ID   MPPA_BOVIN              Reviewed;         525 AA.
AC   Q0P5M8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PMPCA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC       mitochondrial processing protease (MPP), which cleaves the
CC       mitochondrial sequence off newly imported precursors proteins.
CC       {ECO:0000250|UniProtKB:Q10713}.
CC   -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits,
CC       forming the mitochondrial processing protease (MPP) in which PMPCA is
CC       involved in substrate recognition and binding and PMPCB is the
CC       catalytic subunit. {ECO:0000250|UniProtKB:P11914}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q10713}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC       binding site. {ECO:0000305}.
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DR   EMBL; BC119849; AAI19850.1; -; mRNA.
DR   RefSeq; NP_001070432.1; NM_001076964.1.
DR   AlphaFoldDB; Q0P5M8; -.
DR   SMR; Q0P5M8; -.
DR   STRING; 9913.ENSBTAP00000001782; -.
DR   MEROPS; M16.985; -.
DR   MEROPS; M16.P01; -.
DR   PaxDb; Q0P5M8; -.
DR   PRIDE; Q0P5M8; -.
DR   Ensembl; ENSBTAT00000001782; ENSBTAP00000001782; ENSBTAG00000001353.
DR   GeneID; 767847; -.
DR   KEGG; bta:767847; -.
DR   CTD; 23203; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001353; -.
DR   VGNC; VGNC:33075; PMPCA.
DR   eggNOG; KOG2067; Eukaryota.
DR   GeneTree; ENSGT00940000156724; -.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   InParanoid; Q0P5M8; -.
DR   OMA; LKYHHSP; -.
DR   OrthoDB; 631107at2759; -.
DR   TreeFam; TF105031; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000001353; Expressed in laryngeal cartilage and 105 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:UniProtKB.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR037715; PMPCA.
DR   PANTHER; PTHR11851:SF192; PTHR11851:SF192; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT   CHAIN           34..525
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000283040"
FT   MOD_RES         64
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC61"
FT   MOD_RES         299
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q10713"
SQ   SEQUENCE   525 AA;  58135 MW;  9D375E3FA8B7E1C2 CRC64;
     MAAMVLAATR LLRGSGSWGR SRPRFGDPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD
     GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST
     ERFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVGLLADV VLHPRLTDEE
     IEMARMAVQF ELEDLNMRPD PEPLLTEMVH EAAYRENTVG LHRFCPAENV GKMDRDVLHA
     YLRNYYTPDR MVLAGVGVEH AQLVECARKY LLGTCPAWGT GAAVHVDRSV AQYTGGIVKL
     ERDMSNVSLG PTPFPELTHI MIGLESCSFL EGDFIPFAVL NMMMGGGGSF SAGGPGKGMF
     TRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIVTR EFVLMAGTVD
     VVELERAKTQ LTSMLMMNLE ARPVIFEDVG RQVLATRSRK LPHELCALIR DVKPEDIKRV
     ASKMLRGKPA VAALGDLSEL PAYEHVQAAL ASRDGRLPRV YRLFR