ID PMIP_PLEDJ Reviewed; 785 AA.
AC Q6Y5M5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 22-FEB-2023, entry version 70.
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; Synonyms=MIP;
OS Pleurotus djamor (Pink oyster mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=34470;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RV95/957.30;
RX PubMed=14761798; DOI=10.1016/j.fgb.2003.11.008;
RA James T.Y., Kuees U., Rehner S.A., Vilgalys R.;
RT "Evolution of the gene encoding mitochondrial intermediate peptidase and
RT its cosegregation with the A mating-type locus of mushroom fungi.";
RL Fungal Genet. Biol. 41:381-390(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RV95/957.30;
RX PubMed=15219565; DOI=10.1016/j.fgb.2004.04.005;
RA James T.Y., Liou S.-R., Vilgalys R.;
RT "The genetic structure and diversity of the A and B mating-type genes from
RT the tropical oyster mushroom, Pleurotus djamor.";
RL Fungal Genet. Biol. 41:813-825(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY179563; AAO61502.1; -; Genomic_DNA.
DR EMBL; AY462111; AAS46738.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Y5M5; -.
DR SMR; Q6Y5M5; -.
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; 1.10.1370.40; -; 2.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR033851; M3A_MIP.
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 Transit peptide; Zinc.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..785
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000343203"
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 785 AA; 87896 MW; 04FE374000BCB84C CRC64;
MLTRPAQNAL LKSMQPLFRF RGCLLAKSTS TPRRDISTSS RKLAHPTTVP IPPSVDDHAL
VALLDQPSSF GIVSRLFQTQ GGLFGHKELQ QPSGFITLAE ATLVRAQILT NRILRARESQ
DELRKVVKNL DRLSDMLCGV IDLAELVRNA HPDRAWVEAA NQAYETLCEF MNVLNTDVGL
YDVLKAVLSD PTIVQGMGPE EYSTAQIFWH DFEKSAINLP PEQRQRFVSL SSEILVLGRE
FLQEANTARP PASIHASELA GLKDKGMGAR LQLQAQFTQK DLLVYPGSLQ AQMIMRCAPA
EEPRRKLYIA ANSSTPSQIE LLERLLRTRA ELARLVGKES FAHMTLSDKM AKSPENVQYF
LDALMDYTRP YARKALRTLS MRKQAHLQTP PFPTIQPWDR DFYCPPEPPA PPIPLPPLTL
GTVFAGLSRL FYHLYGISLR PAECAPGEVW HPHVHKLEVV DEDAGVIGWI YADLFARRGK
PSGAAHYTVR CSRRTDDDDE AEDGSIPAAE PYVRVSQSFE SSKRHRVRGQ DGEFQLPLVV
LVCEFARPSV SSGPTVLDWH EVMTLFHEMG HAMHSMIGRT EYQNVSGTRC ATDFVELPSI
LMEHFLSSPT VLSLFDVSSS TPSSAWQVGN HHQDPCHSID THSQILLAAM DQIYHSPSVV
DPSFSSTSAL EALHKSRGLI PYVPGTSFQT QFGHLFGYGA TYYSYLFDRA IASRVWSQVF
HANPLNRELG DKYKREVLKF GGGRDPWKMI SHLLDSPWLE NGNADAMKEV GQWRIEDEVG
QPGRH
//
