ID A0A665U7H6_ECHNA Unreviewed; 1015 AA.
AC A0A665U7H6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Insulin degrading enzyme {ECO:0000313|Ensembl:ENSENLP00000014984.1};
GN Name=ide {ECO:0000313|Ensembl:ENSENLP00000014984.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000014984.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000014984.1}
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; A0A665U7H6; -.
DR Ensembl; ENSENLT00000015576.1; ENSENLP00000014984.1; ENSENLG00000006043.1.
DR InParanoid; A0A665U7H6; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000472264; Unplaced.
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:UP000472264};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 72..207
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 234..412
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 418..699
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 702..885
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1015 AA; 117286 MW; 0C2174BB6DBEE73A CRC64;
MFKCIHRTAQ RTRYLQATGT GFCVNKDFRL VSSLQLRMTD PAVKRVVSDI TRSPEDKRVY
RALEFTNGLK AMLISDPTTD KSSAALDVHI GSLSDPGNIS GLAHFCEHML FLGTKKYPKE
NEYSQFLSEH AGSSNAFTSG EHTNYYFDVS HEHLQGALDR FAQFFLCPLF DESCKDREVN
AVDSEHEKNL MNDAWRLFQL EKATGNPNHP FSKFGTGNKL TLETRPSKEG VDIRQELLKF
HSTYYSSNLM GLCVLGRESL DELTSMVVNL FGEVENKNVP VPEFPEHPFQ EEHLRQFYKV
VPIKDIRNLY VTFPIPDLQK YYKSNPGHYL GHLIGHEGPG SLLSELKSKG WVNTLVGGQK
EGAKGFMFFI INVDLTEEGL MHVQDIIFHM FQYIQKLRTE GPQEWVFEEC KDLNKVAFRF
KDKERPRGYT SKVAGLLHYY PLEEVLAAEY LLEDFSPDLI EMVLDKLRPE HVRVAVVSKS
FEGQTDKTEE WYGTQYKQEA ISADVIETWA NADLNGKFKL PMKNEFIPTN FEIYPLEKDP
PSVPTLIKDT AMSKVWFKQD DKFFLPKACL NFEFFSPFAY VDPLHCNMAY LYLELLKDSL
NEYAYAAELA GLNYDLQNTV YGMYLSVKGY SDKQHILLKK IIEKMATFEI DEKRFDIIKE
AYMRSLNNFR AEQPHQHAMY YLRLLMTEVA WTKDELREAL DDVTLPRLKA FIPQLLSRLH
IEALLHGNIT KESALGMMQM VEDTLIEHAH TKPLLPSQLI RYREVQVPDG GWYVYQQRNE
VHNNCGIEIY YQTDMQTTHD NMLLELFCQI ISEPCFNTLR TKEQLGYIVF SGPRRANGVQ
GLRFIMQSEK APHYLESRVE AFLCTMEKAV EEMSEEAFQK HIQALAIRRL DKPKKLSAEC
AKYWGEIISQ QYNFDRDNIE VAYLKTLTKE NIMQFYRERL MVDAPKRHKV SVHVLSREMD
SCPVVGEFPA QNDVNLAPAP SLPQPSLVQD MTEFKRSLPL FPLVKPHINF MAAKL
//
