ID   PMIP_VANPO              Reviewed;         787 AA.
AC   A7TSL2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 81.
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=Kpol_297p8;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480515; EDO14747.1; -; Genomic_DNA.
DR   RefSeq; XP_001642605.1; XM_001642555.1.
DR   AlphaFoldDB; A7TSL2; -.
DR   SMR; A7TSL2; -.
DR   FunCoup; A7TSL2; 663.
DR   STRING; 436907.A7TSL2; -.
DR   MEROPS; M03.006; -.
DR   GeneID; 5542774; -.
DR   KEGG; vpo:Kpol_297p8; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; A7TSL2; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 17530at2759; -.
DR   PhylomeDB; A7TSL2; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0034982; P:mitochondrial protein processing; IEA:EnsemblFungi.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:TreeGrafter.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR   CDD; cd06457; M3A_MIP; 1.
DR   FunFam; 3.40.390.10:FF:000055; Related to mitochondrial intermediate peptidase; 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..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..787
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338596"
FT   ACT_SITE        574
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         573
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         577
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         580
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   787 AA;  90031 MW;  478D339F977CF096 CRC64;
     MQNKVLRGIL FKNVPLGYSY NRSIRHPTFG NSIIRWASTQ VKTSSDVLQR SFDDHLYWTE
     INKQNYSSKE GWGSITKRLK GNKLTTNRSG LFNNEYLTSP EGLKLFSQVS LEKSQKIVDK
     LRSDRTPEGL RLYVQNLDLL SDTLCRVIDL CEFIRSSHPD YKFVEAAQDC YEEMFEFMNM
     LNTDVNLCFT LKHVLENKEI ASKLSEEELR VGRILLEDFE KSGIYMKPEV REQFITLSQS
     ISVIGQEFIS NTDFVKDNNV VVSCNQLDSL GIDPELLSQI EKDIAGKNYK IPTYGYIPFA
     LLKSCPSEEI REKIWVAVHN CSNEQIKRLT DLVKLRAVLS QLLGKKSYAE YQLEGKMAKN
     PKEVIEFIKT LMDFTKPMAA KELDGIAEKK LTIKSNGSNL SVCDILKTVR PWDRDYYSAI
     EREQTSAKNL YGSEEVLKYF TLGNVMQGLS NLFQKIYGIK LELDVPKIGE TWSPEVRKIN
     VISEDEGLIG IIYCDLFERS GKTSNAAHFT ICCSRDISPY ETEDSTTQIA IDSKGTRFQL
     PIISLVCNFS KTMISETDSV CFLHLPEVET LFHEMGHAMH SMLGRTKLQN ISGTRCATDF
     VELPSILMEY FARDPRVLET IGKHYLTKET VKREMLEPHL QDLKYLQHCE TYSQAKMAML
     DQTLHGETIS SHLDHLDVVK LYQDLERQLG VLVDDKSNWC GKFGHLFGYS AVYYSYLFDR
     AIASKIWGAL FERNPFSRAS GDKYRNSVLQ WGGSRDPWHC IASALDKPEL AKGDDEAIKY
     IGSTNQL
//