Contents

Search


tripeptidyl-peptidase 1; TPP-1; cell growth-inhibiting gene 1 protein; lysosomal pepstatin-insensitive protease; LPIC; tripeptidyl aminopeptidase; tripeptidyl-peptidase I; TPP-I (TPP1, GIG1, UNQ267/PRO304)

Function: - lysosomal serine protease with tripeptidyl-peptidase 1 activity - may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases - requires substrates with an unsubstituted N-terminus (putative) - release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity - activated by autocatalytic proteolytical processing upon acidification Cofactor: binds 1 Ca+2 per subunit Structure: - monomer - N-glycosylation - N-glycosylation is required for processing & activity - belongs to the peptidase S53 family Compartment: - lysosome, melanosome Alternative splicing: named isoforms=2 Expression: - detected in all tissues examined - highest levels in heart & placenta - lower & relatively similar levels in other tissues Pathology: - defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 Laboratory: - tripeptidyl peptidase 1 in dried blood spot - tripeptidyl peptidase 1 in fibroblasts - tripeptidyl peptidase 1 in leukocytes

General

aminopeptidase Ca+2 binding protein glycoprotein

Properties

SIZE: entity length = 563 aa MW = 61 kD COMPARTMENT: lysosome MOTIF: signal sequence {1-19} cysteine residue {C111} MODIFICATION: cysteine residue {C122} cysteine residue {C122} MODIFICATION: cysteine residue {C111} N-glycosylation site {N210} N-glycosylation site {N222} glutamate residue {E272} aspartate residue {D276} N-glycosylation site {N286} N-glycosylation site {N313} cysteine residue {C365} MODIFICATION: cysteine residue {C526} N-glycosylation site {N443} serine residue {S475} Ca+2-binding site SITE: 517-517 Ca+2-binding site SITE: 518-518 cysteine residue {C522} MODIFICATION: cysteine residue {C537} cysteine residue {C526} MODIFICATION: cysteine residue {C365} cysteine residue {C537} MODIFICATION: cysteine residue {C522} Ca+2-binding site SITE: 539-539 Ca+2-binding site SITE: 541-541 Ca+2-binding site SITE: 543-543

Database Correlations

OMIM correlations MORBIDMAP 607998 UniProt O14773 PFAM correlations Entrez Gene 1200 Kegg hsa:1200 ENZYME 3.4.14.9

References

  1. UniProt :accession O14773
  2. NCL CLN2; Neural ceroid lipofuscinoses mutation db http://www.ucl.ac.uk/ncl/cln2.shtml
  3. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/TPP1