PMIP_CANAL
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 03-AUG-2022, entry version 98.
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 GeneID; 3646074; -.
DR KEGG; cal:CAALFM_C600340CA; -.
DR CGD; CAL0000183469; orf19.8786.
DR VEuPathDB; FungiDB:C6_00340C_A; -.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; Q59RK9; -.
DR OrthoDB; 642479at2759; -.
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:cellular 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 GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
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; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 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
