IMP2_YEAST
ID IMP2_YEAST Reviewed; 177 AA.
AC P46972; D6VZL0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2;
DE EC=3.4.21.-;
GN Name=IMP2; OrderedLocusNames=YMR035W; ORFNames=YM9973.09;
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].
RX PubMed=8266095; DOI=10.1126/science.8266095;
RA Nunnari J., Fox T.D., Walter P.;
RT "A mitochondrial protease with two catalytic subunits of nonoverlapping
RT specificities.";
RL Science 262:1997-2004(1993).
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 51-62, 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-41; LYS-91; ASP-124 AND ASP-131.
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-95 AND GLY-123.
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. IMP2 substrates include nuclear encoded CYB2,
CC mitochondrially encoded COX2 and cytochrome c1. Required for the
CC stability of IMP1. {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 -!- INTERACTION:
CC P46972; Q05930: MDM30; NbExp=2; IntAct=EBI-9231, EBI-31799;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC membrane protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49213; CAA89151.1; -; Genomic_DNA.
DR EMBL; AY692994; AAT93013.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09934.1; -; Genomic_DNA.
DR PIR; S53952; S53952.
DR RefSeq; NP_013749.1; NM_001182532.1.
DR AlphaFoldDB; P46972; -.
DR SMR; P46972; -.
DR BioGRID; 35207; 309.
DR ComplexPortal; CPX-1892; Mitochondrial inner membrane peptidase complex.
DR DIP; DIP-1941N; -.
DR IntAct; P46972; 4.
DR MINT; P46972; -.
DR STRING; 4932.YMR035W; -.
DR MEROPS; S26.012; -.
DR TCDB; 9.B.391.1.1; the eukaryotic inner membrane peptidase complex (impc) family.
DR MaxQB; P46972; -.
DR PaxDb; P46972; -.
DR PRIDE; P46972; -.
DR EnsemblFungi; YMR035W_mRNA; YMR035W; YMR035W.
DR GeneID; 855051; -.
DR KEGG; sce:YMR035W; -.
DR SGD; S000004638; IMP2.
DR VEuPathDB; FungiDB:YMR035W; -.
DR eggNOG; KOG1568; Eukaryota.
DR GeneTree; ENSGT00550000075044; -.
DR HOGENOM; CLU_028723_4_1_1; -.
DR InParanoid; P46972; -.
DR OMA; IVWPPQR; -.
DR BioCyc; YEAST:G3O-32740-MON; -.
DR PRO; PR:P46972; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P46972; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IC:ComplexPortal.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR037730; IMP2.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR46041; PTHR46041; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..177
FT /note="Mitochondrial inner membrane protease subunit 2"
FT /id="PRO_0000109538"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 41
FT /evidence="ECO:0000250"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT MUTAGEN 41
FT /note="S->A,T: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 91
FT /note="K->H,R: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 95
FT /note="G->D: Reduces processing of CYB2 and presence of
FT IMP1 and SOM1 in the IMP complex."
FT /evidence="ECO:0000269|PubMed:15118906"
FT MUTAGEN 123
FT /note="G->S: Reduces processing of cytochrome c1; no effect
FT on presence of IMP1 and SOM1 in the IMP complex."
FT /evidence="ECO:0000269|PubMed:15118906"
FT MUTAGEN 124
FT /note="D->N,Y: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
FT MUTAGEN 131
FT /note="D->N,E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10608835"
SQ SEQUENCE 177 AA; 19930 MW; 2335F334D8E9A552 CRC64;
MFRAGSSKRF LRNTLIAISW VPVLLTINNN VVHIAQVKGT SMQPTLNPQT ETLATDWVLL
WKFGVKNPSN LSRDDIILFK APTNPRKVYC KRVKGLPFDT IDTKFPYPKP QVNLPRGHIW
VEGDNYFHSI DSNTFGPISS GLVIGKAITI VWPPSRWGTD LKLSTGRDCI SKRAILE
