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   16-JUN-2009, entry version 64.
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 (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to
CC       their mature size. While most mitochondrial precursor proteins are
CC       processed to the mature form in one step by mitochondrial
CC       processing peptidase (MPP), the sequential cleavage by MIP of an
CC       octapeptide after initial processing by MPP is a required step for
CC       a subgroup of nuclear-encoded precursor proteins destined for the
CC       matrix or the inner membrane (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal octapeptide as second
CC       stage of processing of some proteins imported into the
CC       mitochondrion.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; CU329670; CAA94628.1; -; Genomic_DNA.
DR   PIR; T38081; T38081.
DR   RefSeq; NP_593013.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 2541640; -.
DR   KEGG; spo:SPAC1F3.10c; -.
DR   NMPDR; fig|4896.1.peg.2983; -.
DR   GeneDB_Spombe; SPAC1F3.10c; -.
DR   OMA; Q10415; AMGERYR.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000735-MON; -.
DR   BRENDA; 3.4.24.59; 653.
DR   ArrayExpress; Q10415; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Metal-binding; Metalloprotease;
KW   Mitochondrion; Protease; Transit peptide; Zinc.
FT   TRANSIT       1     28       Mitochondrion (Potential).
FT   CHAIN        29    762       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000028582.
FT   ACT_SITE    545    545       By similarity.
FT   METAL       544    544       Zinc; catalytic (By similarity).
FT   METAL       548    548       Zinc; catalytic (By similarity).
FT   METAL       551    551       Zinc; catalytic (By similarity).
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
//