PMIP_PICGU
ID PMIP_PICGU Reviewed; 786 AA.
AC A5DI46;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=PGUG_02947;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408157; EDK38849.2; -; Genomic_DNA.
DR RefSeq; XP_001485218.1; XM_001485168.1.
DR AlphaFoldDB; A5DI46; -.
DR SMR; A5DI46; -.
DR STRING; 4929.XP_001485218.1; -.
DR EnsemblFungi; EDK38849; EDK38849; PGUG_02947.
DR GeneID; 5127052; -.
DR KEGG; pgu:PGUG_02947; -.
DR VEuPathDB; FungiDB:PGUG_02947; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; A5DI46; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR Proteomes; UP000001997; 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; -; 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..786
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338592"
FT ACT_SITE 568
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"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 786 AA; 90517 MW; 784FAB0D1430E2E3 CRC64;
MSSILLRSYR HHAKVWTRPS SKSSFIRSLA SRSNPTSSFE HVRRVFDDDK YYQDFNNGTL
SRKIFSGPRT GLFKNEKLTT PQGLIDFSGQ CLTEAQTLVD TMIREAETSD QGKIHYIRRL
DQLSDILCRV IDVAEFIRVA HPNSKWTHAA QQTHELMFEY MNQLNTNVQL HTILGNILAD
KSITSKLSSE EIMVGEYLKQ DFERSGIYME PHTRENFVAL TQEISVLGSH FNNGIHELKD
YWCEISQQEY EAIDNADLKR EIRRFQQKSP RSSRNSVYIP LAGSLPYSIL QRCSMESVRR
KVWIALHNAS EEQISTLNLF LKYRATLSKM LGYESFAHYQ LEHKMAKNPE NVLTFLENLQ
RKMVDGENSG LISELESLYA MSNHWKPGAS KSDIIHAIQP WDRDYLLHKL QEEKKETQLD
DNISEYLSVG TIMSGLSQLF HSIYSIELLP EPSASGETWA SQVRKIKVFD NETQSTLGFL
YLDFWSPNVL PSHFTIVCSR QLNKDLGEKV EVMKPLVQLD ETESHQLPVI SLVCNFHQGN
SFIGRFAGLE TSKPTLLTLD QVDTIFHEMG HAMHSMIGRT KLQNLSGTRC STDFVELPSV
LMESFSKDPR VLGRIARHYS TNELLPHDIL AKHQHYRNVL ENSETYMQSK MAMLDQVLHG
KSIVKQLEMA RDDIDSTTMY HSLEKELKVF SDQWSTWHGK FPHLFSYGAV YFSYLFDRAI
AEKIWKSLFQ NDPWSREAGT TYKEAILKWG GTRDPWHCLA DALSNQELSK GDEKAMRIIG
GETKDL
