEYTYAA
     RLSGLVYGIA SGMNAILLSV KGYNDKQHIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN
     NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIAQLLS RLHIEALLHG
     NITKQAALGI TQMVEDTLIE HAHTKPLLPS QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI
     EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTQEQLGY IVFSGPRRAN GIQGLRFIIQ
     SEKPPHYLES RVEAFLKTME KCIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI
     ISQQYNFDRD NIEVAYLKTL TKDDIIQFYK PSVIENMTEF KRSLPLFPLV KPHINFMAAK
     L
//
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