COQ9_HUMAN
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 03-AUG-2022, entry version 163.
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};
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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 PDBsum; 4RHP; -.
DR PDBsum; 6AWL; -.
DR PDBsum; 6DEW; -.
DR AlphaFoldDB; O75208; -.
DR SMR; O75208; -.
DR BioGRID; 121326; 215.
DR ComplexPortal; CPX-3642; CoQ biosynthetic complex.
DR IntAct; O75208; 242.
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; O75208; -.
DR PeptideAtlas; O75208; -.
DR PRIDE; O75208; -.
DR ProteomicsDB; 49869; -. [O75208-1]
DR ProteomicsDB; 49870; -. [O75208-2]
DR TopDownProteomics; O75208-1; -. [O75208-1]
DR Antibodypedia; 44070; 122 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 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; WFLAGDK; -.
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; 21 hits in 1081 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 129 other tissues.
DR ExpressionAtlas; O75208; baseline and differential.
DR Genevisible; O75208; HS.
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 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 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
