ID   MPPA_RAT                Reviewed;         524 AA.
AC   P20069;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 156.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   AltName: Full=P-55;
DE   Flags: Precursor;
GN   Name=Pmpca; Synonyms=Mppa;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-44; 113-121; 188-202;
RP   223-231; 235-242; 362-369 AND 486-511, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2236012; DOI=10.1073/pnas.87.20.7978;
RA   Kleiber J., Kalousek F., Swaroop M., Rosenberg L.E.;
RT   "The general mitochondrial matrix processing protease from rat liver:
RT   structural characterization of the catalytic subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7978-7982(1990).
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:0000269|PubMed:2236012}. 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M57728; AAA41632.1; -; mRNA.
DR   PIR; A36205; A36205.
DR   AlphaFoldDB; P20069; -.
DR   SMR; P20069; -.
DR   IntAct; P20069; 1.
DR   STRING; 10116.ENSRNOP00000037642; -.
DR   MEROPS; M16.P01; -.
DR   CarbonylDB; P20069; -.
DR   iPTMnet; P20069; -.
DR   PhosphoSitePlus; P20069; -.
DR   jPOST; P20069; -.
DR   PRIDE; P20069; -.
DR   UCSC; RGD:727897; rat.
DR   RGD; 727897; Pmpca.
DR   eggNOG; KOG2067; Eukaryota.
DR   InParanoid; P20069; -.
DR   PhylomeDB; P20069; -.
DR   Reactome; R-RNO-8949664; Processing of SMDT1.
DR   PRO; PR:P20069; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0016485; P:protein processing; IDA:RGD.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2236012"
FT   CHAIN           33..524
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000026769"
FT   MOD_RES         63
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC61"
SQ   SEQUENCE   524 AA;  58608 MW;  8BF08FBC9FF09DB2 CRC64;
     MATAVWAAAR LLRGSAALCA RPKFGSPAHR RFSSGATYPN IPLSSPLPGV PKPIFATVDG
     QEKFETKVTT LDNGLRVASQ NKFGQFCTLG ILINSGSRYE AKYLSGIAHF LEKLAFSSTA
     RFDSKDEILL TLEKHGGICD CQTSRDTTMY AVSADSKGLD TVVGLLADVV LHPRLTDEEI
     EMTRMAVQFE LEDLNMRPDP EPLLTEMIHE AAFRENTVGL HRFCPVENIG KIDREVLHSY
     LKNYYTPDRM VLAGVGVEHE HLVECARKYL LGVQPAWGAP GAVWMLTAQW HSTRGGSSRW
     RETCQMSALR PPRFQSSHIY GGARELLLLE EDFIPFAVLN MMMGGGGSFS AGGPGKGMFS
     RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV REMVEIITKE FILMGRTVDL
     VELERAKTQL MSMLMMNLES RPVIFEDVGR QVLATHSRKL PHELCTLIRN VKPEDIKRVA
     SKMLRGKPAV AALGDLTDLP TYEHIQAALS SRDGRLPRTY RLFR