ID   PMIP_PICST              Reviewed;         812 AA.
AC   A3LUT4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 92.
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=PICST_89481;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000499; ABN66647.2; -; Genomic_DNA.
DR   RefSeq; XP_001384676.2; XM_001384639.1.
DR   AlphaFoldDB; A3LUT4; -.
DR   SMR; A3LUT4; -.
DR   STRING; 322104.A3LUT4; -.
DR   GeneID; 4839065; -.
DR   KEGG; pic:PICST_89481; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A3LUT4; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000002258; Chromosome 5.
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; 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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..812
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338593"
FT   REGION          19..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         602
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   812 AA;  92517 MW;  54B0D82CDCD7BB7B CRC64;
     MRLSRQLLRS TPFLTRAKPV SGKVSHFRSR TDLKGGSSNS SKSPDSVGDG ASAHLRHIFD
     DQKYFNSFTK SAAETSGKVS SLPAIFSFRR SGLFCNDNLS TPHGLIDFSK NSLREAKSLV
     ESMLHDVKSD PAGRLSYINK LDQLSDILCR VIDVAEFIRV AHPSQKWVNA AQQTHEIMFE
     YMNQLNTNVE LYQNLRDILS DSSVTAQLTE EEIQVGEYLK QDFERSGIHM NPSARNNFVA
     ITQEISLLGS RFNNEIHNLK SYWCEIPRYE FEQLEDSNLK KEILGYQSKA PPSKHSSQTI
     SIPLVGHIPF TILTTCSIES IRREIWISLH NSSDEQIATL NNFLKYRATL AKMLGYKSFS
     HYQLEHKMAK NPENVVTFLT NLQKSLREKG VTEEIKKLYQ YRDDSTISQV QKASTEDIID
     GVKPWDRDYL LEKLQKASNK NLEELENINE YLSVGTIVAG LSELFKSIYN VEFVPVATLK
     GETWDQNQVR KVAVVDDSTK KKLGFLYLDF WSPKVLPSHF TIVCSRKLNL DIKSETKDKM
     RQLVQLDEDE TSQLPVISLI CNFQKSNDGH IGRFAGVENE KPTLLSLNQV DTVFHEMGHA
     MHSMIGRTDL HNLSGTRCAT DFVELPSVLM ESFSKDPRVL CKIAKHYETG EPLSPKLLAQ
     HQTQKVMLDE CETYMQSKMA MLDQVLHSED VVRTISEDFA NFDSTPIYHS LESKLKVFAD
     TWSTWHGKFP HLFSYGAVYY SYLLDRAIAE KIWNGLFAHD PWSREAGEKY KNSILKWGGT
     RDPWECLADA LENDELSKGD SRAMEIIGKD SL
//