ID   PMIP_NEUCR              Reviewed;         805 AA.
AC   Q7SDD5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 108.
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=oct-1; ORFNames=NCU02063;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA34783.1; -; Genomic_DNA.
DR   RefSeq; XP_964019.1; XM_958926.2.
DR   AlphaFoldDB; Q7SDD5; -.
DR   SMR; Q7SDD5; -.
DR   STRING; 367110.Q7SDD5; -.
DR   PaxDb; 5141-EFNCRP00000001042; -.
DR   EnsemblFungi; EAA34783; EAA34783; NCU02063.
DR   GeneID; 3880168; -.
DR   KEGG; ncr:NCU02063; -.
DR   VEuPathDB; FungiDB:NCU02063; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; Q7SDD5; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..805
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338590"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         578
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         582
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         585
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   805 AA;  91095 MW;  8F2F597AB9BD2130 CRC64;
     MIQPLVKASR PRLWVCSDCL LRRTLSPLLR QQRRRFTGFT AHAPKTLTGT IPVTHKNGDT
     KHDDSLLRSI FDSPETWKQF SGDKHGRNVG LFRNAYLTSP HGFLDFAHVS LGKARALVDK
     VLNAQSLDEY RAIVRHLDRL SDILCRVLDM ADFVRVTHPD QQIQRTASMA WDMMYEYMNQ
     LNTMTGLYDQ LVQAMDNPQV STTWSEEERM VAEVLKLDFA KSAVHLPKDA RDKFVHLSSA
     ISQTGTNFIQ HMEPKIPYTT VEKSRMMGMD PVEVKRMASM GKVYVQTLSP QASIALRTVR
     DDHARHQLFM ASRTASRRTV HTLEELMLLR GESAKLSGFE SYGHLVLHDR MMASTPESVR
     QFLQALSENT RPQAQQEVAD LTAAKRAHKG GDATLEPWDK DFYAESIRQA IKSRQKREDL
     SSYFSLGTVM QGLSRIFTRL YGIRFVPREP MPGETWHPDV RRLDVVSDVE GHVAVLYCDL
     FYRPLKSPNP AHFTLRCSRE LSPHEIAETA HTQAENPHVL IPSFESAEFA ANDGMAYSRS
     QDGAIKQLPT IALVCDFPQQ SHNRPALLSF FQLETLFHEM GHAIHSILAR TSFQNVSGTR
     CATDLAELPS TLMEYFAADP SVLALFARHY ETDNPLPYEW VDNKIREARR FEALDTENQI
     ILAMLDQELH SSKAVQGHID STEIFHSLQR QFSTAPPDPQ GTAWQGFFGH LVGYGSTYYS
     YLFDRVLAQR VWNVVFNSGQ GGAALQRENG ERLKENLLKW GGSKDPWKCL AGALKDERLE
     GGGEKAMKLV GSWGGQRGTK SDQAV
//