PMIP_ASPOR
ID PMIP_ASPOR Reviewed; 800 AA.
AC Q2UN31;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=AO090001000525;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007154; BAE57034.1; -; Genomic_DNA.
DR RefSeq; XP_001819036.1; XM_001818984.1.
DR AlphaFoldDB; Q2UN31; -.
DR SMR; Q2UN31; -.
DR STRING; 510516.Q2UN31; -.
DR PRIDE; Q2UN31; -.
DR EnsemblFungi; BAE57034; BAE57034; AO090001000525.
DR GeneID; 5991007; -.
DR KEGG; aor:AO090001000525; -.
DR VEuPathDB; FungiDB:AO090001000525; -.
DR HOGENOM; CLU_001805_0_0_1; -.
DR OMA; VVYCDLF; -.
DR Proteomes; UP000006564; Chromosome 2.
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:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..800
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338573"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 800 AA; 89243 MW; 474F93077541B66F CRC64;
MAGHMLMPLR RRPWTCRACL QRLQQPRRSL ETAASPSSQS DVYDYAPTNH STQKKSNDET
LRRVFDSQPF WREFSQRSAT QSKPTGLVQN QYLTNPDGFR AFANVSLQRC QAIVAKVLAA
STLEEYRDMA RDLDRLSDLL CRVIDLSDFI RVIHPDPRVQ EAATQAYALM FEYMNVLNTT
TGLNDQLKKA ASNPDVTSYW SEEEKIVAQI LIKDFSNSAI HMPPNERQRF VNLSNDISQL
GSNFVNSAEP AKSQVVVGAN SLRGLDPILV QQIRRWNRTA SVPTTGMIPR LALRSVHDEG
VRREVYLATR TSSSRQLHRL EELLSKRAEL AQLSGHASFG HMTLSDKMAK SPEAVSNFLT
ALVGSNREYV QEELSKLQAM KGGSPLQPWD HAYYVHQRVL QYSQSRRSRE LSAVPEFFSL
GTVMQGLSRL FDRLYGVRLV PQETAAGETW NPDVRRLDVV DEAERHIAVI YCDLFSRPNK
HPNPAHFTLR CAREISSEEV AECATMDHSA HPNDGMATAV DPQSKTLRQL PTIALVCDFA
EPPATGAGRP SLLSEHSVRT LFHEMGHALH SILGQTRLQS ISGTRCATDF AELPSVLMER
FATEPAVLSM YARHWQTDQP LSESMMLSME KDRLAHGSIY GAVENEAQIL MALVDQAYHS
IPADKAGQID STAIYHQVSS AHSTLPDPTD SRPPTSWQGF FGHLYGYGAT YYSYIFDRAI
ANKIWEDVFQ AGKAAVDREA GERYKNEVLR WGGGRNGWDC VAGVLGSANA ANANGRLAEG
GDEAMREVGR WGLGRDGVSG
