ID   PMIP_DEBHA              Reviewed;         794 AA.
AC   Q6BJ61;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 109.
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=DEHA2G04928g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968;
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; CR382139; CAG90217.2; -; Genomic_DNA.
DR   RefSeq; XP_461760.2; XM_461760.1.
DR   AlphaFoldDB; Q6BJ61; -.
DR   SMR; Q6BJ61; -.
DR   STRING; 284592.Q6BJ61; -.
DR   GeneID; 2904636; -.
DR   KEGG; dha:DEHA2G04928g; -.
DR   VEuPathDB; FungiDB:DEHA2G04928g; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q6BJ61; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
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..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..794
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338583"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         581
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         585
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         588
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   794 AA;  90794 MW;  C4E8BCE83A403C84 CRC64;
     MRVTSSRLLQ GGSLVSRVLK RRLNNASRTK KGWFSTRTLA DSNEHLRRVF DDQAYFDNFT
     KSGAPEGAMN SLFGGNGVGL FRNRALISPQ GLVDFSEESL ERAKMLVSNM MAEVKTSEQG
     RLEYIKKLDQ LSDVLCRVID VAEFIRVSHP SQKWVDAAQR THEIMFEYMN QLNTNVELYE
     SLRDLLIDPA ITTKLSKEEI EVGEYLRQDF ERSGIHMDPN TRNNFVAITQ EISLLGSHFN
     NDIHSLESYW CNISRSEFDK ISDTVVKSEI YGYQSSSPAS QNKDSGNIYI PLAGHIPYTI
     LSKCEVESVR RKVWISLHNS PKEQIDTLNA FVKYRALLAK MLGYKSFAHY QLEHKMAKNP
     ENVLTLLRNL QQGLISKEYG VCEEVKKLHS FKNGDDAVMT DEEILEDVKP WDREYLLAQL
     QSQTLKDEEP LEDISEYFSV GTIVSGLSKL FYSIYNVNLI PEATLKGETW DSNQVRKLNV
     FDVTSNKKLG YLYLDFWSPK VLPSHFTIVC SRKLNTDIGS ESRDEMREMV QLDENEQHQL
     PVISLVCNLS KPQGTGVGRF TGMDSRKPTL LSLDQVDTIF HEMGHAMHSM IGKTDLHNLS
     GTRCVTDFVE LPSVLMESFS KDPRVLCKIA KHYRTKEPLS KETLAKHQSH RVLLEESETF
     MQSKMAMLDQ VLHNEDIINC GIKDFDSTAV YHHLESQLKV FADKWSTWHG KFPHLFSYGA
     VYYSYLLDRA IAEKIWHGLF KDDPWSREAG QKYKDSILKW GGTRDPWVCL ADALGDERLG
     KGDSKAMEII GQKV
//