COQ9_RAT
ID COQ9_RAT Reviewed; 312 AA.
AC Q68FT1; A1L109;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE Flags: Precursor;
GN Name=Coq9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Binds a phospholipid of
CC at least 10 carbons in each acyl group. May be required to present its
CC bound-lipid to COQ7. {ECO:0000250|UniProtKB:O75208}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:Q8K1Z0}.
CC -!- SUBUNIT: Homodimer. Interacts with COQ7.
CC {ECO:0000250|UniProtKB:O75208}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}.
CC -!- DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid
CC metabolism regulator protein). {ECO:0000250|UniProtKB:O75208}.
CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR EMBL; AABR03113798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03113818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079370; AAH79370.1; -; mRNA.
DR EMBL; BC104702; AAI04703.1; -; mRNA.
DR EMBL; BC127449; AAI27450.1; -; mRNA.
DR RefSeq; NP_001030334.1; NM_001035257.1.
DR AlphaFoldDB; Q68FT1; -.
DR SMR; Q68FT1; -.
DR STRING; 10116.ENSRNOP00000021716; -.
DR iPTMnet; Q68FT1; -.
DR PhosphoSitePlus; Q68FT1; -.
DR jPOST; Q68FT1; -.
DR PaxDb; Q68FT1; -.
DR PRIDE; Q68FT1; -.
DR Ensembl; ENSRNOT00000094912; ENSRNOP00000078182; ENSRNOG00000016190.
DR GeneID; 498909; -.
DR KEGG; rno:498909; -.
DR UCSC; RGD:1586040; rat.
DR CTD; 57017; -.
DR RGD; 1586040; Coq9.
DR eggNOG; KOG2969; Eukaryota.
DR GeneTree; ENSGT00390000009328; -.
DR HOGENOM; CLU_057411_0_2_1; -.
DR InParanoid; Q68FT1; -.
DR OMA; WFLAGDK; -.
DR OrthoDB; 1304924at2759; -.
DR PhylomeDB; Q68FT1; -.
DR TreeFam; TF324653; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q68FT1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000016190; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q68FT1; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:RGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
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 Acetylation; Lipid-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..312
FT /note="Ubiquinone biosynthesis protein COQ9, mitochondrial"
FT /id="PRO_0000228639"
FT REGION 43..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235..238
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250|UniProtKB:O75208"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1Z0"
SQ SEQUENCE 312 AA; 35146 MW; 7A52D53775DDE649 CRC64;
MAATAAVSGV LRRLGWRLLQ LRCLPVARCQ SPLMPRAFHT AVGFRSSEEQ RQQPPHSSQQ
HSETQGPEFS RPPPRYTDQS GEEEEDYESE EQIQHRILTA ALEFVPDHGW TAEAIAEGAQ
SLGLSSAAAS MFGSDGSELI LHFVTQCNAR LNHVLEEEQK LVQLGQAEKR KTDQFLRDAV
ETRLRMLIPY IEHWPRALSI LLLPQNIPPS LSLLTSMVDD MWHYAGDQST DFNWYTRRAV
LAGIYNTTEL VMMQDSSPDF EDTWRFLDNR INDAMNMGHT AKQVKSTGEA LVQGLMGAAV
TLKNLTGLNQ RR
