Pitrm1
entrez
69617
canonical
uniprot
Q8K411
canonical
ensembl
ENSMUSG00000021193
resolver
ensp
ENSMUSP00000152229
resolver
ensp
ENSMUSP00000236858
resolver
genesymbol
Pitrm1
resolver
genesymbol_syn
Kiaa1104
resolver
genesymbol_syn
Ntup1
resolver
uniprot
Q3THC4
resolver
uniprot
Q3TJI1
resolver
uniprot
Q3TPP0
resolver
uniprot
Q3URQ8
resolver
uniprot
Q4KUG2
resolver
uniprot
Q4KUG3
resolver
uniprot
Q6ZPX6
resolver
uniprot
Q922N1
resolver
uniprot
Q9CV63
resolver
uniprot_entry
PREP_MOUSE
resolver
uniprot_sec
Q3THC4
resolver
uniprot_sec
Q3TJI1
resolver
uniprot_sec
Q3TPP0
resolver
uniprot_sec
Q3URQ8
resolver
uniprot_sec
Q4KUG2
resolver
uniprot_sec
Q4KUG3
resolver
uniprot_sec
Q6ZPX6
resolver
uniprot_sec
Q922N1
resolver
uniprot_sec
Q9CV63
resolver
activity_regulation
ACTIVITY REGULATION: Mainly exists in a closed and catalytically competent conformation but a closed-to-open switch allows substrate entry into the catalytic chamber. Substrate binding induces closure and dimerization. A disulfide bond may lock the enzyme in a closed conformation preventing substrate entry into the catalytic chamber, participating in redox regulation of the enzyme. Inhibited by metal-chelating agents. Inhibited by nickel and zinc excess, and slightly activated by manganese. {ECO:0000250|UniProtKB:Q5JRX3}.
uniprot
proteins
amino_acid_sequence
MWRFSGRRGLCAVQRLSCGRVHHRVWREKSDQACERALQYKVGEKIHGFTVNQVTPVPELFLTAVKLSHDNTGARYLHLAREDKNNLFSVQFRTTPMDSTGVPHVLEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAMTASDYTIYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPRDPQTPLIFKGVVFNEMKGAFTDNERIFSQHLQNKLLPDHTYSVVSGGDPLCIPELTWEQLKQFHATHYHPSNARFFTYGNFQLEGHLKQIHEEALSKFQRLEQSTAVPAQPHWDKPREFHITCGPDSLATETAKQTTVSVSFLLPDITDTFEAFTLSLLSSLLIAGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDVKTVRELVDRTIEEVIEKGFEDDRIEALLHKIEIQTKHQSASFGLTLTSYIASCWNHDGDPVELLQIGSQLTRFRKCLKENPKFLQEKVEQYFKNNQHKLTLSMKPDDKYYEKQTQMETEKLEQKVNSLSPADKQQIYEKGLELQTQQSKHQDASCLPALKVSDIEPSMPFTKLDIGLAAGDIPVQYCPQPTNGMVYFRAFSSLNTLPEDLRPIVPLFCSVLTKLGCGILNYREQAQQIELKTGGMSVTPHVLPDDSQLDTYEQGVLFSSLCLERNLPDMMHLWSEIFNNPCFEEEEHFKVLVKMTAQELSNGISDSGHLYAALRASKTLTPSGDLQETFSGMDQVKVMKRIAEMTDIKPILRKLPRIKKYLLNCDNMRCSVNATPQQMPQAEKEVENFLRNVGRSKKERKPVRPHIVEKPTPSGPSGAAHVSGSQIVRKLVTDPTFKPCQMKTHFVLPFPVNYIGECVRTVPYADPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLTHSGIFTLYSYRDPNSIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDSPVAPSDKGMDHFLYGLSDEMKQAYREQLFAVNHDKLTSVSHKYLGIGKSTHGLAILGPENSKIAKDPSWIIK
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42. {ECO:0000250|UniProtKB:Q5JRX3}.
uniprot
proteins
mass_dalton
117372
uniprot
proteins
post_translational_modification
PTM: A disulfide bond locks the enzyme in the closed conformation preventing substrate entry into the catalytic chamber. {ECO:0000250|UniProtKB:Q5JRX3}.
uniprot
proteins
protein_family
Peptidase M16 family
uniprot
proteins
protein_family
PreP subfamily
uniprot
proteins
pubmed
12490196
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15919810
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
1036
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q5JRX3}.
uniprot
proteins