ID PMIP_ASPTN Reviewed; 802 AA.
AC Q0CI79;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 22-FEB-2023, entry version 83.
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=ATEG_06605;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=EAU33149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAU33149.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH476602; EAU33149.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215783.1; XM_001215783.1.
DR AlphaFoldDB; Q0CI79; -.
DR SMR; Q0CI79; -.
DR STRING; 341663.Q0CI79; -.
DR EnsemblFungi; EAU33149; EAU33149; ATEG_06605.
DR GeneID; 4322361; -.
DR eggNOG; KOG2090; Eukaryota.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; 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..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..802
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338574"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 565
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"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 802 AA; 89472 MW; 3E92F4BA281CEB5F CRC64;
MGGPKLLMPL RPRPWTCRTC LQRLHSARRS LKTAASPSPQ STSFEYNRSA HNTQKSTTDD
ETLRRVFDSP SFWKEFSQRS SLHTKPTGLV QNQYLTSPEG FRTFANVSLH KCQAIVHKVL
AASTLEEYRD MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFDYMNVLN
TTTGLNDQLK KAAANPDVTS HWSAEEKIVA QILIKDFSNS AIHMPPNERQ RFVNLSNEIS
QLGSNFVNAA EPAKSHVVVG TNSLRGLDPL LVQQIKRWNR TASVPTMGMI PRLVLRSVHD
EGVRKDVYLA TRTSSSRQIK RLEQLLAKRA ELAQLSGYAS FGHMTLSDKM AKSPEAVSNF
LTSLVGSNRQ FVHEELAQLQ GMKGSSPLQA WDHAYYVHQR VMQYSQSRRS RELSIVPEFF
SLGTVMQGLS RLFNRLYGVR LVPQETAPGE TWNPDVRRLD VVDEAERHIA VIYCDLFSRP
NKHPNPAHFT LRCSREISNQ EVAECASMDQ SAHPNDGMAT AVDPQSKTLR QLPTIALVCD
FPDPPATSAG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM
ERFATAPEVL SMYARHWQTD QPLSENMMRS MEQDRTAHGS IYGAVENEAQ ILMALVDQAY
HSVPAEAAGK IDSTAIYHQV SQAHSSLPEP SDTQPPTSWQ GFFGHLYGYG ATYYSYIFDR
AIANKLWEDV FQSGQASVDR NAGERYKNEV LRWGGGRNGW DCVAGVLGSG NPSNADGRLV
EGGDDAMREV GRWGLGRDGV SG
//
