PMIP_COPC7
ID PMIP_COPC7 Reviewed; 776 AA.
AC A8N2T3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=CC1G_01835;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACS02000001; EAU92790.2; -; Genomic_DNA.
DR RefSeq; XP_001829155.2; XM_001829103.2.
DR AlphaFoldDB; A8N2T3; -.
DR SMR; A8N2T3; -.
DR STRING; 5346.XP_001829155.2; -.
DR EnsemblFungi; EAU92790; EAU92790; CC1G_01835.
DR GeneID; 6005581; -.
DR KEGG; cci:CC1G_01835; -.
DR VEuPathDB; FungiDB:CC1G_01835; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; A8N2T3; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR Proteomes; UP000001861; 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..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..776
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338580"
FT ACT_SITE 561
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 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 776 AA; 87377 MW; 359633EECC153F99 CRC64;
MLNSARTVLA RHSARQLYRF RGCLVHQQRH RHQVQRTLAT HVQRHLPASL DDKALVALFD
QPNGSKLRSP FNTTGLFGHP NLTHPRALVS LAESTLVRAQ LLTQRILEAG KSEHELAKVV
KNLDRLSDML CGVIDLAELV RNAHPDRLWV EAANHAYETL CEFMNVLNTH TGLYEVLKQV
LSNPTLVNSL SPEAYQTALI FWRDFEKSAI DLPPAQRNKF VSLSSDILVL GRQFLENAST
PRPPTSIKAS DLAGLKDKGM GVRLQLQAQF TNRDLQIYPG SLQAHMIMRS APNEEPRRRL
YLAANSSTQE QIEVLEALLK KRAELAQLVG RESFAHMTLD DKMAKTPDNV TNFLDALIDH
TRPFARSALR TLAQRKQAHH GLSSLPIIQA WDRDFYCPPD PPAPPIPLPP LTLGTVFMGL
SRLFRHLYGV SLRPVPSASG EVWHTDVQKL EVVDEDQGII GWIYADLFAR RGKASGAAHY
TVRCSRRTDD DDEQGDGMFE GAELQILESQ EFEAVKRHRL PNQEGVFQLP LVVLLCEFTR
PTVSKGGTIL EWHEVQTLFH EMGHAMHSML GRTEYQNVSG TRCATDFVEL PSILMEHFLN
SPAVLSLFDA DGTSTLRQIG NHHHDPCHAI DTYSQIMLAV VDQIYHSPTV LDPSFDSTRE
YGNLQNTRGL IPYVPGTSYQ TQFGHLFGYG ATYYSYLFDR AIASRVWSKV FSKDPLDREL
GEKYKREVLR WGGARDPWEM VATLLDAPEL AAGDAEAMRE VGRWRIEDEV GVGGRH
