UniProt functional annotation for P10507



	UniProt functional annotation for P10507

UniProt code: P10507.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity). {ECO:0000250|UniProtKB:Q03346, ECO:0000269|PubMed:2007593, ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444}.

Catalytic activity: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000269|PubMed:2007593, ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444};

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9654444}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9654444};

Activity regulation: Binding to MAS2 is required for catalytic activity (PubMed:9654444, PubMed:9299349). Inhibited by high levels (> 1uM) of zinc (PubMed:9654444). Inhibited by metal chelators ethylenediaminetetraacetic acid (EDTA) and O-phenanthroline (PubMed:9654444). {ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444}.

Subunit: Heterodimer of MAS2 (alpha) and MAS1 (beta) subunits, forming the mitochondrial processing protease (MPP) in which MAS2 is involved in substrate recognition and binding and MAS1 is the catalytic subunit. {ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9299349}.

Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3044780}.

Miscellaneous: Present with 1360 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the peptidase M16 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity). {ECO:0000250\|UniProtKB:Q03346, ECO:0000269\|PubMed:2007593, ECO:0000269\|PubMed:9299349, ECO:0000269\|PubMed:9654444}.


Catalytic activity:		Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000269\|PubMed:2007593, ECO:0000269\|PubMed:9299349, ECO:0000269\|PubMed:9654444};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:9654444}; Note=Binds 1 zinc ion per subunit. {ECO:0000269\|PubMed:11470436, ECO:0000269\|PubMed:9654444};
Activity regulation:		Binding to MAS2 is required for catalytic activity (PubMed:9654444, PubMed:9299349). Inhibited by high levels (> 1uM) of zinc (PubMed:9654444). Inhibited by metal chelators ethylenediaminetetraacetic acid (EDTA) and O-phenanthroline (PubMed:9654444). {ECO:0000269\|PubMed:9299349, ECO:0000269\|PubMed:9654444}.
Subunit:		Heterodimer of MAS2 (alpha) and MAS1 (beta) subunits, forming the mitochondrial processing protease (MPP) in which MAS2 is involved in substrate recognition and binding and MAS1 is the catalytic subunit. {ECO:0000269\|PubMed:11470436, ECO:0000269\|PubMed:9299349}.
Subcellular location:		Mitochondrion matrix {ECO:0000269\|PubMed:3044780}.
Miscellaneous:		Present with 1360 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the peptidase M16 family. {ECO:0000305}.