COQ9_YEAST
ID COQ9_YEAST Reviewed; 260 AA.
AC Q05779; D6VYK3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE Flags: Precursor;
GN Name=COQ9; OrderedLocusNames=YLR201C;
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 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, AND SUBCELLULAR LOCATION.
RX PubMed=16027161; DOI=10.1074/jbc.m503277200;
RA Johnson A., Gin P., Marbois B.N., Hsieh E.J., Wu M., Barros M.H.,
RA Clarke C.F., Tzagoloff A.;
RT "COQ9, a new gene required for the biosynthesis of coenzyme Q in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:31397-31404(2005).
RN [7]
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF LEU-135; MET-174; ASP-185; TRP-188;
RP TYR-189 AND LEU-204.
RX PubMed=25339443; DOI=10.1073/pnas.1413128111;
RA Lohman D.C., Forouhar F., Beebe E.T., Stefely M.S., Minogue C.E.,
RA Ulbrich A., Stefely J.A., Sukumar S., Luna-Sanchez M., Jochem A., Lew S.,
RA Seetharaman J., Xiao R., Wang H., Westphall M.S., Wrobel R.L.,
RA Everett J.K., Mitchell J.C., Lopez L.C., Coon J.J., Tong L.,
RA Pagliarini D.J.;
RT "Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to
RT enable coenzyme Q biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4697-4705(2014).
CC -!- FUNCTION: Lipid-binding protein involved in the biosynthesis of
CC coenzyme Q, also named ubiquinone, an essential lipid-soluble electron
CC transporter for aerobic cellular respiration.
CC {ECO:0000250|UniProtKB:O75208, ECO:0000269|PubMed:16027161,
CC ECO:0000269|PubMed:25339443}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:25339443}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16027161}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16027161}; Matrix side {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16027161}.
CC -!- MISCELLANEOUS: Present with 3420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR EMBL; U14913; AAB67447.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09519.1; -; Genomic_DNA.
DR PIR; S48553; S48553.
DR RefSeq; NP_013302.1; NM_001182088.1.
DR AlphaFoldDB; Q05779; -.
DR SMR; Q05779; -.
DR BioGRID; 31470; 199.
DR ComplexPortal; CPX-1155; CoQ biosynthetic complex.
DR DIP; DIP-3854N; -.
DR IntAct; Q05779; 6.
DR STRING; 4932.YLR201C; -.
DR iPTMnet; Q05779; -.
DR MaxQB; Q05779; -.
DR PaxDb; Q05779; -.
DR PRIDE; Q05779; -.
DR DNASU; 850898; -.
DR EnsemblFungi; YLR201C_mRNA; YLR201C; YLR201C.
DR GeneID; 850898; -.
DR KEGG; sce:YLR201C; -.
DR SGD; S000004191; COQ9.
DR VEuPathDB; FungiDB:YLR201C; -.
DR eggNOG; KOG2969; Eukaryota.
DR GeneTree; ENSGT00390000009328; -.
DR HOGENOM; CLU_057411_1_1_1; -.
DR InParanoid; Q05779; -.
DR OMA; SELFMAQ; -.
DR BioCyc; YEAST:G3O-32321-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q05779; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05779; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:UniProtKB.
DR GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IMP:SGD.
DR InterPro; IPR013718; COQ9.
DR InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR PANTHER; PTHR21427; PTHR21427; 1.
DR Pfam; PF08511; COQ9; 1.
DR TIGRFAMs; TIGR02396; diverge_rpsU; 1.
PE 1: Evidence at protein level;
KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..260
FT /note="Ubiquinone biosynthesis protein COQ9, mitochondrial"
FT /id="PRO_0000227686"
FT BINDING 189..192
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250|UniProtKB:O75208"
FT MUTAGEN 135
FT /note="L->E,K: Inability to grow on nonfermentable carbon
FT sources."
FT /evidence="ECO:0000269|PubMed:25339443"
FT MUTAGEN 174
FT /note="M->E: Impaired ability to grow on nonfermentable
FT carbon sources."
FT /evidence="ECO:0000269|PubMed:25339443"
FT MUTAGEN 185
FT /note="D->K: Inability to grow on nonfermentable carbon
FT sources."
FT /evidence="ECO:0000269|PubMed:25339443"
FT MUTAGEN 188
FT /note="W->K: Inability to grow on nonfermentable carbon
FT sources."
FT /evidence="ECO:0000269|PubMed:25339443"
FT MUTAGEN 189
FT /note="Y->D,K: Impaired ability to grow on nonfermentable
FT carbon sources."
FT /evidence="ECO:0000269|PubMed:25339443"
FT MUTAGEN 204
FT /note="L->K: Impaired ability to grow on nonfermentable
FT carbon sources."
FT /evidence="ECO:0000269|PubMed:25339443"
SQ SEQUENCE 260 AA; 29958 MW; 7B92318973210D67 CRC64;
MLCRNTARTG CKFFRLYHSN PIEHVKPIHI KPLTYGKESP QYKVLSLALQ KFVPEHGFSE
RSIVESLNEL GYPSSMISSI GAPNSPSFFH SSTAVMELIK FQLVDKRYRL TEGINPDVTP
QYKLPSLEHL LLKRLEMDKP IGGHLSELMS QLAIPSAFLF ETAIPELHRL SDDMIYFSNE
KDHHDSAWYA KRLAVSSTYI GSKLFMAQDK SHNYKETFTF AKDKLHRVMR LGEYYNNTEE
FAWYTLMSTV NLIKSQLVRG
