Pmpcb
entrez
64198
canonical
uniprot
Q03346
canonical
ensembl
ENSRNOG00000012693
resolver
ensembl
ENSRNOG00055021562
resolver
ensembl
ENSRNOG00065017894
resolver
ensp
ENSRNOP00000017017
resolver
ensp
ENSRNOP00055029960
resolver
ensp
ENSRNOP00065023829
resolver
enst
ENSRNOT00055036872
resolver
enst
ENSRNOT00065029984
resolver
genesymbol
Pmpcb
resolver
genesymbol_syn
Mppb
resolver
uniprot
Q68G08
resolver
uniprot_entry
MPPB_RAT
resolver
uniprot_sec
Q68G08
resolver
activity_regulation
ACTIVITY REGULATION: Binding to PMPCA is required for catalytic activity. {ECO:0000250|UniProtKB:P10507}.
uniprot
proteins
amino_acid_sequence
MAAAAVSRTLLPVAGRRLWGFTRRLPLRAAAAQPLYFGGDRLRSTQAAPQVVLNVPETQVTCLENGLRVASENSGISTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVCHNELLELAKFHFGDSLCAHKGDVPALPPCKFTGSEIRVRDDKMPLAHLAVAIEAVGWTHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCEQATVADMLHAVQKEWMRLCTAVSESEVARAKNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVDAEMVREVCTKYIYGKSPAIAALGPIERLPDFNQICSNMRWTRD
uniprot
proteins
ec_number
3.4.24.64
uniprot
proteins
function
FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable) (PubMed:12433926). Preferentially, cleaves after an arginine at position P2 (PubMed:12433926). Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088). {ECO:0000269|PubMed:12433926, ECO:0000269|PubMed:22354088, ECO:0000305|PubMed:22354088}.
uniprot
proteins
mass_dalton
54265
uniprot
proteins
mutagenesis
MUTAGEN 191; /note="E->A: Loss of substrate cleavage site specificity. Complete loss of cleavage site specificity following an arginine at position P2; when associated with A-195."; /evidence="ECO:0000269|PubMed:12433926"; MUTAGEN 195; /note="D->A: Severe loss of cleavage site specificity following an arginine at position P2. The loss is complete; when associated with A-191."; /evidence="ECO:0000269|PubMed:12433926
uniprot
proteins
protein_family
Peptidase M16 family
uniprot
proteins
pubmed
12433926
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22354088
uniprot
proteins
pubmed
8422255
uniprot
proteins
pubmed
8506385
uniprot
proteins
sequence_length
489
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:O75439}.
uniprot
proteins