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CLN2 Protein, Antibody, ELISA Kit, cDNA Clone

CLN2 Related Areas

CLN2 Related Pathways

CLN2 Related Product

    CLN2 Summary & Protein Information

    CLN2 Background

    Gene Summary: TPP1 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 TPP1 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. [provided by RefSeq, Jul 2008]
    General information above from NCBI
    Catalytic activity: Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
    Cofactor: Binds 1 calcium ion per subunit.
    Subunit structure: Monomer.
    Subcellular location: Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
    Tissue specificity: Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.
    Post-translational: Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity.
    Involvement in disease: Neuronal ceroid lipofuscinosis 2 (CLN2) [MIM:204500]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the peptidase S53 family.
    General information above from UniProt

    Tripeptidyl-peptidase 1 (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. TPP1 / CLN2 May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.

    CLN2 Alternative Name

    cell growth-inhibiting gene 1 protein,CLN2,GIG1,growth-inhibiting protein 1,LPIC,lysosomal pepstatin insensitive protease,TPP-1,tripeptidyl aminopeptidase,tripeptidyl-peptidase 1, [human]
    ceroid-lipofuscinosis,Cln2,LPIC,lysosomal pepstatin-insensitive protease,neuronal 2,TPP-1,TPP-I,tripeptidyl aminopeptidase,tripeptidyl peptidase-I,tripeptidyl-peptidase 1, [mouse]

    CLN2 Related Studies

  • Xin H, et al. (2007) TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature. 445(7127): 559-62.
  • O'Connor MS, et al. (2006) A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc Natl Acad Sci U S A. 103(32): 11874-9.
  • Abreu E, et al. (2010) TIN2-tethered TPP1 recruits human telomerase to telomeres in vivo. Mol Cell Biol. 30(12): 2971-82.
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