PMIP_CANGA
ID PMIP_CANGA Reviewed; 761 AA.
AC Q6FW88;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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; OrderedLocusNames=CAGL0D02112g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380950; CAG58417.1; -; Genomic_DNA.
DR RefSeq; XP_445506.1; XM_445506.1.
DR AlphaFoldDB; Q6FW88; -.
DR SMR; Q6FW88; -.
DR STRING; 5478.XP_445506.1; -.
DR MEROPS; M03.006; -.
DR EnsemblFungi; CAG58417; CAG58417; CAGL0D02112g.
DR GeneID; 2887167; -.
DR KEGG; cgr:CAGL0D02112g; -.
DR CGD; CAL0128069; CAGL0D02112g.
DR VEuPathDB; FungiDB:CAGL0D02112g; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; Q6FW88; -.
DR OMA; VVYCDLF; -.
DR Proteomes; UP000002428; Chromosome D.
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:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
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..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..761
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338577"
FT ACT_SITE 548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 761 AA; 87333 MW; 89CA8567A26EC72E CRC64;
MLIQKILLNK EISRLPRILS ILNYTGLRWL SGSSGRNTTE LQRIFDDSKY WQSLSENTTQ
YTKETGLFKN PYLTSTDGLR QFSHDSLHKA HKLAEILRNS VSKEEKVHYI MNLDQLSDTL
CRVIDLCEFL RSAHPDQSYV EAAQMCHEEM FEFMNVLNTD VVLCNKLKEV LEDPEILKVL
SEEERKVGEI LLDDFEKSGI YMKAGIREQF IELSQQISVI GQEFINNTDY VAKEFIKVKR
DEMDKSGISP LLTARLNRDL TGKYYKIPTY GQIPLQILKS CPDEDIRKEV WAALHNCPKA
QIQRLNQLVR LRVILSNLLG KQSYSDYQLD NKMAGSPENV KGFIKTLMNV TKPLAARELE
FIARDKLNAP DSRHMSDNEI LSIVKPWDKN YFSSKYDSDN EMAMIRDEQL RYYFSLGNVI
NGLSELFKRI YGITLQPSRT ENGETWSPDV RRLDVISEEE GLVGVIYCDL FERVGKISNP
AHFTVCCSRQ VYPDENDFTT IQTGQNSDGT VFQLPVISLV CNFSTVALPN GNRTCFLHMN
EIETLFHEMG HAMHSMLGRT RLQNISGTRC ATDFVELPSI LMEHFARDIR VLRTIGSHYE
TSEPAPEALL NDYLDKTQFL QHCETYSQAK MAMLDQKLHG SFSLSDIERI DSAKIYQKLE
TRLQVLADDE SNWCGRFGHL FGYGATYYSY LFDRAIASKV WDSLFKDDPF NRTGGEKFKE
RVLKWGGLKN PWSCIADVLE KPDLAKGGAE AMTYIGDSED L
