| Tag | Content |
|---|
| CPLM ID | CPLM-021724 |
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 | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 308 | LYKIVPIKDIRNLYV | acetylation | [1] | | 436 | RPRGYTSKIAGKLHY | acetylation | [1] |
|
Reference | [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome. Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ. Mol Cell. 2013 Jan 10;49(1):186-99. [ PMID: 23201123] |
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 (By similarity). |
Sequence Annotation | NP_BIND 895 901 ATP (By similarity).
MOTIF 853 858 SlyX motif.
ACT_SITE 111 111 Proton acceptor (By similarity).
METAL 108 108 Zinc (By similarity).
METAL 112 112 Zinc (By similarity).
METAL 189 189 Zinc (By similarity).
BINDING 429 429 ATP (By similarity). |
Keyword | Allosteric enzyme; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; 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 PALPGTLRSI LGARPPPAKR LCGFPKQTYS TMSNPAIQRI EDQIVKSPED 60
KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK 120
YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLLDASCKD 180
REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE 240
LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLRQ 300
LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GYYLGHLIGH EGPGSLLSEL KSKGWVNTLV 360
GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV 420
AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI 480
VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILSL 540
EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL 600
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKRYNDKQPI LLKKITEKMA TFEIDKKRFE 660
IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL 720
SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ 780
QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA 840
NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL 900
SAECAKYWGE IISQQYNYDR DNIEVAYLKT LTKDDIIRFY QEMLAVDAPR RHKVSVHVLA 960
REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL 1019 |
Gene Ontology | GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:MGI. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; ISS:UniProtKB. GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB. 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:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |