ID   PMIP_COPC7              Reviewed;         776 AA.
AC   A8N2T3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   24-JAN-2024, entry version 78.
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 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000001; EAU92790.2; -; Genomic_DNA.
DR   RefSeq; XP_001829155.2; XM_001829103.2.
DR   AlphaFoldDB; A8N2T3; -.
DR   SMR; A8N2T3; -.
DR   STRING; 240176.A8N2T3; -.
DR   GeneID; 6005581; -.
DR   KEGG; cci:CC1G_01835; -.
DR   VEuPathDB; FungiDB:CC1G_01835; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A8N2T3; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 2.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
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   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..776
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338580"
FT   ACT_SITE        561
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         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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"
SQ   SEQUENCE   776 AA;  87377 MW;  359633EECC153F99 CRC64;
     MLNSARTVLA RHSARQLYRF RGCLVHQQRH RHQVQRTLAT HVQRHLPASL DDKALVALFD
     QPNGSKLRSP FNTTGLFGHP NLTHPRALVS LAESTLVRAQ LLTQRILEAG KSEHELAKVV
     KNLDRLSDML CGVIDLAELV RNAHPDRLWV EAANHAYETL CEFMNVLNTH TGLYEVLKQV
     LSNPTLVNSL SPEAYQTALI FWRDFEKSAI DLPPAQRNKF VSLSSDILVL GRQFLENAST
     PRPPTSIKAS DLAGLKDKGM GVRLQLQAQF TNRDLQIYPG SLQAHMIMRS APNEEPRRRL
     YLAANSSTQE QIEVLEALLK KRAELAQLVG RESFAHMTLD DKMAKTPDNV TNFLDALIDH
     TRPFARSALR TLAQRKQAHH GLSSLPIIQA WDRDFYCPPD PPAPPIPLPP LTLGTVFMGL
     SRLFRHLYGV SLRPVPSASG EVWHTDVQKL EVVDEDQGII GWIYADLFAR RGKASGAAHY
     TVRCSRRTDD DDEQGDGMFE GAELQILESQ EFEAVKRHRL PNQEGVFQLP LVVLLCEFTR
     PTVSKGGTIL EWHEVQTLFH EMGHAMHSML GRTEYQNVSG TRCATDFVEL PSILMEHFLN
     SPAVLSLFDA DGTSTLRQIG NHHHDPCHAI DTYSQIMLAV VDQIYHSPTV LDPSFDSTRE
     YGNLQNTRGL IPYVPGTSYQ TQFGHLFGYG ATYYSYLFDR AIASRVWSKV FSKDPLDREL
     GEKYKREVLR WGGARDPWEM VATLLDAPEL AAGDAEAMRE VGRWRIEDEV GVGGRH
//