COA1_YEAST
ID COA1_YEAST Reviewed; 197 AA.
AC P40452; D6VVC9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome c oxidase assembly factor 1;
GN Name=COA1; Synonyms=FMP35; OrderedLocusNames=YIL157C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH COX1; COX14; MSS51 AND
RP SHY1.
RX PubMed=17882260; DOI=10.1038/sj.emboj.7601861;
RA Pierrel F., Bestwick M.L., Cobine P.A., Khalimonchuk O., Cricco J.A.,
RA Winge D.R.;
RT "Coa1 links the Mss51 post-translational function to Cox1 cofactor
RT insertion in cytochrome c oxidase assembly.";
RL EMBO J. 26:4335-4346(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH MSS51 AND
RP SHY1.
RX PubMed=17882259; DOI=10.1038/sj.emboj.7601862;
RA Mick D.U., Wagner K., van der Laan M., Frazier A.E., Perschil I.,
RA Pawlas M., Meyer H.E., Warscheid B., Rehling P.;
RT "Shy1 couples Cox1 translational regulation to cytochrome c oxidase
RT assembly.";
RL EMBO J. 26:4347-4358(2007).
CC -!- FUNCTION: Required for efficient assembly of cytochrome c oxidase in
CC the mitochondrial inner membrane. Involved in a step coupling MSS51-
CC dependent cotranslational insertion of COX1 to the addition of its heme
CC A and copper B cofactors. {ECO:0000269|PubMed:17882259,
CC ECO:0000269|PubMed:17882260}.
CC -!- SUBUNIT: Interacts with COX1, COX14, MSS51 and SHY1.
CC {ECO:0000269|PubMed:17882259, ECO:0000269|PubMed:17882260}.
CC -!- INTERACTION:
CC P40452; P39103: COX14; NbExp=2; IntAct=EBI-25287, EBI-5113;
CC P40452; P32335: MSS51; NbExp=3; IntAct=EBI-25287, EBI-11318;
CC P40452; P53266: SHY1; NbExp=5; IntAct=EBI-25287, EBI-17111;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the COA1 family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86121.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08395.1; -; Genomic_DNA.
DR PIR; S48377; S48377.
DR RefSeq; NP_012109.1; NM_001179505.1.
DR AlphaFoldDB; P40452; -.
DR SMR; P40452; -.
DR BioGRID; 34835; 92.
DR DIP; DIP-4708N; -.
DR IntAct; P40452; 6.
DR MINT; P40452; -.
DR STRING; 4932.YIL157C; -.
DR iPTMnet; P40452; -.
DR MaxQB; P40452; -.
DR PaxDb; P40452; -.
DR PRIDE; P40452; -.
DR EnsemblFungi; YIL157C_mRNA; YIL157C; YIL157C.
DR GeneID; 854649; -.
DR KEGG; sce:YIL157C; -.
DR SGD; S000001419; COA1.
DR VEuPathDB; FungiDB:YIL157C; -.
DR eggNOG; ENOG502RZQV; Eukaryota.
DR HOGENOM; CLU_092488_2_1_1; -.
DR InParanoid; P40452; -.
DR OMA; EFLIHEW; -.
DR BioCyc; YEAST:G3O-31405-MON; -.
DR PRO; PR:P40452; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40452; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR InterPro; IPR014807; Coa1.
DR InterPro; IPR042432; Coa1_fungi.
DR PANTHER; PTHR28523; PTHR28523; 1.
DR Pfam; PF08695; Coa1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..197
FT /note="Cytochrome c oxidase assembly factor 1"
FT /id="PRO_0000202954"
FT TOPO_DOM 1..73
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..197
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
SQ SEQUENCE 197 AA; 22044 MW; 2CE6635E5D043C37 CRC64;
MMLRLVTKGL PKVTPSAAKA VLVRGSLLHS FSTSARFNNS VAEDEAKIVL KDKNRPLRID
RELPDPTTER RKRIAGFLLF SVAIGSALSL IFNYEKTESP IISNTLYYIR RSPATKNILG
ESIEFDGIIP WVYGELNSVK GRINITFYIK GDKNVTGTVR LVADRNTHDE EFLIHEWSVT
AAGQKIDLLA ENTKTPI
