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COA4_YEAST
ID   COA4_YEAST              Reviewed;          96 AA.
AC   Q05809; D6VYL8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Cytochrome oxidase assembly factor 4;
DE   AltName: Full=Cx9C motif-containing protein 3;
GN   Name=COA4; Synonyms=CMC3; OrderedLocusNames=YLR218C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   IDENTIFICATION OF PROBABLE INITIATION SITE, DOMAIN, FUNCTION, AND
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   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20624914; DOI=10.1128/mcb.00228-10;
RA   Bestwick M., Jeong M.Y., Khalimonchuk O., Kim H., Winge D.R.;
RT   "Analysis of Leigh syndrome mutations in the yeast SURF1 homolog reveals a
RT   new member of the cytochrome oxidase assembly factor family.";
RL   Mol. Cell. Biol. 30:4480-4491(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).
CC   -!- FUNCTION: Involved in cytochrome c oxidase assembly or stability.
CC       {ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20624914}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468,
CC       ECO:0000269|PubMed:20624914}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468,
CC       ECO:0000269|PubMed:20624914}; Intermembrane side
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468,
CC       ECO:0000269|PubMed:20624914}. Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:22984289}. Note=Imported into the mitochondria via
CC       the mitochondrial MIA40-ERV1 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 907 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COA4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB67446.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=DAA09534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14913; AAB67446.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006945; DAA09534.1; ALT_INIT; Genomic_DNA.
DR   PIR; S48568; S48568.
DR   RefSeq; NP_013319.1; NM_001182105.1.
DR   AlphaFoldDB; Q05809; -.
DR   BioGRID; 31485; 276.
DR   DIP; DIP-4791N; -.
DR   MINT; Q05809; -.
DR   STRING; 4932.YLR218C; -.
DR   MaxQB; Q05809; -.
DR   PaxDb; Q05809; -.
DR   PRIDE; Q05809; -.
DR   GeneID; 850915; -.
DR   KEGG; sce:YLR218C; -.
DR   SGD; S000004208; COA4.
DR   eggNOG; KOG4138; Eukaryota.
DR   HOGENOM; CLU_123495_0_0_1; -.
DR   InParanoid; Q05809; -.
DR   BioCyc; YEAST:G3O-32332-MON; -.
DR   PRO; PR:Q05809; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05809; 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:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR   GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:SGD.
DR   InterPro; IPR039870; Coa4-like.
DR   PANTHER; PTHR13639; PTHR13639; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Repeat.
FT   CHAIN           1..96
FT                   /note="Cytochrome oxidase assembly factor 4"
FT                   /id="PRO_0000247207"
FT   DOMAIN          36..77
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           39..49
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           59..69
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        39..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        49..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   96 AA;  11239 MW;  CF7B3A4415C87A9C CRC64;
     MSETGETSEY YKQALEEYKE VQEDEDPDVW DTRISKTGCY VENLALQLCH AETGDWRQCF
     NEMALFRKCW EKNGNRERVS TVDVDGTTSK DSEKKK
 
 
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