PMIP_NEUCR
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 03-AUG-2022, entry version 103.
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; 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 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:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
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 GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..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