CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006494
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Insulin-degrading enzyme 
Protein Synonyms/Alias
 Insulin protease; Insulinase; Insulysin 
Gene Name
 Ide 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
192AVDSEHEKNVMNDAWacetylation[1]
303EHLKQLYKIVPIKDIacetylation[1]
308LYKIVPIKDIRNLYVacetylation[1]
308LYKIVPIKDIRNLYVubiquitination[2]
364NTLVGGQKEGARGFMacetylation[1]
436RPRGYTSKIAGKLHYacetylation[1]
566LWFKQDDKFFLPKACacetylation[1]
656MATFEIDKKRFEIIKacetylation[1]
713DVTLPRLKAFIPQLLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. 
Sequence Annotation
 NP_BIND 895 901 ATP.
 MOTIF 853 858 SlyX motif.
 ACT_SITE 111 111 Proton acceptor (By similarity).
 METAL 108 108 Zinc.
 METAL 112 112 Zinc.
 METAL 189 189 Zinc.
 BINDING 429 429 ATP.  
Keyword
 3D-structure; Allosteric enzyme; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleotide-binding; Protease; Reference proteome; Secreted; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1019 AA 
Protein Sequence
MRNGLVWLLH PALPSTLHSI LGARPPPVKR LCGFPKQIYS TMNNPAIQRI EDHIVKSPED 60
KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK 120
YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDASCKD 180
REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE 240
LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ 300
LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV 360
GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV 420
AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI 480
VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILAL 540
EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL 600
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKITEKMA TFEIDKKRFE 660
IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL 720
SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ 780
RRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA 840
NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL 900
SAECAKYWGE IISQQYNYDR DNIEVAYLKT LSKDDIIKFY KEMLAVDAPR RHKVSVHVLA 960
REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL 1019 
Gene Ontology
 GO:0009986; C:cell surface; IDA:RGD.
 GO:0031597; C:cytosolic proteasome complex; IDA:RGD.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0005782; C:peroxisomal matrix; IDA:RGD.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; ISS:UniProtKB.
 GO:0016887; F:ATPase activity; IDA:RGD.
 GO:0001540; F:beta-amyloid binding; IPI:RGD.
 GO:0031626; F:beta-endorphin binding; IMP:RGD.
 GO:0043559; F:insulin binding; IMP:RGD.
 GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0050435; P:beta-amyloid metabolic process; ISS:UniProtKB.
 GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
 GO:0008340; P:determination of adult lifespan; IEA:Compara.
 GO:0042447; P:hormone catabolic process; IDA:RGD.
 GO:1901143; P:insulin catabolic process; IEA:Compara.
 GO:0045861; P:negative regulation of proteolysis; IDA:RGD.
 GO:0032461; P:positive regulation of protein oligomerization; IEA:Compara.
 GO:0051291; P:protein heterooligomerization; IDA:RGD.
 GO:0051289; P:protein homotetramerization; IDA:RGD.
 GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:RGD.
 GO:0010992; P:ubiquitin homeostasis; IEA:Compara. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR001431; Pept_M16_Zn_BS.
 IPR007863; Peptidase_M16_C. 
Pfam
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS