ID   PMIP_COPC7              Reviewed;         777 AA.
AC   A8N2T3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
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=CC1G_01835;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / FGSC 9003) (Inky cap
OS   fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC   Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Kodira C.D., Zeng Q., Alvarado L., Yandava C., Oleary S.,
RA   Dietrich F.S., Pukkila P.J.;
RT   "Annotation of the Coprinopsis cinerea genome.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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; AACS01000026; EAU92790.1; -; Genomic_DNA.
DR   RefSeq; XP_001829155.1; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 6005581; -.
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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT       1     39       Mitochondrion (Potential).
FT   CHAIN        40    777       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000338580.
FT   COMPBIAS    490    493       Poly-Asp.
FT   ACT_SITE    562    562       By similarity.
FT   METAL       561    561       Zinc; catalytic (By similarity).
FT   METAL       565    565       Zinc; catalytic (By similarity).
FT   METAL       568    568       Zinc; catalytic (By similarity).
SQ   SEQUENCE   777 AA;  87437 MW;  1BE83120B6ECF1B2 CRC64;
     MLSSSARTVL ARHSARQLYR FRGCLVHQQR HRHQVQRTLA THVQRHLPAS LDDKALVALF
     DQPNGSKLRS PFNTTGLFGH PNLTHPRALV SLAESTLVRA QLLTQRILEA GKSEHELAKV
     VKNLDRLSDM LCGVIDLAEL VRNAHPDRLW VEAANHAYET LCEFMNVLNT HTGLYEVLKQ
     VLSNPTLVNS LSPEAYQTAL IFWRDFEKSA IDLPPAQRNK FVSLSSDILV LGRQFLENAS
     TPRPPTSIKA SDLAGLKDKG MGVRLQLQAQ FTNRDLQIYP GSLQAHMIMR SAPNEEPRRR
     LYLAANSSTQ EQIEVLEALL KKRAELAQLV GRESFAHMTL DDKMAKTPDN VTNFLDALID
     HTRPFARSAL RTLAQRKQAH HGLSSLPIIQ AWDRDFYCPP DPPAPPIPLP PLTLGTVFMG
     LSRLFRHLYG VSLRPVPSAS GEVWHTDVQK LEVVDEDQGI IGWIYADLFA RRGKASGAAH
     YTVRCSRRTD DDDEQGDGMF EGAELQILES QEFEAVKRHR LPNQEGVFQL PLVVLLCEFT
     RPTVSKGGTI LEWHEVQTLF HEMGHAMHSM LGRTEYQNVS GTRCATDFVE LPSILMEHFL
     NSPAVLSLFD ADGTSTLRQI GNHHHDPCHA IDTYSQIMLA VVDQIYHSPT VLDPSFDSTR
     EYGNLQNTRG LIPYVPGTSY QTQFGHLFGY GATYYSYLFD RAIASRVWSK VFSKDPLDRE
     LGEKYKREVL RWGGARDPWE MVATLLDAPE LAAGDAEAMR EVGRWRIEDE VGVGGRH
//