ID PMIP_EREGS Reviewed; 776 AA.
AC Q753X4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 119.
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=AFR198W;
OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53569.1; -; Genomic_DNA.
DR RefSeq; NP_985745.1; NM_211099.1.
DR AlphaFoldDB; Q753X4; -.
DR SMR; Q753X4; -.
DR STRING; 284811.Q753X4; -.
DR MEROPS; M03.006; -.
DR EnsemblFungi; AAS53569; AAS53569; AGOS_AFR198W.
DR GeneID; 4622005; -.
DR KEGG; ago:AGOS_AFR198W; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; Q753X4; -.
DR OMA; ALMFEYM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..776
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338568"
FT REGION 48..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 776 AA; 88597 MW; 78E4201F03A2B72F CRC64;
MFVRFYKRLD RQYIQSQRRW ILSSNKCLLQ GNKNATISPL RRAFDDQDHW EESQAQNTSS
EQDNKGKNSS YFWSRSKATA PQVAHTGLFQ NPYLNSPEGL RKFANKSLTE ATALVRNLRE
DSSQEGLVRY IIRLDQLSDI LCRVIDLCEF LRAAHPDEQF VAAAQECHEQ MFEIMNILNT
DVVLCKRLKQ VLSDENISSK LSSEEIRVGH ILLEDFEKAG AYASPEVRKQ FIQLSQNISI
IGQDFINNTE SLSSSYIKIP CKDLESSGTS HLVLRQLTKD TMGNNYKIPT SGYAPYTLLN
ACPSEAIRRQ VWTAMFSCSE KQVKRLKSLL QLRRKLANIM GATDYVSYQL EGKMAKSPEN
VKNFLNTLVD HTKPLAAGEL EELAKLKRNV ENLSETNTLK LMRPWDRDYY SSLSPNFTRP
NHRVDGFTSI NTYFSLGVVM QGISDLFRDI YGISLKPVVA QAGETWAPDV RKLQVISETE
GIIGLIYCDL LERPGKTTSP SHFTVCCSRQ IYPEENDFST IQVGENPDGS RFQMPVISLI
CNFRATRHGK NKSLCLLELS DVETLFHEMG HALHSMLGRT QLQNLSGTRC VTDFVELPSI
LMEHFAKDRR VLLRISSNYA TGEPIPEELL SAFQEQNNFL KNTETFSQIK MSMLDQRLHS
ITDQDDIIAV YHGLEREMEV LVDDQTNWCG RFGHLFGYGA SYYSYLMDRA IAAKIWDHLF
KKDPFSRSSG EKFKEGVLKW GGSRDAWQCI ADALDEPRLV KGDDWAMRFI GEVEDM
//
