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COXM1_YEAST
ID   COXM1_YEAST             Reviewed;         111 AA.
AC   P36064; D6VX60;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=COX assembly mitochondrial protein;
DE   AltName: Full=COX biogenesis factor CMC1;
DE   AltName: Full=Cx9C mitochondrial COX assembly protein 1;
DE   AltName: Full=Mitochondrial metallochaperone-like protein CMC1;
GN   Name=CMC1; OrderedLocusNames=YKL137W;
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=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   IDENTIFICATION OF FRAMESHIFTS.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18443040; DOI=10.1128/mcb.01920-07;
RA   Horn D., Al-Ali H., Barrientos A.;
RT   "Cmc1p is a conserved mitochondrial twin CX(9)C protein involved in
RT   cytochrome c oxidase biogenesis.";
RL   Mol. Cell. Biol. 28:4354-4364(2008).
RN   [6]
RP   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   [7]
RP   FUNCTION, AND INTERACTION WITH CMC2.
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   [8]
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).
CC   -!- FUNCTION: Required for mitochondrial cytochrome c oxidase (COX)
CC       assembly and respiration. Binds copper. May be involved in copper
CC       trafficking and distribution to mitochondrial COX and SOD1.
CC       {ECO:0000269|PubMed:18443040, ECO:0000269|PubMed:20220131}.
CC   -!- SUBUNIT: Interacts with CMC2. {ECO:0000269|PubMed:20220131}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:18443040, ECO:0000269|PubMed:19703468}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:18443040,
CC       ECO:0000269|PubMed:19703468}; Intermembrane side
CC       {ECO:0000269|PubMed:18443040, ECO:0000269|PubMed:19703468}.
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 259 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CMC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA81978.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z28137; CAA81978.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006944; DAA09026.1; -; Genomic_DNA.
DR   PIR; S37966; S37966.
DR   RefSeq; NP_012785.2; NM_001179703.1.
DR   AlphaFoldDB; P36064; -.
DR   BioGRID; 34000; 205.
DR   DIP; DIP-4543N; -.
DR   IntAct; P36064; 1.
DR   STRING; 4932.YKL137W; -.
DR   MaxQB; P36064; -.
DR   PaxDb; P36064; -.
DR   PRIDE; P36064; -.
DR   EnsemblFungi; YKL137W_mRNA; YKL137W; YKL137W.
DR   GeneID; 853721; -.
DR   KEGG; sce:YKL137W; -.
DR   SGD; S000001620; CMC1.
DR   VEuPathDB; FungiDB:YKL137W; -.
DR   eggNOG; KOG4624; Eukaryota.
DR   HOGENOM; CLU_147575_0_0_1; -.
DR   InParanoid; P36064; -.
DR   OMA; IKAYVEC; -.
DR   BioCyc; YEAST:G3O-31914-MON; -.
DR   PRO; PR:P36064; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36064; protein.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase 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..111
FT                   /note="COX assembly mitochondrial protein"
FT                   /id="PRO_0000203147"
FT   DOMAIN          39..82
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           42..52
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           64..74
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        42..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        52..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   111 AA;  13007 MW;  8934C73F1AB75632 CRC64;
     MEQNKDPQMI SKHSSRLPIW VLSPREEQQA RKNLKTETYK KCANFVQAMA DCAKANGMKV
     FPTCDKQRDE MKSCLLFYQT DEKYLDGERD KIVLEKINKL EKLCQKQSST K
 
 
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