ID   MPPA_PONAB              Reviewed;         525 AA.
AC   Q5R513; Q5R992;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 75.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859499; CAH91668.1; -; mRNA.
DR   EMBL; CR861072; CAH93153.1; -; mRNA.
DR   RefSeq; NP_001126859.1; NM_001133387.1.
DR   AlphaFoldDB; Q5R513; -.
DR   SMR; Q5R513; -.
DR   STRING; 9601.ENSPPYP00000022172; -.
DR   MEROPS; M16.985; -.
DR   MEROPS; M16.P01; -.
DR   GeneID; 100173868; -.
DR   KEGG; pon:100173868; -.
DR   CTD; 23203; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   InParanoid; Q5R513; -.
DR   OrthoDB; 631107at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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                   /evidence="ECO:0000250"
FT   CHAIN           34..525
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000045849"
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"
FT   CONFLICT        20
FT                   /note="C -> S (in Ref. 1; CAH93153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="R -> L (in Ref. 1; CAH93153)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58340 MW;  22B7CA78966A091C CRC64;
     MAAVVLAATR LLRGSGSWGC SRLRFGPPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD
     GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST
     ARFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVGLLADV VLQPRLTDEE
     VEMTRMTVQF ELEDLNLRPD PEPLLTEMIH EAAYRENTVG LHRFCPTENI AKINREVLHS
     YLRNYYTPDR MVLAGVGVEH EHLVDCARKY LLGIQPAWGS AEAVDIDRSV AQYTGGIAKR
     ERDMSNVSLG PTPIPELTHI MVGLESCSFL EEDFIPFAVL NMMMGGGGSF SAGGPGKGMF
     SRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIITK EFILMSGTVD
     AVELERAKTQ LTSMLMMNLE SRPVIFEDVG RQVLATRSRK LPHELCTLIR NVKPEDVKRV
     ASKMLRGKPA VAALGDLTDL PTYEHIQTAL SSKDGRLPRT YRLFR