ID   MPPA_SCHPO              Reviewed;         502 AA.
AC   O94745;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Probable mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   Flags: Precursor;
GN   Name=mas2; ORFNames=SPBC18E5.12c, SPBC23G7.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:P11914}.
CC   -!- SUBUNIT: Heterodimer of mas2 (alpha) and mas1 (beta) subunits, forming
CC       the mitochondrial processing protease (MPP) in which mas2 is involved
CC       in substrate recognition and binding and mas1 is the catalytic subunit.
CC       {ECO:0000250|UniProtKB:P11914}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:16823372}.
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; CU329671; CAA22672.2; -; Genomic_DNA.
DR   PIR; T39763; T39763.
DR   RefSeq; NP_595859.2; NM_001021763.2.
DR   AlphaFoldDB; O94745; -.
DR   SMR; O94745; -.
DR   BioGRID; 277236; 1.
DR   STRING; 4896.SPBC18E5.12c.1; -.
DR   MaxQB; O94745; -.
DR   PaxDb; O94745; -.
DR   EnsemblFungi; SPBC18E5.12c.1; SPBC18E5.12c.1:pep; SPBC18E5.12c.
DR   GeneID; 2540713; -.
DR   KEGG; spo:SPBC18E5.12c; -.
DR   PomBase; SPBC18E5.12c; mas2.
DR   VEuPathDB; FungiDB:SPBC18E5.12c; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   InParanoid; O94745; -.
DR   OMA; LKYHHSP; -.
DR   Reactome; R-SPO-611105; Respiratory electron transport.
DR   PRO; PR:O94745; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:PomBase.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:PomBase.
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   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..502
FT                   /note="Probable mitochondrial-processing peptidase subunit
FT                   alpha"
FT                   /id="PRO_0000026772"
SQ   SEQUENCE   502 AA;  55578 MW;  8543230258A6A16C CRC64;
     MSFLTTPKML SEYQCLKNIG FSHKTVLKRR LFRKECTPAL KSFYSTQDPA LNEVRTEKLK
     NGVTYVCDPR PGHFSGLGVY VKAGSRYETK KFSGVSHFMD RLAFQATERT PVGEMKAKLE
     NLGGNYMCST SRESMIYQAA VFNDDVKSMS KLLAETVLAP KIQEDDLVHY RDSIIYENSE
     LWTKPDALLG EFAHVTAFQN NTLGNCLLCT PDKVNGITAT SIREYLKYFY RPEHLTLAYA
     GIPQEIAKEI TKELYGHLPS SSLPPLEAIP SHYTGGFMGI KKSEAPPVPY QQEFTHVVIA
     MEGLPVTDPD IYALACLQFL LGGGGSFSAG GPGKGMYSRL YLNVLNQYPW VETCMAFNHS
     YTDSGLFGMF VTILDDAAHL AAPLIIRELC NTVLSVTSEE TERAKNQLKS SLLMNLESRM
     ISLEDLGRQI QTQNGLYITP KEMIEKIDAL TPSDLSRVAR RVLTGNVSNP GNGTGKPTVL
     IHGNVDEVGD VFALCKKAGI GH