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0IDE_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameIDE
DescriptionInsulin-degrading enzyme (ec 3.4.24.56) (insulysin) (insulinase) (insulin protease).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005615 extracellular space (TAS)
0005777 peroxisome (TAS)
0005625 soluble fraction (TAS)
0003824 catalytic activity (TAS)
0004231 insulysin activity (TAS)
0004871 signal transducer activity (TAS)
0006508 proteolysis and peptidolysis (TAS)
0007548 sex differentiation (TAS)
0007165 signal transduction (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are His.lu.sp or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as abXHEbbHbc.here a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. The majority of the sequences in this entry are metallopeptidases and non-peptidase homologs belong to MEROPS peptidase family M16 (clan ME).ubfamilies M16A.16B and M16C; they include:Insulinase.nsulin-degrading enzyme ()Mitochondrial processing peptidase alpha subunit.Alpha-MPP.Pitrlysin.rotease III precursor ()Nardilysin.)Ubiquinol-cytochrome C reductase complex core protein I.itochondrial precursor ()Coenzyme PQQ synthesis protein F ()These proteins do not share many regions of sequence similarity; the most noticeable is in the N-terminal section. This region includes a conserved histidine followed.wo residues later by a glutamate and another histidine. In pitrilysin.t has been shown that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity.The proteins classified as non-peptidase homologues either have been found experimentally to be without peptidase activity.r lack amino acid residues that are believed to be essential for the catalytic activity.
  IPR011765:Peptidase M16, N-terminal
These metallopeptidases belong to MEROPS peptidase family M16 (clan ME). They include proteins.hich are classified as non-peptidase homologues either have been found experimentally to be without peptidase activity.r lack amino acid residues that are believed to be essential for the catalytic activity. The peptidases in this group of sequences include:Insulinase.nsulin-degrading enzyme ()Mitochondrial processing peptidase alpha subunit.Alpha-MPP.Pitrlysin.rotease III precursor ()Nardilysin.)Ubiquinol-cytochrome C reductase complex core protein I.itochondrial precursor ()Coenzyme PQQ synthesis protein F ()These proteins do not share many regions of sequence similarity; the most noticeable is in the N-terminal section. This region includes a conserved histidine followed.wo residues later by a glutamate and another histidine. In pitrilysin.t has been shown that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity. The mitochondrial processing peptidase consists of two structurally related domains. One is the active peptidase whereas the other.he C-terminal region.s inactive. The two domains hold the substrate like a clamp .
  IPR007863:Peptidase M16, C-terminal
IPR011765:Peptidase_M16 
Evalue:-66.6197891235352 
Location:73-211IPR007863:Peptidase_M16_C 
Evalue:-33.9586067199707 
Location:235-417IPR007863:Peptidase_M16_C 
Evalue:-19.4202156066895 
Location:705-888
SequencesProtein: IDE_HUMAN (1018 aa)
mRNA: NM_004969
Local Annotation
Synapse Ontology
transmitter inactivated by its enzyme etc.
sdb:0141 extracellular metabolism  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01408
  Level 3 annotation:
    insulysin
  Level 2 annotation:
    Alzheimer's disease
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 86 residues, 94204020-94204276Exon2: 24 residues, 94205312-94205380Exon3: 26 residues, 94206095-94206168Exon4: 22 residues, 94210927-94210989Exon5: 93 residues, 94213467-94213740Exon6: 58 residues, 94215412-94215580Exon7: 39 residues, 94218615-94218727Exon8: 32 residues, 94219990-94220082Exon9: 42 residues, 94224577-94224698Exon10: 39 residues, 94225620-94225731Exon11: 50 residues, 94229013-94229158Exon12: 29 residues, 94232991-94233074Exon13: 43 residues, 94236932-94237055Exon14: 36 residues, 94240229-94240332Exon15: 36 residues, 94254530-94254634Exon16: 29 residues, 94256178-94256259Exon17: 32 residues, 94257311-94257403Exon18: 33 residues, 94257849-94257942Exon19: 56 residues, 94258464-94258627Exon20: 39 residues, 94259786-94259899Exon21: 43 residues, 94264656-94264779Exon22: 58 residues, 94281484-94281654Exon23: 71 residues, 94284314-94284522Exon24: 63 residues, 94287102-94287287Exon25: 53 residues, 94323658-94323813Exon26: 2 residues, -Jump to IDE_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2626 94342970-94405130 ~-62K 5333(KIF11)(+)Loci: 3908 94204020-94323813 ~-120K 5332(IDE)(-)Link out to UCSC