ID   PMIP_COPSC              Reviewed;         772 AA.
AC   Q6Y5M7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
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; Synonyms=MIP;
OS   Coprinopsis scobicola (Ink cap fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=71696;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Cb.M8;
RX   PubMed=14761798; DOI=10.1016/j.fgb.2003.11.008;
RA   James T.Y., Kuees U., Rehner S.A., Vilgalys R.;
RT   "Evolution of the gene encoding mitochondrial intermediate peptidase and
RT   its cosegregation with the A mating-type locus of mushroom fungi.";
RL   Fungal Genet. Biol. 41:381-390(2004).
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; AY179561; AAO61500.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Y5M7; -.
DR   SMR; Q6Y5M7; -.
DR   PRIDE; Q6Y5M7; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.10; -; 1.
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   Transit peptide; Zinc.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..772
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000343201"
FT   ACT_SITE        557
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         560
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         563
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   772 AA;  86698 MW;  3ACB37CE292B2ED0 CRC64;
     MLARPSTTVL ARRPFFRFRG CLNEPRPTKA RCLATAATHH QIPSTVDDKA LVDLFDQPSL
     SKVRSHFHST GLFGHPSLTH PRSLVSLAES TLVRAQLLTQ RILDAKESED ELAHVVKNLD
     RLSDMLCGVI DLAELVRNAH PDRLWVEAGN HAYETLCEFM NVLNTHTGLN DTLKTVLSNP
     TLVKSLDPEA YQTALIFSRD FEKSGIDLPP ATRNKFVSLS SDILILGRQF LENASTPRPP
     TSVKASELAG LKDKGMGVRL QLQAQFTNRD LQVYPGSLQA QMIMRAAPNE EPRRKLYLAA
     NSSTPEQIHV LETLLKKRAE LAQLVGRDSF AHMTLDDKMA KKPEHVTNFL DALIDHTRPF
     ARNALRTLAQ RKQAHHNLPA LPVIQAWDRD FYCPPDPPAP PIPLPPLTIG TVFMGLSRLF
     RHLYGVSLRP AQAASGEVWH PDVQKLEVVD EQQGIIGWIY ADLFPRRGKA SGAAHYTVRC
     SRRTDDDDEA NDGMFEGTEL QIQESQQFEA VKRHRLPNQE GVYQLPLVVL LTEFARPSLS
     KGAAVLEWHE VQTLFHEMGH AMHSMLGRTE YQNVSGTRCA TDFVELPSIL MEHFLNSPAV
     LSLFDADNTT SLRQIGNHHN DPCHAIDTYS QIMLAVVDQV YHSPSVLNSS FDSTNEFANL
     VNKRGLIPYV PGTSFQTQFG HLFGYGATYY SYLFDRAIAS RVWSKVFSRD PLNRELGEQY
     KQEVLRWGGA RDPWEMVSTL LDQPELAAGD AEAMREVGRW RIEDEVGNSG RH