ID   PMIP_LACBS              Reviewed;         772 AA.
AC   B0CRC2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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; Synonyms=alpha-fg, MIP; ORFNames=LACBIDRAFT_181082;
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX   NCBI_TaxID=486041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686;
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547091; EDR15793.1; -; Genomic_DNA.
DR   RefSeq; XP_001874001.1; XM_001873966.1.
DR   AlphaFoldDB; B0CRC2; -.
DR   SMR; B0CRC2; -.
DR   STRING; 486041.B0CRC2; -.
DR   EnsemblFungi; EDR15793; EDR15793; LACBIDRAFT_181082.
DR   GeneID; 6069018; -.
DR   KEGG; lbc:LACBIDRAFT_181082; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   InParanoid; B0CRC2; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000001194; 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   Gene3D; 1.10.1370.10; -; 2.
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..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..772
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000338585"
FT   ACT_SITE        557
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         560
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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"
SQ   SEQUENCE   772 AA;  86856 MW;  8E4B2FA8D81D1F7F CRC64;
     MFANSARNAL KKRPQNLQPF RFQGCLFSKR ANRPLTTKVQ HLIYASVDDK ALVTLFDQPR
     STLRSPFATT GLFGHPSLTH PRALISLADA TVVRAQLLTD RILRARESRT ELLRVVKNLD
     RLSDMLCGVI DLAELVRNAH PDRSWVDAAN RAYETLCEFM NVLNTHVGLY EVLKAVLSDP
     SIVKTLGPEA HQTALIFWRD FEKSAIDLPA EQRKKFVSLS SDILVLGRQF LEGANAPRPP
     ASIKPSQLSG LKDKGMGVRL QLQAQFTQRD LQVYPGSLQA QMIMRSAPEE EPRRQVYLAA
     NSSTPQQIEV LEKLLRTRAE LARLVGRDSF AHMTLDDKMA KTPDNVWNFL DALMDHTKPF
     ARRALHTLSE RKQLHHGTSS LPIIQAWDRD FYCPPDPPAP PIPLPPLTLG TVFMGLSRLF
     QHMYGISLRP ADSASGEVWH TDVQKLEVVD QDQGIIGWIY ADLFARRGKA SGAAHYTVRC
     SRRTDDDDES SDGTVEGAEL LIYESQEFEA VKRHRLPNQD GIYQLPLVVL LCEFARPTPS
     KGPTVLEWHE VLTLFHEMGH AMHSMIGRTE YQNVAGTRCA TDFVEFPSIL MEHFLNSPTV
     LSLFDVDGTS TVRHIGNHHN DPCHFIDTYS QILLAAVDQV YHSPAVLDPT FDSTAELAKV
     HNTRGLIPYV PGTSFQTQFG HLYGYGATYY SYLLDRAIAS RVWRNVFLDD PLDRETGEKF
     KCEVLRFGGG KDPWKMVSAL LDVPELSTGD AEAMREIGRW KINSEIGVHG RH