ID   PMIP_COPDI              Reviewed;         773 AA.
AC   Q6Y5M6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Coprinellus disseminatus (Fairy ink cap fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinellus.
OX   NCBI_TaxID=71703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C345.1;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C345.1;
RX   PubMed=16461425; DOI=10.1534/genetics.105.051128;
RA   James T.Y., Srivilai P., Kuees U., Vilgalys R.;
RT   "Evolution of the bipolar mating system of the mushroom Coprinellus
RT   disseminatus from its tetrapolar ancestors involves loss of mating-type-
RT   specific pheromone receptor function.";
RL   Genetics 172:1877-1891(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY179562; AAO61501.1; -; Genomic_DNA.
DR   EMBL; DQ056143; AAZ14915.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Y5M6; -.
DR   SMR; Q6Y5M6; -.
DR   PRIDE; Q6Y5M6; -.
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..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..773
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000343200"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         557
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         561
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   773 AA;  86682 MW;  FA780288468F285A CRC64;
     MLGRAACKVL HRHALKNPYR FRGCLVAQKE TTRQLATHVQ HHLPASADDR LLVDLFDQPG
     ASTSKSSFAS TGLFGHPTLT HPGALISLAE ATLVRAQLLT ERILRARESR DELVKVVKNL
     DRLSDMLCGV IDLAELVRNA HPERLWMEAA NHAYETLCEF MNVLNTHVGL YEVLKVVLSD
     PSIVKTLSPE AYQTALIFWR DFEKSAIDLP PAERQKFVSL SSDILSLGRQ FLENANTPRP
     PTSIKASHLA GLKDQGMGVR LQLQARFTKK DLQVYPGSLQ AQMIMRSAPE EEPRRRIYIA
     SNSSTPEQIS VLEALLRKRA ELAQLIGRPS FAHLTLDDKM AKTPENVSNF LDALMDHTRP
     FARRALHTLA QRKQAHHNLP SLPVVQAWDR DFYCPPDPPA PPIPLPPLTL GTVFMGLSRL
     FRHLYGVSLR PAKSASGETW HADVQKLEVV DENQGIIGWI YADLFARRNK ASGAAHYTVR
     CSRRADDDDE AGDLTLEGEG HRIQESQAFE SVKRHRLPNQ DGVYQLPLVV LLTEFARPSI
     SRGPTVLEWY EVLTLFHEMG HAMHSMLGRT EYQNVSGTRC ATDFVELPSI LMEHFLNSPT
     VLSLFDADST TTLRATGNNH ADPCHSIDTY SQILLAAVDQ RYHSPSALDP SFDSTAELAN
     LHNTRGLMPY VPETSFQTQF GHLFGYGATY YSYLFDRAIA SRVWSKVFAE NPLDRSRGER
     LRGEVLMHGG ARDPWHMVSA LMKMPELESG DAEAMREVGK WRIEDEVGIS GRH