MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP000590

UniProt Annotations

Entry Information
Gene Nametripeptidyl peptidase I
Protein EntryTPP1_HUMAN
UniProt IDO14773
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=O14773-1; Sequence=Displayed; Name=2; IsoId=O14773-2; Sequence=VSP_013118; Note=No experimental confirmation available.;
Catalytic ActivityRelease of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
DiseaseCeroid lipofuscinosis, neuronal, 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. {ECO:0000269|PubMed:10330339, ECO:0000269|PubMed:10665500, ECO:0000269|PubMed:11241479, ECO:0000269|PubMed:11339651, ECO:0000269|PubMed:11589012, ECO:0000269|PubMed:12376936, ECO:0000269|PubMed:12414822, ECO:0000269|PubMed:12698559, ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:20340139, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:9295267}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseSpinocerebellar ataxia, autosomal recessive, 7 (SCAR7) [MIM:609270]: Spinocerebellar ataxia defines a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR7 patients show difficulty walking and writing, dysarthria, limb ataxia, and cerebellar atrophy. {ECO:0000269|PubMed:23418007}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionLysosomal serine protease with tripeptidyl-peptidase I 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 (By similarity). {ECO:0000250}.
PtmActivated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218}.
Sequence CautionSequence=AAM08412.1; Type=Miscellaneous discrepancy; Note=Incorrectly indicated as originating from bovine.; Evidence={ECO:0000305}; Sequence=AAQ88866.1; Type=Frameshift; Positions=551; Evidence={ECO:0000305};
SimilarityContains 1 peptidase S53 domain. {ECO:0000305}.
Subcellular LocationLysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
SubunitMonomer. {ECO:0000269|PubMed:19038967}.
Tissue SpecificityDetected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.
Web ResourceName=Mendelian genes trieptidyl peptidase I (TPP1); Note=Leiden Open Variation Database (LOVD); URL="http://www.lovd.nl/TPP1";
Web ResourceName=NCL CLN2; Note=Neural Ceroid Lipofuscinoses mutation db; URL="http://www.ucl.ac.uk/ncl/cln2.shtml";
  logo