COXM2_YEAST
ID COXM2_YEAST Reviewed; 109 AA.
AC Q3E7A4; D6VPU0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=COX assembly mitochondrial protein 2;
DE AltName: Full=Cx9C motif-containing protein 2;
DE AltName: Full=Mitochondrial metallochaperone-like protein CMC2;
GN Name=CMC2; OrderedLocusNames=YBL059C-A;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19703468; DOI=10.1016/j.jmb.2009.08.041;
RA Longen S., Bien M., Bihlmaier K., Kloeppel C., Kauff F., Hammermeister M.,
RA Westermann B., Herrmann J.M., Riemer J.;
RT "Systematic analysis of the twin cx(9)c protein family.";
RL J. Mol. Biol. 393:356-368(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CMC1.
RX PubMed=20220131; DOI=10.1074/jbc.m110.104786;
RA Horn D., Zhou W., Trevisson E., Al-Ali H., Harris T.K., Salviati L.,
RA Barrientos A.;
RT "The conserved mitochondrial twin Cx9C protein Cmc2 Is a Cmc1 homologue
RT essential for cytochrome c oxidase biogenesis.";
RL J. Biol. Chem. 285:15088-15099(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP 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 [8]
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).
CC -!- FUNCTION: Required for mitochondrial cytochrome c oxidase (COX)
CC assembly and respiration. May be involved in copper trafficking and
CC distribution to mitochondrial COX and SOD1.
CC {ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20220131}.
CC -!- SUBUNIT: Interacts with CMC1. {ECO:0000269|PubMed:20220131}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20220131}; Peripheral
CC membrane protein {ECO:0000269|PubMed:19703468,
CC ECO:0000269|PubMed:20220131}; Intermembrane side
CC {ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20220131}.
CC Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
CC Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1
CC machinery.
CC -!- DOMAIN: The twin Cx9C 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:0000250}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CMC family. {ECO:0000305}.
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DR EMBL; Z23261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z35821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006936; DAA07060.1; -; Genomic_DNA.
DR RefSeq; NP_031358.1; NM_001184440.1.
DR AlphaFoldDB; Q3E7A4; -.
DR SMR; Q3E7A4; -.
DR BioGRID; 32639; 106.
DR IntAct; Q3E7A4; 1.
DR MINT; Q3E7A4; -.
DR STRING; 4932.YBL059C-A; -.
DR MaxQB; Q3E7A4; -.
DR PaxDb; Q3E7A4; -.
DR PRIDE; Q3E7A4; -.
DR EnsemblFungi; YBL059C-A_mRNA; YBL059C-A; YBL059C-A.
DR GeneID; 852220; -.
DR KEGG; sce:YBL059C-A; -.
DR SGD; S000007488; CMC2.
DR VEuPathDB; FungiDB:YBL059C-A; -.
DR eggNOG; KOG4148; Eukaryota.
DR HOGENOM; CLU_169286_3_1_1; -.
DR InParanoid; Q3E7A4; -.
DR OMA; GMCNFEK; -.
DR BioCyc; YEAST:G3O-29248-MON; -.
DR PRO; PR:Q3E7A4; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; Q3E7A4; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:SGD.
DR InterPro; IPR013892; Cyt_c_biogenesis_Cmc1-like.
DR PANTHER; PTHR22977; PTHR22977; 1.
DR Pfam; PF08583; Cmc1; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Chaperone; Copper; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat.
FT CHAIN 1..109
FT /note="COX assembly mitochondrial protein 2"
FT /id="PRO_0000248414"
FT DOMAIN 10..54
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 13..23
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 36..46
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 13..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 23..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 109 AA; 12947 MW; 5D740EFEC60E5E5F CRC64;
MHPQLEAERF HSCLDFINAL DKCHQKEYYK RIFGLCNNEK DALNKCLKEA SLNNKKRAVI
ESRIKRADVE KRWKKIEEEE YGEDAILKTI LDRQYAKKKQ ESDNDANSK
