ID   PMIP_SCHPO              Reviewed;         762 AA.
AC   Q10415;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   AltName: Full=Octapeptidyl aminopeptidase;
DE   Flags: Precursor;
GN   Name=oct1; ORFNames=SPAC1F3.10c;
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).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size. While most mitochondrial precursor proteins are processed
CC       to the mature form in one step by mitochondrial processing peptidase
CC       (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC       processing by MPP is a required step for a subgroup of nuclear-encoded
CC       precursor proteins destined for the matrix or the inner membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA94628.1; -; Genomic_DNA.
DR   PIR; T38081; T38081.
DR   RefSeq; NP_593013.1; NM_001018412.2.
DR   AlphaFoldDB; Q10415; -.
DR   SMR; Q10415; -.
DR   STRING; 4896.SPAC1F3.10c.1; -.
DR   iPTMnet; Q10415; -.
DR   MaxQB; Q10415; -.
DR   PaxDb; Q10415; -.
DR   PRIDE; Q10415; -.
DR   EnsemblFungi; SPAC1F3.10c.1; SPAC1F3.10c.1:pep; SPAC1F3.10c.
DR   GeneID; 2541640; -.
DR   KEGG; spo:SPAC1F3.10c; -.
DR   PomBase; SPAC1F3.10c; oct1.
DR   VEuPathDB; FungiDB:SPAC1F3.10c; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q10415; -.
DR   OMA; VVYCDLF; -.
DR   PhylomeDB; Q10415; -.
DR   PRO; PR:Q10415; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISO:PomBase.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISO:PomBase.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISO:PomBase.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..762
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000028582"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         544
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         548
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         551
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   762 AA;  86286 MW;  C6420C1F99001EFC CRC64;
     MQVRTLLTLG KKKVIGNRQC ILSLYRKYSN VQSRKAEDQL LRQIFDDQNI AVNQITKRNG
     IQGVGLFRNH FLSDKDTGFL RLAETASEKC KAVIEDLLLE DTEDGSIVVS KFDRISNLLC
     SVIDLFEFVR CAHPDKMVVM KAEEAYSYLF ELMNTLNTHQ GLYEKLKCSL QQTPTLKDTD
     PEAYTVGRVF LQDFEKSGVN LESSKRNSFV KKSSESATLG RAFFNNSMNR PQRYLTISKQ
     RLAGSDPYFV RSLSKNDKNF IMIPTVGYEG TQALISVANP DVRKEIYMEG HKGTVEEVEL
     LNSYLRSKAE VAKLVGKSSF ADLQLIDKMA NAPKHVVEFL ENLSLKNSSV LKKILNNLAL
     MKKKELNLNF LPSFDVWDRE YYTARYKQSL INQKPSLNPS ITNYRRFFSV GTVIQGLSRL
     FSSLYGLRFV PADISPGEVW HPDVNKVNVY NENDHVMGVI YFDLFARTGK TDGAAHFTIR
     SSRELDLTSF DDSISLGFDD ATNIRVKDNK RYQIPVISLL CNFVRSSGMD PTFLDLWDVK
     TLFHEMGHAM HSILGHTKYQ NLAGTRCATD FVELPSIIME FFMSNPAVLP LYARYEGTEI
     PLPVQVLNHH NMVENSSAPL DLQSQICMAM VDQLFHSKVV LDPSFNSIDE VTNVTRKFSG
     FESAPPAAWY LQFSHLYGYS ATYYSYIFDT VLASLIFSKL FAGNPLSREA GEKFRKAILR
     WGGSRSPWEC VAEALEQPIL ATGGEEAMRR IGSEGIKATS TF