THOP1

THOP1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1S4B, 2O36
Identifiers
Aliases	THOP1 , EP24.15, MEPD_HUMAN, MP78, TOP, thimet oligopeptidase 1
External IDs	OMIM: 601117 MGI: 1354165 HomoloGene: 55726 GeneCards: THOP1
Gene location (Human)
Chr.	Chromosome 19 (human)
End	2,815,807 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	80,918,393 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; anterior pituitary; ; gastrocnemius muscle; ; prefrontal cortex; ; cingulate gyrus; ; ganglionic eminence; ; Brodmann area 9; ; nucleus accumbens; ; caudate nucleus; ; amygdala;
	Top expressed in
	spermatid; ; spermatocyte; ; esophagus; ; seminiferous tubule; ; lip; ; internal carotid artery; ; external carotid artery; ; lacrimal gland; ; somite; ; secondary oocyte;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	peptide binding ; peptidase activity ; hydrolase activity ; metallopeptidase activity ; metal ion binding ; metalloendopeptidase activity ;
Cellular component	cytoplasm ; mitochondrial intermembrane space ; cytosol ;
Biological process	proteolysis ; peptide metabolic process ; protein polyubiquitination ;
	Sources:Amigo / QuickGO
Orthologs
	7064
	50492
	ENSG00000172009
	ENSMUSG00000004929
	P52888
	Q8C1A5
	NM_003249
	NM_022653
	NP_003240
	NP_073144
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated February 15, 2024

Thimet oligopeptidase is an enzyme that in humans is encoded by the THOP1 gene.^[5]^[6]

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Thimet oligopeptidases, also known as TOPs, are a type of M3 metallopeptidases. These enzymes can be found in animals and plants, showing distinctive functions. In animals and humans, they are involved in the degradation of peptides, such as bradykinin, neurotensin, angiotensin I, and Aβ peptide, helping to regulate physiological processes. In plants, their role is related to the degradation of targeting peptides and the immune response to pathogens through Salicylic Acid (SA)-dependent stress signaling. In Arabidopsis thaliana—recognized as a model plant for scientific studies—two thimet oligopeptidases, known as TOP1 and TOP2, have been identified as targets for salicylic acid binding in the plant. These TOP enzymes are key components to understand the SA-mediated signaling where interactions exist with different components and most of the pathways are unknown.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000172009 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004929 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Torres MP, Prange C, Lennon G (Dec 1998). "Human endopeptidase 24.15 (THOP1) is localized on chromosome 19p13.3 and is excluded from the linkage region for late-onset Alzheimer disease". Genomics. 53 (2): 239–40. doi:10.1006/geno.1998.5487. PMID 9790774.
↑ "Entrez Gene: THOP1 thimet oligopeptidase 1".

Thompson A, Huber G, Malherbe P (1995). "Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide". Biochem. Biophys. Res. Commun. 213 (1): 66–73. doi:10.1006/bbrc.1995.2099. PMID 7639763.
Papastoitsis G, Siman R, Scott R, Abraham CR (1994). "Identification of a metalloprotease from Alzheimer's disease brain able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments". Biochemistry. 33 (1): 192–9. doi:10.1021/bi00167a025. PMID 8286339.
Dando PM, Brown MA, Barrett AJ (1993). "Human thimet oligopeptidase". Biochem. J. 294 (Pt 2): 451–7. doi:10.1042/bj2940451. PMC 1134475 . PMID 8373360.
Meckelein B, de Silva HA, Roses AD, et al. (1997). "Human endopeptidase (THOP1) is localized on chromosome 19 within the linkage region for the late-onset alzheimer disease AD2 locus". Genomics. 31 (2): 246–9. doi: 10.1006/geno.1996.0041 . PMID 8824811.
Crack PJ, Wu TJ, Cummins PM, et al. (1999). "The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane". Brain Res. 835 (2): 113–24. doi:10.1016/S0006-8993(99)01494-8. PMID 10415366. S2CID 23769423.
Pineau C, McCool S, Glucksman MJ, et al. (2000). "Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testes". J. Cell Sci. 112 (20): 3455–62. doi:10.1242/jcs.112.20.3455. PMID 10504294.
Ferro ES, Tullai JW, Glucksman MJ, Roberts JL (1999). "Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)". DNA Cell Biol. 18 (10): 781–9. doi:10.1089/104454999314926. hdl: 11449/37910 . PMID 10541437.
Tullai JW, Cummins PM, Pabon A, et al. (2001). "The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation". J. Biol. Chem. 275 (47): 36514–22. doi: 10.1074/jbc.M001843200 . PMID 10969067.
Molina HM, Carmona AK, Kouyoumdjian M, Borges DR (2000). "Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase". Life Sci. 67 (5): 509–20. doi:10.1016/S0024-3205(00)00650-0. PMID 10993116.
Saric T, Beninga J, Graef CI, et al. (2001). "Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase". J. Biol. Chem. 276 (39): 36474–81. doi: 10.1074/jbc.M105517200 . PMID 11479311.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Gioli-Pereira L, Fontenele-Neto JD, Borges DR, Kouyoumdjian M (2003). "Localization of EP24.15, a major liver kininase". J. Histochem. Cytochem. 51 (1): 125–7. doi: 10.1177/002215540305100115 . PMID 12502762.
York IA, Mo AX, Lemerise K, et al. (2003). "The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation". Immunity. 18 (3): 429–40. doi: 10.1016/S1074-7613(03)00058-X . PMID 12648459.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID 14702039.
Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW (2004). "Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization". J. Biol. Chem. 279 (19): 20480–9. doi: 10.1074/jbc.M400795200 . PMID 14998993.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19" (PDF). Nature. 428 (6982): 529–35. Bibcode:2004Natur.428..529G. doi: 10.1038/nature02399 . PMID 15057824.
Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147 . PMID 15231747.
Saric T, Graef CI, Goldberg AL (2004). "Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases". J. Biol. Chem. 279 (45): 46723–32. doi: 10.1074/jbc.M406537200 . PMID 15328361.
Shivakumar BR, Wang Z, Hammond TG, Harris RC (2005). "EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor". Cell Biochem. Funct. 23 (3): 195–204. doi:10.1002/cbf.1176. PMID 15376229. S2CID 5695331.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000172009 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004929 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9790774-5] Torres MP, Prange C, Lennon G (Dec 1998). "Human endopeptidase 24.15 (THOP1) is localized on chromosome 19p13.3 and is excluded from the linkage region for late-onset Alzheimer disease". Genomics. 53 (2): 239–40. doi:10.1006/geno.1998.5487. PMID 9790774.

[entrez-6] "Entrez Gene: THOP1 thimet oligopeptidase 1".

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THOP1

Related Research Articles

References

Further reading