ID COQ9_HUMAN Reviewed; 318 AA. AC O75208; A8K3L2; Q7L5V7; Q7Z5T6; Q8NBL4; Q9NTJ2; Q9P056; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 171. DE RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial; DE Flags: Precursor; GN Name=COQ9; Synonyms=C16orf49; ORFNames=HSPC326, PSEC0129; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., RA Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from human RT chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, Skin, and Uterus; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-318 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [8] RP INVOLVEMENT IN COQ10D5. RX PubMed=19375058; DOI=10.1016/j.ajhg.2009.03.018; RA Duncan A.J., Bitner-Glindzicz M., Meunier B., Costello H., Hargreaves I.P., RA Lopez L.C., Hirano M., Quinzii C.M., Sadowski M.I., Hardy J., Singleton A., RA Clayton P.T., Rahman S.; RT "A nonsense mutation in COQ9 causes autosomal-recessive neonatal-onset RT primary coenzyme Q10 deficiency: a potentially treatable form of RT mitochondrial disease."; RL Am. J. Hum. Genet. 84:558-566(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] {ECO:0007744|PDB:4RHP} RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 84-318 IN COMPLEX WITH RP DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE, FUNCTION, LIPID-BINDING, RP INTERACTION WITH COQ7, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-190; RP MET-227; ASP-237; TRP-240; TYR-241 AND LEU-256. 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. 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:0000269|PubMed:25339443}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000250|UniProtKB:Q8K1Z0}. CC -!- SUBUNIT: Homodimer. Interacts with COQ7. {ECO:0000269|PubMed:25339443}. CC -!- INTERACTION: CC O75208; Q96CM8: ACSF2; NbExp=4; IntAct=EBI-724524, EBI-2876502; CC O75208; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-724524, EBI-10827839; CC O75208; P54886: ALDH18A1; NbExp=3; IntAct=EBI-724524, EBI-1210304; CC O75208; O95393: BMP10; NbExp=3; IntAct=EBI-724524, EBI-3922513; CC O75208; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-724524, EBI-10271156; CC O75208; Q5HYK3: COQ5; NbExp=11; IntAct=EBI-724524, EBI-12577722; CC O75208; Q99807: COQ7; NbExp=8; IntAct=EBI-724524, EBI-11017131; CC O75208; Q8NI60: COQ8A; NbExp=11; IntAct=EBI-724524, EBI-745535; CC O75208; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-724524, EBI-12019274; CC O75208; O14569: CYB561D2; NbExp=3; IntAct=EBI-724524, EBI-717654; CC O75208; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-724524, EBI-2680384; CC O75208; Q08426: EHHADH; NbExp=3; IntAct=EBI-724524, EBI-2339219; CC O75208; Q10471: GALNT2; NbExp=3; IntAct=EBI-724524, EBI-10226985; CC O75208; P09601: HMOX1; NbExp=3; IntAct=EBI-724524, EBI-2806151; CC O75208; P43628: KIR2DL3; NbExp=3; IntAct=EBI-724524, EBI-8632435; CC O75208; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-724524, EBI-12866138; CC O75208; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-724524, EBI-1054848; CC O75208; Q9NRY7: PLSCR2; NbExp=3; IntAct=EBI-724524, EBI-3937430; CC O75208; Q59EV6: PPGB; NbExp=3; IntAct=EBI-724524, EBI-14210385; CC O75208; Q14162: SCARF1; NbExp=3; IntAct=EBI-724524, EBI-12056025; CC O75208; Q13277: STX3; NbExp=3; IntAct=EBI-724524, EBI-1394295; CC O75208; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-724524, EBI-10329860; CC O75208; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-724524, EBI-2339195; CC O75208; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-724524, EBI-8649725; CC O75208; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-724524, EBI-12015604; CC O75208; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-724524, EBI-717441; CC O75208; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-724524, EBI-765817; CC O75208; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-724524, EBI-12045841; CC O75208; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-724524, EBI-12190699; CC O75208; Q14508: WFDC2; NbExp=3; IntAct=EBI-724524, EBI-723529; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75208-1; Sequence=Displayed; CC Name=2; CC IsoId=O75208-2; Sequence=VSP_017683, VSP_017684; CC -!- DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid CC metabolism regulator protein). {ECO:0000269|PubMed:25339443}. CC -!- DISEASE: Coenzyme Q10 deficiency, primary, 5 (COQ10D5) [MIM:614654]: A CC form of coenzyme Q10 deficiency, an autosomal recessive disorder with CC variable manifestations consistent with 5 major phenotypes. The CC phenotypes include an encephalomyopathic form with seizures and ataxia; CC a multisystem infantile form with encephalopathy, cardiomyopathy and CC renal failure; a predominantly cerebellar form with ataxia and CC cerebellar atrophy; Leigh syndrome with growth retardation; and an CC isolated myopathic form. {ECO:0000269|PubMed:19375058}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF29004.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF161444; AAF29004.1; ALT_FRAME; mRNA. DR EMBL; AK075438; BAC11621.1; -; mRNA. DR EMBL; AK290627; BAF83316.1; -; mRNA. DR EMBL; AC004382; AAC24313.1; -; Genomic_DNA. DR EMBL; CH471092; EAW82928.1; -; Genomic_DNA. DR EMBL; BC001478; AAH01478.2; -; mRNA. DR EMBL; BC054340; AAH54340.2; -; mRNA. DR EMBL; BC064946; AAH64946.1; -; mRNA. DR EMBL; AL136884; CAB66818.2; -; mRNA. DR CCDS; CCDS32459.1; -. [O75208-1] DR PIR; T46490; T46490. DR RefSeq; NP_064708.1; NM_020312.3. [O75208-1] DR PDB; 4RHP; X-ray; 2.39 A; A/B=84-318. DR PDB; 6AWL; X-ray; 2.00 A; A/B=1-318. DR PDB; 6DEW; X-ray; 2.00 A; A/B/C/D/E/F=79-287. DR PDB; 7SSP; EM; 3.50 A; A/B/C/D=1-318. DR PDB; 7SSS; EM; 2.40 A; A/B/C/D=1-318. DR PDBsum; 4RHP; -. DR PDBsum; 6AWL; -. DR PDBsum; 6DEW; -. DR PDBsum; 7SSP; -. DR PDBsum; 7SSS; -. DR AlphaFoldDB; O75208; -. DR EMDB; EMD-25412; -. DR EMDB; EMD-25413; -. DR SMR; O75208; -. DR BioGRID; 121326; 216. DR ComplexPortal; CPX-3642; CoQ biosynthetic complex. DR IntAct; O75208; 243. DR STRING; 9606.ENSP00000262507; -. DR GlyGen; O75208; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75208; -. DR PhosphoSitePlus; O75208; -. DR BioMuta; COQ9; -. DR EPD; O75208; -. DR jPOST; O75208; -. DR MassIVE; O75208; -. DR MaxQB; O75208; -. DR PaxDb; 9606-ENSP00000262507; -. DR PeptideAtlas; O75208; -. DR ProteomicsDB; 49869; -. [O75208-1] DR ProteomicsDB; 49870; -. [O75208-2] DR Pumba; O75208; -. DR TopDownProteomics; O75208-1; -. [O75208-1] DR Antibodypedia; 44070; 132 antibodies from 24 providers. DR DNASU; 57017; -. DR Ensembl; ENST00000262507.11; ENSP00000262507.5; ENSG00000088682.14. [O75208-1] DR GeneID; 57017; -. DR KEGG; hsa:57017; -. DR MANE-Select; ENST00000262507.11; ENSP00000262507.5; NM_020312.4; NP_064708.1. DR UCSC; uc002elq.4; human. [O75208-1] DR AGR; HGNC:25302; -. DR CTD; 57017; -. DR DisGeNET; 57017; -. DR GeneCards; COQ9; -. DR GeneReviews; COQ9; -. DR HGNC; HGNC:25302; COQ9. DR HPA; ENSG00000088682; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; COQ9; -. DR MIM; 612837; gene. DR MIM; 614654; phenotype. DR neXtProt; NX_O75208; -. DR OpenTargets; ENSG00000088682; -. DR Orphanet; 319678; Encephalopathy-hypertrophic cardiomyopathy-renal tubular disease syndrome. DR PharmGKB; PA142672085; -. DR VEuPathDB; HostDB:ENSG00000088682; -. DR eggNOG; KOG2969; Eukaryota. DR GeneTree; ENSGT00390000009328; -. DR HOGENOM; CLU_057411_0_2_1; -. DR InParanoid; O75208; -. DR OMA; WTETAMI; -. DR OrthoDB; 10272at2759; -. DR PhylomeDB; O75208; -. DR TreeFam; TF324653; -. DR PathwayCommons; O75208; -. DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis. DR SignaLink; O75208; -. DR