Tripeptidyl peptidase I

From Wikipedia, the free encyclopedia

Identifiers

TPP1; CLN2; GIG1; LPIC; MGC21297; TPP I

External IDs

OMIM: 607998 MGI: 1336194 HomoloGene: 335

Gene ontology
Molecular Function:	• aminopeptidase activity • serine-type endopeptidase activity • protein binding • tripeptidyl-peptidase I activity
Cellular Component:	• soluble fraction • mitochondrion • lysosome
Biological Process:	• proteolysis • lipid metabolic process • lysosome organization and biogenesis • nervous system development • protein catabolic process • peptide catabolic process • bone resorption • positive regulation of proteolysis • regulation of balance

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000391 (mRNA)
NP_000382 (protein)

NM_009906 (mRNA)
NP_034036 (protein)

Location

Chr 11: 6.59 - 6.6 Mb

Chr 7: 105.62 - 105.63 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: TPP1 tripeptidyl peptidase I.

[edit] 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.