ID   PMIP_YARLI              Reviewed;         776 AA.
AC   Q6CHD6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 106.
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; OrderedLocusNames=YALI0A09988g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(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; CR382127; CAG83853.1; -; Genomic_DNA.
DR   RefSeq; XP_499926.1; XM_499926.1.
DR   AlphaFoldDB; Q6CHD6; -.
DR   SMR; Q6CHD6; -.
DR   STRING; 284591.Q6CHD6; -.
DR   EnsemblFungi; CAG83853; CAG83853; YALI0_A09988g.
DR   GeneID; 2905768; -.
DR   KEGG; yli:YALI0A09988g; -.
DR   VEuPathDB; FungiDB:YALI0_A09988g; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q6CHD6; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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; 1.
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..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..776
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338597"
FT   ACT_SITE        562
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         565
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         568
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;  87572 MW;  60F6B023BA9AEF67 CRC64;
     MRRFSTLSRR LQRVVPASSA STANTSPSPA LYTGLEPKIK ESQDSLIRAV FDNGDVWQDF
     SQKSVAKPKQ SRSITGFINY LTNESDYETG LFMNDFLKTP AGFQKYTAAS IEEAGQLIQQ
     LLGALTQRDK LRHAITTFDR LSDVLCQVID LAEFIRAAHP EQHFVQAAQE AHEQMYEYMN
     VLNTSVELYT VLDMVFKDSE IVNQLTHEEK VVGTLLLEDF KKSGVTLDDA GRENFVSLTT
     KISLLGRDFI SSNHPKEDYI TLTQGEAQGL DPQLAQQLSQ GNSVYVPTGG VPGQLALRGM
     KNENSRKLLW SKMRESSDKS IESLEDLLVS RLELANLMGK ESYADYLLSD KMAGNPENVM
     RFLNGLLDKT LPGAKKELSV LEQIKKQATG NPKSILQAWD KSYYASQLLY QKRNKTKTAH
     MLSEYFSVGT VVQGLSRIFD KIYGIRFVPT ETKTGETWHH DVRRLDVVSE TEGLIGIMYA
     DLFQREGKSP NPAHFTVRCS REIYPDELAH MSSSPIAKVP TLNLNGKVFQ IPTIALICDF
     TTPHDLYPSL LSYQEVETLF HEMGHAIHSM LGRTSLHNVC GTRCATDFVE LPSVFMENFA
     SNPESLALFA RHYSSDSPLP YQQLERHLNE QSYFKDVEQY TQIKMAMLDQ VLHGNILKSI
     TNGHFNSQKL YDNLEKDRPL FPPSPSSWHG SFGHLFGYGA SYYCYLLDRQ MADIVWKKLF
     SKNPLSRDAG SRMKNEVLQW GGSRDPWECI AGVLEDPELA KGGSQAMEKI GNYDKH
//