PMIP_PICST
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 03-AUG-2022, entry version 87.
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; 4924.XP_001384676.2; -.
DR PRIDE; A3LUT4; -.
DR EnsemblFungi; ABN66647; ABN66647; PICST_89481.
DR GeneID; 4839065; -.
DR KEGG; pic:PICST_89481; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; A3LUT4; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
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 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..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