UniPathway; UPA00232; -. DR BioGRID-ORCS; 57017; 22 hits in 1165 CRISPR screens. DR ChiTaRS; COQ9; human. DR GeneWiki; COQ9; -. DR GenomeRNAi; 57017; -. DR Pharos; O75208; Tbio. DR PRO; PR:O75208; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O75208; Protein. DR Bgee; ENSG00000088682; Expressed in apex of heart and 131 other cell types or tissues. DR ExpressionAtlas; O75208; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB. DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IPI:ComplexPortal. DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl. DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB. DR Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1. DR InterPro; IPR013718; COQ9_C. DR InterPro; IPR048674; COQ9_HTH. DR InterPro; IPR012762; Ubiq_biosynth_COQ9. DR NCBIfam; TIGR02396; diverge_rpsU; 1. DR PANTHER; PTHR21427; UBIQUINONE BIOSYNTHESIS PROTEIN COQ9, MITOCHONDRIAL; 1. DR PANTHER; PTHR21427:SF19; UBIQUINONE BIOSYNTHESIS PROTEIN COQ9, MITOCHONDRIAL; 1. DR Pfam; PF08511; COQ9; 1. DR Pfam; PF21392; COQ9_N; 1. DR Genevisible; O75208; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Lipid-binding; KW Mitochondrion; Primary mitochondrial disease; Reference proteome; KW Transit peptide; Ubiquinone biosynthesis. FT TRANSIT 1..44 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 45..318 FT /note="Ubiquinone biosynthesis protein COQ9, mitochondrial" FT /id="PRO_0000228637" FT REGION 44..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 45..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 241..244 FT /ligand="1,2-diacylglycero-3-phosphoethanolamine" FT /ligand_id="ChEBI:CHEBI:57613" FT /evidence="ECO:0000269|PubMed:25339443, FT ECO:0007744|PDB:4RHP" FT MOD_RES 175 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8K1Z0" FT VAR_SEQ 127..135 FT /note="SLGLSSAAA -> VCIGEGGAT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16303743" FT /id="VSP_017683" FT VAR_SEQ 136..318 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16303743" FT /id="VSP_017684" FT MUTAGEN 190 FT /note="L->E: Impairs interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT MUTAGEN 227 FT /note="M->E: Impairs interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT MUTAGEN 237 FT /note="D->K: Impairs interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT MUTAGEN 240 FT /note="W->D,K: Abolishes interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT MUTAGEN 241 FT /note="Y->D,K: Abolishes interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT MUTAGEN 256 FT /note="L->K: Impairs interaction with COQ7." FT /evidence="ECO:0000269|PubMed:25339443" FT HELIX 96..108 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 118..127 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 132..137 FT /evidence="ECO:0007829|PDB:6AWL" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 143..169 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 178..191 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 192..199 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 200..207 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 210..212 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 213..231 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 240..259 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 267..282 FT /evidence="ECO:0007829|PDB:6AWL" FT HELIX 287..309 FT /evidence="ECO:0007829|PDB:6AWL" SQ SEQUENCE 318 AA; 35509 MW; F648B4B409E749DA CRC64; MAAAAVSGAL GRAGWRLLQL RCLPVARCRQ ALVPRAFHAS AVGLRSSDEQ KQQPPNSFSQ QHSETQGAEK PDPESSHSPP RYTDQGGEEE EDYESEEQLQ HRILTAALEF VPAHGWTAEA IAEGAQSLGL SSAAASMFGK DGSELILHFV TQCNTRLTRV LEEEQKLVQL GQAEKRKTDQ FLRDAVETRL RMLIPYIEHW PRALSILMLP HNIPSSLSLL TSMVDDMWHY AGDQSTDFNW YTRRAMLAAI YNTTELVMMQ DSSPDFEDTW RFLENRVNDA MNMGHTAKQV KSTGEALVQG LMGAAVTLKN LTGLNQRR //