3.4.24.15: thimet oligopeptidase
This is an abbreviated version!
For detailed information about thimet oligopeptidase, go to the full flat file.
Word Map on EC 3.4.24.15
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3.4.24.15
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angiotensin
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aminopeptidase
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endothelial
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angiotensin-converting
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neuropeptides
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metastasis
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timp
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mmp-9
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metalloproteinase
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neurotensin
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carboxypeptidase
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thrombospondin
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chondrocytes
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cartilage
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osteoarthritis
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endopeptidases
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neurolysin
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disintegrin
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transwell
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enkephalin
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captopril
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natriuretic
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1,10-phenanthroline
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phosphoramidon
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zinc-dependent
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dynorphins
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aggrecan
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bestatin
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ace2
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enkephalinase
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adam17
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hexxh
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i-converting
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gcpii
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endothelin-converting
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thiorphan
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endopeptidase-24.11
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lhrh
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insulin-degrading
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angiotensin-1-7
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post-proline
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adamts1
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enkephalin-containing
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medicine
- 3.4.24.15
- angiotensin
- aminopeptidase
- endothelial
-
angiotensin-converting
- neuropeptides
- metastasis
- timp
- mmp-9
- metalloproteinase
- neurotensin
- carboxypeptidase
- thrombospondin
- chondrocytes
- cartilage
- osteoarthritis
- endopeptidases
- neurolysin
-
disintegrin
-
transwell
- enkephalin
- captopril
-
natriuretic
- 1,10-phenanthroline
- phosphoramidon
-
zinc-dependent
- dynorphins
- aggrecan
- bestatin
- ace2
- enkephalinase
- adam17
-
hexxh
-
i-converting
- gcpii
-
endothelin-converting
- thiorphan
- endopeptidase-24.11
- lhrh
-
insulin-degrading
-
angiotensin-1-7
-
post-proline
- adamts1
-
enkephalin-containing
- medicine
Reaction
Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues =
Synonyms
BIE, bradykinin-inactivating endopeptidase, EC 3.4.22.19, EC 3.4.99.31, endo-oligopeptidase A, endooligopeptidase A, endopeptidase 24-15, endopeptidase 24.15, endopeptidase EC 3.4.24.15, EOPA, EP 24.15, EP24.15, MdpA, metallo-dipeptidase aeruginosa, metalloendopeptidase 24.15, metalloendopeptidase EC 3.4.24.15, metallopeptidase, More, MP78, neutral endopeptidase 24.15, PA4498, peptidase, thimet oligo-, Pz peptidase A, Pz peptidase B, Pz-peptidase, Pz-peptidase A, soluble metallo-endopeptidase, soluble metallopeptidase, thimet oligopeptidase, thimet peptidase, thimet-oligopeptidase, thiol-dependent metalloendopeptidase, THOP1, TOP, Top1, Top2
ECTree
3.4.24.15 thimet oligopeptidaseAdvanced search results
results (
results (Localization
Localization on EC 3.4.24.15 - thimet oligopeptidase
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
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EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space
additional information
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EP24.15 colocalizes with calmodulin in the cytosol of resting HEK293 cells
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activity in cytosol may be significant for regulation of major histocompatibility complex class I expression
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the enzyme form in the extracellular space is significant for neuropeptide processing
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biotinylated enzyme is released into the cell media similar to constitutive release. Secretion inhibitor glyburide decreases the amount of enzyme released into media
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the enzyme is secreted. THOP1 secretion from cultured cells has been shown to occur through an unconventional secretory pathway, and is facilitated by interaction with 14-3-3 epsilon and/or calmodulin, the process is regulated by phosphorylation of THOP1 at Ser644
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the enzyme is secreted. THOP1 secretion from cultured cells has been shown to occur through an unconventional secretory pathway, and is facilitated by interaction with 14-3-3 epsilon and/or calmodulin, the process is regulated by phosphorylation of THOP1 at Ser644
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EP24.15 is predominantly located in the cytoplasm and is secreted into the extracellular space
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intracellular EP24.15 is present throughout the cell, both cytosolic and particulate, with less nuclear localization and no co-localization with either the endoplasmatic reticulum marker calnexin or Golgi marker GM130, overview
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localized between lipid rafts in the plasma membrane, at the exofacial leaflet of lipid rafts. Biotinylated enzyme is released into the cell media similar to constitutive release
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EP24.15 is associated with the extracellular surface of the cell discernable from the secreted enzyme
additional information
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overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium
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additional information
the enzyme shows a broad tissue and subcellular compartment distribution
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additional information
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no activity in membranes of B16F10-Nex2 cells, overview
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additional information
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determination of subcellular localization, fractionation and immunohistochemic analysis, overview
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additional information
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secretion of EP24.15 from AT-t20 cells can be stimulated by A23187 and corticotrophin-releasing hormone and blocked by brefeldin A and nocodazole
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additional information
THOP1 can be secreted or associated to the external surface of the plasma membrane to function as a neuropeptide-degrading enzyme. The amount of THOP1 found in the nucleus is inversely correlated with that found in the cytosol and associated to the cytosolic face of organelles, suggesting that the enzyme can be mobilized from one intracellular compartment to the other. Predominant intracellular localization of THOP1
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additional information
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no activity in membranes of B16F10-Nex2 cells, overview
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additional information
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THOP1 can be secreted or associated to the external surface of the plasma membrane to function as a neuropeptide-degrading enzyme. The amount of THOP1 found in the nucleus is inversely correlated with that found in the cytosol and associated to the cytosolic face of organelles, suggesting that the enzyme can be mobilized from one intracellular compartment to the other. Predominant intracellular localization of THOP1
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additional information
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EP24.15 does not contain a membrane anchoring motif yet it is localised to the extracellular surface of the plasma membrane
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