ID   PMIP_CANAL              Reviewed;         783 AA.
AC   Q59RK9; A0A1D8PPC3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   13-SEP-2023, entry version 103.
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=CAALFM_C600340CA;
GN   ORFNames=CaO19.1195, CaO19.8786;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017628; AOW29983.1; -; Genomic_DNA.
DR   RefSeq; XP_712312.2; XM_707219.2.
DR   AlphaFoldDB; Q59RK9; -.
DR   SMR; Q59RK9; -.
DR   STRING; 237561.Q59RK9; -.
DR   EnsemblFungi; C6_00340C_A-T; C6_00340C_A-T-p1; C6_00340C_A.
DR   GeneID; 3646074; -.
DR   KEGG; cal:CAALFM_C600340CA; -.
DR   CGD; CAL0000183469; OCT1.
DR   VEuPathDB; FungiDB:C6_00340C_A; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q59RK9; -.
DR   OrthoDB; 735202at2759; -.
DR   PRO; PR:Q59RK9; -.
DR   Proteomes; UP000000559; Chromosome 6.
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:0006879; P:intracellular iron ion homeostasis; IEA:EnsemblFungi.
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   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..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..783
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338576"
FT   ACT_SITE        566
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         569
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         572
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   783 AA;  89388 MW;  1FFEF3589BA8DB51 CRC64;
     MKAGIPLSRC TQRIPLLVAR QVSRNITTTT TKFSLAPEYN HIRKVFDSQK YFNHFTKQGS
     HATLFSSPQT GLFHNEYLTT PQGLVDFSQQ SLSQAKQLVS EMLSQVNTVD GKLKFIKKLD
     QLSDILCRVI DVAEFIRVVH PSVKWINAAQ QTHEMMFEFM NQLNTNVELY SSLRDILNNP
     LITEQLTPEE IKVGEYLRQD FERSGIHMDP QTRENFVTIT QEISLLGSQF GNQINGLKSY
     WCPVTVAEWE SIEDPQLKKE IKNYQSKYDG IRQSETIQIP LVANIPYTIL TNCSSDTLRK
     KVWVALHNSP DEQIETLNRF ISYRALLSKM LNYKSFADYQ LEHKMAKTPE NVITFLFNLQ
     KSLIKKGVVE ELSQLSEIKH NGSGSASVND IVNDIKPWDR DYLLARLQQR MQSEVSAGNV
     KEYFSVGTVI AGLNELFTRL YDISFVPMAA LKGETWDSHQ VRKIKVVDNA ANKTLGFLYL
     DFWSTKVLPS HFTIVCSRRL NTSIGSETIE GMEKLVQLDE DYQLPVVSLV CNFASSGNFS
     FGRFAGVENE KPTLLTLDQV DTIFHEMGHA MHSMIGRTEL HNLSGTRCST DFVELPSVLM
     ESFSKDPRVI CQIGRHFDTD EKLPESLLGQ AHEHRIMLDA CETFMQSKMA MLDQKLHNEE
     MVNLLAKGLY EVDSTKVYHS VEKELKVFAD EWSTWHGKFP HLFSYGAVYY SYLLDRAIAD
     KIWQGLFAKD PWNGEAGKKY KESVLKWGGT RDPWECLADA LGNDELKQGD SRAMEIIGQN
     SNL
//