PMIP_ASPNC
ID PMIP_ASPNC Reviewed; 799 AA.
AC A2QWM4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=An11g05710;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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; AM270239; CAK40728.1; -; Genomic_DNA.
DR RefSeq; XP_001394557.1; XM_001394520.2.
DR AlphaFoldDB; A2QWM4; -.
DR SMR; A2QWM4; -.
DR PaxDb; A2QWM4; -.
DR PRIDE; A2QWM4; -.
DR EnsemblFungi; CAK40728; CAK40728; An11g05710.
DR GeneID; 4984800; -.
DR KEGG; ang:ANI_1_762094; -.
DR VEuPathDB; FungiDB:An11g05710; -.
DR HOGENOM; CLU_001805_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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; PS00039; DEAD_ATP_HELICASE; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..799
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338572"
FT ACT_SITE 563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 799 AA; 88989 MW; BE7D0384194750AD CRC64;
MGASLLLPLR RRPWTCRTCL LQARRSLETA ASPATHRAAF DYLPSKNDAQ KKSDDDTLRR
VFDSQPFWRE FSQRSAAHLK PTGLVQNQYL TSPDGFRVFA TTTLQKCQAI VAKVLAGTTL
EDYQSMARDL DRLSDLLCRV IDLSDFIRVI HPDPRVQEAA TQAYALMFEY MNVLNTTTGL
NDQLKKAAAN PEVTARWSDE EKIVAQILIK DFSNSAIHMP PHARQRFVNL SNDISQLGNT
FVNAAEPAKS HVTVSANSLR GLDPILVQQI KRWNRTASVP SMGLIPRLAL RSVHDEGVRR
EVYLATRTSS ARQIQRLEQL LAKRAELAQL SGYDSFAHMT LSDKMAKSPE AVSNFLTSLV
GSNRPYVQEE LAQLQSMKGS AGRLQPWDHA YYVHQRVLQY SQSRRSRELS AVPEFFSLGT
VMQGLSRLFD RLYGVRLVPQ ETAAGETWNS DVRRLDVVDE ADRHIAVIYC DLFSRPNKHP
NPAHYTLRCA REISAEEVAE CATTMDASAH PNDGMATAVD RDAKTLRQLP TIALVCDFPE
PPATGTGRPS LLSEHSVRTL FHEMGHALHS ILGQTRLQSI SGTRCATDFA ELPSVLMERF
ATAPEVLALY ARHWETDAPL SESMMQHMEK DRTAHGSIYG AMENESQILM ALVDQAYHSL
PAGQATSIDS TAVFHQVSAE HCTLPDPTDT KPPTSWQGFF GHLHGYGATY YSYIFDRAIA
NKLWEDVFQQ GKAAVDRQAG ERYKNEVLRW GGGRNGWNCV AGVLGSAHPA NADGRLVEGG
DEAMREVGRW GLGRDGVSE
