IMP1_YEAST
ID IMP1_YEAST Reviewed; 190 AA.
AC P28627; D6VZX2; E9P8W1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Mitochondrial inner membrane protease subunit 1;
DE EC=3.4.21.-;
GN Name=IMP1; Synonyms=PET2858; OrderedLocusNames=YMR150C;
GN ORFNames=YM9375.20C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-88.
RX PubMed=1886606; DOI=10.1007/bf00282462;
RA Behrens M., Michaelis G., Pratje E.;
RT "Mitochondrial inner membrane protease 1 of Saccharomyces cerevisiae shows
RT sequence similarity to the Escherichia coli leader peptidase.";
RL Mol. Gen. Genet. 228:167-176(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-16, AND SUBUNIT.
RX PubMed=8132591; DOI=10.1016/s0021-9258(17)37013-8;
RA Schneider A., Oppliger W., Jenoe P.;
RT "Purified inner membrane protease I of yeast mitochondria is a
RT heterodimer.";
RL J. Biol. Chem. 269:8635-8638(1994).
RN [6]
RP MUTAGENESIS OF SER-40; LYS-84; ARG-85; ASP-131 AND ASP-138.
RX PubMed=10608835; DOI=10.1074/jbc.274.53.37750;
RA Chen X., Van Valkenburgh C., Fang H., Green N.;
RT "Signal peptides having standard and nonstandard cleavage sites can be
RT processed by Imp1p of the mitochondrial inner membrane protease.";
RL J. Biol. Chem. 274:37750-37754(1999).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-88 AND GLY-130.
RX PubMed=15118906; DOI=10.1007/s00438-004-1011-y;
RA Esser K., Jan P.S., Pratje E., Michaelis G.;
RT "The mitochondrial IMP peptidase of yeast: functional analysis of domains
RT and identification of Gut2 as a new natural substrate.";
RL Mol. Genet. Genomics 271:616-626(2004).
CC -!- FUNCTION: Catalytic component of the mitochondrial inner membrane
CC peptidase (IMP) complex. IMP catalyzes the removal of signal peptides
CC required for the targeting of proteins from the mitochondrial matrix,
CC across the inner membrane, into the inter-membrane space. The two
CC catalytic IMP subunits seem to have non-overlapping substrate
CC specificities. IMP1 substrates include nuclear encoded CYB2,
CC mitochondrially encoded COX2, NADH-cytochrome b5 reductase and GUT2.
CC {ECO:0000269|PubMed:15118906}.
CC -!- SUBUNIT: Component of the mitochondrial inner membrane peptidase (IMP)
CC complex which at least consists of IMP1, IMP2 and SOM1.
CC {ECO:0000269|PubMed:8132591}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; S55518; AAB19704.1; -; Genomic_DNA.
DR EMBL; Z47071; CAA87365.1; -; Genomic_DNA.
DR EMBL; AY558415; AAS56741.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10046.1; -; Genomic_DNA.
DR PIR; S16817; S16817.
DR RefSeq; NP_013870.1; NM_001182652.1.
DR AlphaFoldDB; P28627; -.
DR SMR; P28627; -.
DR BioGRID; 35326; 82.
DR ComplexPortal; CPX-1892; Mitochondrial inner membrane peptidase complex.
DR DIP; DIP-8328N; -.
DR IntAct; P28627; 2.
DR STRING; 4932.YMR150C; -.
DR MEROPS; S26.002; -.
DR TCDB; 9.B.391.1.1; the eukaryotic inner membrane peptidase complex (impc) family.
DR PaxDb; P28627; -.
DR PRIDE; P28627; -.
DR EnsemblFungi; YMR150C_mRNA; YMR150C; YMR150C.
DR GeneID; 855182; -.
DR KEGG; sce:YMR150C; -.
DR SGD; S000004758; IMP1.
DR VEuPathDB; FungiDB:YMR150C; -.
DR eggNOG; KOG0171; Eukaryota.
DR GeneTree; ENSGT00550000075025; -.
DR HOGENOM; CLU_028723_4_3_1; -.
DR InParanoid; P28627; -.
DR OMA; CKGPSME; -.
DR BioCyc; YEAST:G3O-32841-MON; -.
DR PRO; PR:P28627; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P28627; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004175; F:endopeptidase activity; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IDA:SGD.
DR GO; GO:0006465; P:signal peptide processing; IC:ComplexPortal.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8132591"
FT CHAIN 2..190
FT /note="Mitochondrial inner membrane protease subunit 1"
FT /id="PRO_0000109537"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /evidence="ECO:0000250"
FT MUTAGEN 40
FT /note="S->A,T: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 84
FT /note="K->H,R: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 85
FT /note="R->A: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 88
FT /note="G->D: In pet ts2858; temperature-sensitive;
FT abolishes processing of CYB2 and presence of SOM1 in the
FT IMP complex."
FT /evidence="ECO:0000269|PubMed:15118906,
FT ECO:0000269|PubMed:1886606"
FT MUTAGEN 130
FT /note="G->S: Abolishes processing of CYB2 and COX2 and
FT presence of SOM1 in the IMP complex."
FT /evidence="ECO:0000269|PubMed:15118906"
FT MUTAGEN 131
FT /note="D->E,N: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 131
FT /note="D->Y: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 138
FT /note="D->N,E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT CONFLICT 178
FT /note="I -> V (in Ref. 4; AAS56741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21433 MW; 81B044C3B57DABB3 CRC64;
MTVGTLPIWS KTFSYAIRSL CFLHIIHMYA YEFTETRGES MLPTLSATND YVHVLKNFQN
GRGIKMGDCI VALKPTDPNH RICKRVTGMP GDLVLVDPST IVNYVGDVLV DEERFGTYIK
VPEGHVWVTG DNLSHSLDSR TYNALPMGLI MGKIVAANNF DKPFWDGSIR NIWGFKWINN
TFLDVQAKSN
