ID   PMIP_CANGA              Reviewed;         761 AA.
AC   Q6FW88;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 111.
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=CAGL0D02112g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
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; CR380950; CAG58417.1; -; Genomic_DNA.
DR   RefSeq; XP_445506.1; XM_445506.1.
DR   AlphaFoldDB; Q6FW88; -.
DR   SMR; Q6FW88; -.
DR   STRING; 284593.Q6FW88; -.
DR   MEROPS; M03.006; -.
DR   EnsemblFungi; CAGL0D02112g-T; CAGL0D02112g-T-p1; CAGL0D02112g.
DR   GeneID; 2887167; -.
DR   KEGG; cgr:CAGL0D02112g; -.
DR   CGD; CAL0128069; CAGL0D02112g.
DR   VEuPathDB; FungiDB:CAGL0D02112g; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q6FW88; -.
DR   OMA; ALMFEYM; -.
DR   Proteomes; UP000002428; Chromosome D.
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:0006879; P:intracellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..761
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338577"
FT   ACT_SITE        548
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         547
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         551
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         554
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   761 AA;  87333 MW;  89CA8567A26EC72E CRC64;
     MLIQKILLNK EISRLPRILS ILNYTGLRWL SGSSGRNTTE LQRIFDDSKY WQSLSENTTQ
     YTKETGLFKN PYLTSTDGLR QFSHDSLHKA HKLAEILRNS VSKEEKVHYI MNLDQLSDTL
     CRVIDLCEFL RSAHPDQSYV EAAQMCHEEM FEFMNVLNTD VVLCNKLKEV LEDPEILKVL
     SEEERKVGEI LLDDFEKSGI YMKAGIREQF IELSQQISVI GQEFINNTDY VAKEFIKVKR
     DEMDKSGISP LLTARLNRDL TGKYYKIPTY GQIPLQILKS CPDEDIRKEV WAALHNCPKA
     QIQRLNQLVR LRVILSNLLG KQSYSDYQLD NKMAGSPENV KGFIKTLMNV TKPLAARELE
     FIARDKLNAP DSRHMSDNEI LSIVKPWDKN YFSSKYDSDN EMAMIRDEQL RYYFSLGNVI
     NGLSELFKRI YGITLQPSRT ENGETWSPDV RRLDVISEEE GLVGVIYCDL FERVGKISNP
     AHFTVCCSRQ VYPDENDFTT IQTGQNSDGT VFQLPVISLV CNFSTVALPN GNRTCFLHMN
     EIETLFHEMG HAMHSMLGRT RLQNISGTRC ATDFVELPSI LMEHFARDIR VLRTIGSHYE
     TSEPAPEALL NDYLDKTQFL QHCETYSQAK MAMLDQKLHG SFSLSDIERI DSAKIYQKLE
     TRLQVLADDE SNWCGRFGHL FGYGATYYSY LFDRAIASKV WDSLFKDDPF NRTGGEKFKE
     RVLKWGGLKN PWSCIADVLE KPDLAKGGAE AMTYIGDSED L
//