PMIP_DEBHA
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 03-AUG-2022, entry version 104.
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 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; 4959.XP_461760.2; -.
DR EnsemblFungi; CAG90217; CAG90217; DEHA2G04928g.
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; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
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 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..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
