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Details on Person Thimet oligopeptidase (THOP1, EP24.15) is a zinc-dependent p...

Class:IdSummation:8940621
_displayNameThimet oligopeptidase (THOP1, EP24.15) is a zinc-dependent p...
_timestamp2017-01-12 13:18:02
created[InstanceEdit:8940602] Jupe, Steve, 2016-09-27
literatureReference[LiteratureReference:8940633] Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
[LiteratureReference:8940649] A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
[LiteratureReference:8955617] Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain
[LiteratureReference:8940626] Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells
[LiteratureReference:8940586] Thimet oligopeptidase (EC 3.4.24.15), a novel protein on the route of MHC class I antigen presentation
[LiteratureReference:8940637] Regulation of cell-surface major histocompatibility complex class I expression by the endopeptidase EC3.4.24.15 (thimet oligopeptidase)
[LiteratureReference:8940577] The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation
[LiteratureReference:8940630] Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes
[LiteratureReference:8940623] Alternative Antigen Processing for MHC Class I: Multiple Roads Lead to Rome
[LiteratureReference:8940625] Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol
[LiteratureReference:8940587] Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase
[LiteratureReference:8955613] Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction
[LiteratureReference:8940634] Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization
[LiteratureReference:8940579] Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
modified[InstanceEdit:8940662] Jupe, Steve, 2016-09-27
[InstanceEdit:8955619] Jupe, Steve, 2017-01-12
textThimet oligopeptidase (THOP1, EP24.15) is a zinc-dependent peptidase of the metallopeptidase M3 family (Pierotti et al. 1990). It was first described as a neuropeptide-degrading enzyme present in the soluble fraction of brain homogenates (Orlowski et al. 1983). However, its predominant location in the cytosol and nucleus suggests that extracellular degradation of neuropeptides and hormones is not its primary function (Fontenele-Neto et al. 2001). THOP1 can metabolize peptides within cells, thereby affecting antigen presentation and G protein-coupled receptor signal transduction. It was shown in vivo to participate in antigen presentation through MHC-I (Silva et al. 1999, Kim et al. 2003, Yorl et al. 2003) and in vitro to bind (Portaro et al. 1999) or degrade (Saric et al. 2001) some MHC-I associated peptides. THOP1 can degrade a broad range of intracellular peptides containing 5–17 amino acids (Oliveira et al. 2001, Berti et al. 2009). Substrate size is restricted because its catalytic center is located in a deep channel (Ray et al. 2004). THOP1 can both degrade existing peptides and generate new peptides, making it a versatile enzyme for regulating intracellular peptide function including antigen presentation (Berti et al. 2009, Russo et al. 2012).

Cytotoxic T lymphocytes (CTLs) recognize peptides presented by HLA class I molecules on the cell surface. The C terminus of these CTL epitopes is considered to be produced by the proteasome, but is complemented by THOP1 and other cytosolic endopeptidases such as Nardilysin (Kessler et al. 2011, Oliveira & van Hall 2015).
(summation)[BlackBoxEvent:8940641] THOP1 cleaves oligopeptide fragment (8-16aa) [Homo sapiens]
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