SOM1_YEAST
ID SOM1_YEAST Reviewed; 74 AA.
AC Q05676; D3DLJ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein SOM1, mitochondrial;
DE AltName: Full=Mitochondrial inner membrane protease subunit SOM1;
DE Flags: Precursor;
GN Name=SOM1; OrderedLocusNames=YEL059C-A; ORFNames=YEL059BC;
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], FUNCTION, AND IDENTIFICATION IN THE IMP
RP COMPLEX.
RC STRAIN=SC167;
RX PubMed=8879245; DOI=10.1007/bf02173009;
RA Esser K., Pratje E., Michaelis G.;
RT "SOM1, a small new gene required for mitochondrial inner membrane peptidase
RT function in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 252:437-445(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=15254042; DOI=10.1074/jbc.m406915200;
RA Liang H., Luo W., Green N., Fang H.;
RT "Cargo sequences are important for Som1p-dependent signal peptide cleavage
RT in yeast mitochondria.";
RL J. Biol. Chem. 279:39396-39400(2004).
CC -!- FUNCTION: Non-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. SOM1
CC facilitates cleavage of a subset of IMP substrates.
CC {ECO:0000269|PubMed:15254042, ECO:0000269|PubMed:8879245}.
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:8879245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X90459; CAA62083.1; -; Genomic_DNA.
DR EMBL; U18795; AAB65036.1; -; Genomic_DNA.
DR EMBL; AY558445; AAS56771.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07595.1; -; Genomic_DNA.
DR PIR; S72624; S72624.
DR RefSeq; NP_058154.3; NM_001180854.3.
DR AlphaFoldDB; Q05676; -.
DR BioGRID; 36670; 227.
DR ComplexPortal; CPX-1892; Mitochondrial inner membrane peptidase complex.
DR IntAct; Q05676; 1.
DR STRING; 4932.YEL059C-A; -.
DR TCDB; 9.B.391.1.1; the eukaryotic inner membrane peptidase complex (impc) family.
DR MaxQB; Q05676; -.
DR PaxDb; Q05676; -.
DR PRIDE; Q05676; -.
DR EnsemblFungi; YEL059C-A_mRNA; YEL059C-A; YEL059C-A.
DR GeneID; 856650; -.
DR KEGG; sce:YEL059C-A; -.
DR SGD; S000002954; SOM1.
DR VEuPathDB; FungiDB:YEL059C-A; -.
DR eggNOG; ENOG502SBH3; Eukaryota.
DR HOGENOM; CLU_160156_0_0_1; -.
DR InParanoid; Q05676; -.
DR OMA; NECHFDG; -.
DR BioCyc; YEAST:G3O-30351-MON; -.
DR PRO; PR:Q05676; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; Q05676; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IPI:SGD.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IC:ComplexPortal.
DR InterPro; IPR024645; Mitochondr_Som1.
DR Pfam; PF11093; Mitochondr_Som1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..74
FT /note="Protein SOM1, mitochondrial"
FT /id="PRO_0000022385"
SQ SEQUENCE 74 AA; 8416 MW; B41CBA3547954E97 CRC64;
MAPPTTIRTR DQALAPLATL DSQTNCRLKE LVQWECQFKG AEYVCSPFKR LFEHCIAPDK
SATNYEVTDT YTNS
