UniProt functional annotation for P17655



	UniProt functional annotation for P17655

UniProt code: P17655.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity). {ECO:0000250|UniProtKB:O08529, ECO:0000269|PubMed:17650508}.

Catalytic activity: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250};

Activity regulation: Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.

Subunit: Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3. {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:Q07009}.

Subcellular location: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.

Tissue specificity: Ubiquitous.

Similarity: Belongs to the peptidase C2 family. {ECO:0000305}.

Sequence caution: Sequence=AAH07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; Sequence=AAH11828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity). {ECO:0000250\|UniProtKB:O08529, ECO:0000269\|PubMed:17650508}.


Catalytic activity:		Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
Cofactor:		Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250};
Activity regulation:		Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.
Subunit:		Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3. {ECO:0000250\|UniProtKB:O08529, ECO:0000250\|UniProtKB:Q07009}.
Subcellular location:		Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
Tissue specificity:		Ubiquitous.
Similarity:		Belongs to the peptidase C2 family. {ECO:0000305}.
Sequence caution:		Sequence=AAH07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; Sequence=AAH11828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};