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TPP1 / CLN2 is 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.
|Gene Name:||tripeptidyl peptidase I|
|Family/Subfamily:||Protease , Serine S53|
|Synonyms:||TPP1, CLN2, GIG1, LPIC, LINCL, TPP-I, Tripeptidyl aminopeptidase, Tripeptidyl peptidase I, Tripeptidyl-peptidase 1, Tripeptidyl-peptidase I, TPP-1, Growth-inhibiting protein 1|
|Target Sequences:||NM_000391 NP_000382.3 O14773|
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