ID   PMIP_PLEDJ              Reviewed;         785 AA.
AC   Q6Y5M5;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 70.
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   Pleurotus djamor (Pink oyster mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=34470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RV95/957.30;
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=RV95/957.30;
RX   PubMed=15219565; DOI=10.1016/j.fgb.2004.04.005;
RA   James T.Y., Liou S.-R., Vilgalys R.;
RT   "The genetic structure and diversity of the A and B mating-type genes from
RT   the tropical oyster mushroom, Pleurotus djamor.";
RL   Fungal Genet. Biol. 41:813-825(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; AY179563; AAO61502.1; -; Genomic_DNA.
DR   EMBL; AY462111; AAS46738.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6Y5M5; -.
DR   SMR; Q6Y5M5; -.
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   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 1.10.1370.40; -; 2.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..785
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000343203"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   785 AA;  87896 MW;  04FE374000BCB84C CRC64;
     MLTRPAQNAL LKSMQPLFRF RGCLLAKSTS TPRRDISTSS RKLAHPTTVP IPPSVDDHAL
     VALLDQPSSF GIVSRLFQTQ GGLFGHKELQ QPSGFITLAE ATLVRAQILT NRILRARESQ
     DELRKVVKNL DRLSDMLCGV IDLAELVRNA HPDRAWVEAA NQAYETLCEF MNVLNTDVGL
     YDVLKAVLSD PTIVQGMGPE EYSTAQIFWH DFEKSAINLP PEQRQRFVSL SSEILVLGRE
     FLQEANTARP PASIHASELA GLKDKGMGAR LQLQAQFTQK DLLVYPGSLQ AQMIMRCAPA
     EEPRRKLYIA ANSSTPSQIE LLERLLRTRA ELARLVGKES FAHMTLSDKM AKSPENVQYF
     LDALMDYTRP YARKALRTLS MRKQAHLQTP PFPTIQPWDR DFYCPPEPPA PPIPLPPLTL
     GTVFAGLSRL FYHLYGISLR PAECAPGEVW HPHVHKLEVV DEDAGVIGWI YADLFARRGK
     PSGAAHYTVR CSRRTDDDDE AEDGSIPAAE PYVRVSQSFE SSKRHRVRGQ DGEFQLPLVV
     LVCEFARPSV SSGPTVLDWH EVMTLFHEMG HAMHSMIGRT EYQNVSGTRC ATDFVELPSI
     LMEHFLSSPT VLSLFDVSSS TPSSAWQVGN HHQDPCHSID THSQILLAAM DQIYHSPSVV
     DPSFSSTSAL EALHKSRGLI PYVPGTSFQT QFGHLFGYGA TYYSYLFDRA IASRVWSQVF
     HANPLNRELG DKYKREVLKF GGGRDPWKMI SHLLDSPWLE NGNADAMKEV GQWRIEDEVG
     QPGRH
//