Tripeptidyl peptidase I
Tripeptidyl peptidase I | |||||||||||
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Identifiers | |||||||||||
Symbols | TPP1 ; CLN2; GIG1; LPIC; MGC21297; TPP I | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 335 | ||||||||||
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RNA expression pattern | |||||||||||
File:PBB GE TPP1 200743 s at tn.png | |||||||||||
File:PBB GE TPP1 200742 s at tn.png | |||||||||||
File:PBB GE TPP1 214196 s at tn.png | |||||||||||
More reference expression data | |||||||||||
Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
Tripeptidyl peptidase I, also known as TPP1, is a human gene.[1]
This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.[1]
References
Further reading
- Mole SE, Mitchison HM, Munroe PB (1999). "Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5". Hum. Mutat. 14 (3): 199–215. doi:10.1002/(SICI)1098-1004(1999)14:3<199::AID-HUMU3>3.0.CO;2-A. PMID 10477428.
- Dawson G, Cho S (2000). "Batten's disease: clues to neuronal protein catabolism in lysosomes". J. Neurosci. Res. 60 (2): 133–40. PMID 10740217.
- Hofmann SL, Atashband A, Cho SK; et al. (2003). "Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2)". Curr. Mol. Med. 2 (5): 423–37. PMID 12125808.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
- Page AE, Fuller K, Chambers TJ, Warburton MJ (1993). "Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption". Arch. Biochem. Biophys. 306 (2): 354–9. PMID 8215436.
- Sleat DE, Donnelly RJ, Lackland H; et al. (1997). "Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis". Science. 277 (5333): 1802–5. PMID 9295267.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
- Liu CG, Sleat DE, Donnelly RJ, Lobel P (1998). "Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis". Genomics. 50 (2): 206–12. doi:10.1006/geno.1998.5328. PMID 9653647.
- Rawlings ND, Barrett AJ (1999). "Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis". Biochim. Biophys. Acta. 1429 (2): 496–500. PMID 9989235.
- Vines DJ, Warburton MJ (1999). "Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I.". FEBS Lett. 443 (2): 131–5. PMID 9989590.
- Sleat DE, Gin RM, Sohar I; et al. (1999). "Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder". Am. J. Hum. Genet. 64 (6): 1511–23. PMID 10330339.
- Junaid MA, Wu G, Pullarkat RK (2000). "Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis". J. Neurochem. 74 (1): 287–94. PMID 10617131.
- Ezaki J, Takeda-Ezaki M, Oda K, Kominami E (2000). "Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis". Biochem. Biophys. Res. Commun. 268 (3): 904–8. doi:10.1006/bbrc.2000.2207. PMID 10679303.
- Haines JL, Boustany RM, Alroy J; et al. (2000). "Chromosomal localization of two genes underlying late-infantile neuronal ceroid lipofuscinosis". Neurogenetics. 1 (3): 217–22. PMID 10737126.
- Ezaki J, Takeda-Ezaki M, Kominami E (2000). "Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase". J. Biochem. 128 (3): 509–16. PMID 10965052.
- Lin L, Sohar I, Lackland H, Lobel P (2001). "The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH". J. Biol. Chem. 276 (3): 2249–55. doi:10.1074/jbc.M008562200. PMID 11054422.
- Lam CW, Poon PM, Tong SF, Ko CH (2001). "Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis". Am. J. Med. Genet. 99 (2): 161–3. PMID 11241479.
- Zhong N, Moroziewicz DN, Ju W; et al. (2001). "Heterogeneity of late-infantile neuronal ceroid lipofuscinosis". Genet. Med. 2 (6): 312–8. PMID 11339651.
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