COA6_YEAST
ID COA6_YEAST Reviewed; 104 AA.
AC Q3E846; D6W072;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome c oxidase assembly factor 6 {ECO:0000303|PubMed:22984289};
GN Name=COA6 {ECO:0000303|PubMed:22984289};
GN OrderedLocusNames=YMR244C-A {ECO:0000312|SGD:S000004857};
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=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 [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 DOMAIN.
RX PubMed=20922212; DOI=10.1039/c0mb00058b;
RA Cavallaro G.;
RT "Genome-wide analysis of eukaryotic twin CX9C proteins.";
RL Mol. Biosyst. 6:2459-2470(2010).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION
RP [LARGE SCALE ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF CYS-25; TRP-26; CYS-35; CYS-57 AND CYS-68.
RX PubMed=24549041; DOI=10.1093/hmg/ddu069;
RA Ghosh A., Trivedi P.P., Timbalia S.A., Griffin A.T., Rahn J.J., Chan S.S.,
RA Gohil V.M.;
RT "Copper supplementation restores cytochrome c oxidase assembly defect in a
RT mitochondrial disease model of COA6 deficiency.";
RL Hum. Mol. Genet. 23:3596-3606(2014).
RN [9]
RP FUNCTION, AND INTERACTION WITH COX2.
RX PubMed=25959673; DOI=10.1016/j.cmet.2015.04.012;
RA Pacheu-Grau D., Bareth B., Dudek J., Juris L., Voegtle F.N., Wissel M.,
RA Leary S.C., Dennerlein S., Rehling P., Deckers M.;
RT "Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c
RT oxidase assembly links two mitochondrial cardiomyopathies.";
RL Cell Metab. 21:823-833(2015).
CC -!- FUNCTION: Involved in the maturation of the mitochondrial respiratory
CC chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps
CC of complex IV assembly. Mitochondrial respiratory chain complex IV or
CC cytochrome c oxidase is the component of the respiratory chain that
CC catalyzes the transfer of electrons from intermembrane space cytochrome
CC c to molecular oxygen in the matrix and as a consequence contributes to
CC the proton gradient involved in mitochondrial ATP synthesis. May also
CC be required for efficient formation of respiratory supercomplexes
CC comprised of complexes III and IV. {ECO:0000269|PubMed:22984289,
CC ECO:0000269|PubMed:24549041}.
CC -!- SUBUNIT: Interacts with COX2. {ECO:0000269|PubMed:25959673}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}. Note=Imported into the mitochondria via
CC the mitochondrial MIA40-ERV1 machinery. {ECO:0000269|PubMed:22984289}.
CC -!- DOMAIN: The Cx9C/Cx10C motifs are involved in the recognition by the
CC mitochondrial MIA40-ERV1 disulfide relay system and the subsequent
CC transfer of disulfide bonds by dithiol/disulfide exchange reactions to
CC the newly imported protein. {ECO:0000305|PubMed:20922212}.
CC -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; Z48756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006946; DAA10146.1; -; Genomic_DNA.
DR RefSeq; NP_013972.1; NM_001182751.1.
DR AlphaFoldDB; Q3E846; -.
DR SMR; Q3E846; -.
DR BioGRID; 35424; 75.
DR STRING; 4932.YMR244C-A; -.
DR MaxQB; Q3E846; -.
DR PaxDb; Q3E846; -.
DR PRIDE; Q3E846; -.
DR EnsemblFungi; YMR244C-A_mRNA; YMR244C-A; YMR244C-A.
DR GeneID; 855287; -.
DR KEGG; sce:YMR244C-A; -.
DR SGD; S000004857; COA6.
DR VEuPathDB; FungiDB:YMR244C-A; -.
DR eggNOG; ENOG502S7HF; Eukaryota.
DR HOGENOM; CLU_142408_0_0_1; -.
DR InParanoid; Q3E846; -.
DR OMA; SRDAYFA; -.
DR BioCyc; YEAST:G3O-32924-MON; -.
DR PRO; PR:Q3E846; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q3E846; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISS:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IDA:UniProtKB.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR Pfam; PF02297; COX6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..104
FT /note="Cytochrome c oxidase assembly factor 6"
FT /id="PRO_0000247793"
FT DOMAIN 22..76
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 25..35
FT /note="Cx9C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 57..68
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 25..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:20922212"
FT DISULFID 35..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:20922212"
FT MUTAGEN 25
FT /note="C->A: Loss of function. Localizes correctly to the
FT mitochondrion, but reduces the steady-state level of the
FT protein in the mitochondrial fraction."
FT /evidence="ECO:0000269|PubMed:24549041"
FT MUTAGEN 26
FT /note="W->C: Loss of function. Localizes correctly to the
FT mitochondrion, but severely reduces the steady-state level
FT of the protein in the mitochondrial fraction."
FT MUTAGEN 35
FT /note="C->A: Loss of function. Localizes correctly to the
FT mitochondrion, but reduces the steady-state level of the
FT protein in the mitochondrial fraction."
FT MUTAGEN 57
FT /note="C->A: Loss of function. Localizes correctly to the
FT mitochondrion, but reduces the steady-state level of the
FT protein in the mitochondrial fraction."
FT MUTAGEN 68
FT /note="C->A: Loss of function. Localizes correctly to the
FT mitochondrion, but severely reduces the steady-state level
FT of the protein in the mitochondrial fraction."
SQ SEQUENCE 104 AA; 12445 MW; 2EAEA1E69DB919DF CRC64;
MGLFSFDGGK KESQPPNTRS QRKLCWESRD AFFQCLDKAD ILDAMDPKNS KSIKSHCKVE
NEKFEENCAH SWIKYFKEKR VIDFKREQTI KRIEQEAKQR ERNQ
