ID COQ2_HUMAN Reviewed; 371 AA. AC Q96H96; O95331; Q1JQ78; Q684R2; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 18-JAN-2017, entry version 124. DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189}; DE Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189}; DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725}; DE AltName: Full=4-hydroxybenzoate decaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189}; DE AltName: Full=COQ2 homolog; DE Short=hCOQ2; DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189}; DE Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189}; DE Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189}; DE Flags: Precursor; GN Name=COQ2 {ECO:0000255|HAMAP-Rule:MF_03189}; Synonyms=CL640; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP AND TISSUE SPECIFICITY. RC TISSUE=Liver, and Muscle; RX PubMed=15153069; DOI=10.1042/BJ20040261; RA Forsgren M., Attersand A., Lake S., Gruenler J., Swiezewska E., RA Dallner G., Climent I.; RT "Isolation and functional expression of human COQ2, a gene encoding a RT polyprenyl transferase involved in the synthesis of CoQ2."; RL Biochem. J. 382:519-526(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, Melanoma, and Pancreatic carcinoma; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-334 (ISOFORM 3). RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.; RT "Full-insert sequence of mapped XREF EST."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-371 (ISOFORM 3). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP CHARACTERIZATION OF VARIANTS COQ10D1 CYS-247, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=17374725; DOI=10.1093/hmg/ddm058; RA Lopez-Martin J.M., Salviati L., Trevisson E., Montini G., DiMauro S., RA Quinzii C., Hirano M., Rodriguez-Hernandez A., Cordero M.D., RA Sanchez-Alcazar J.A., Santos-Ocana C., Navas P.; RT "Missense mutation of the COQ2 gene causes defects of bioenergetics RT and de novo pyrimidine synthesis."; RL Hum. Mol. Genet. 16:1091-1097(2007). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND CHARACTERIZATION OF RP VARIANTS COQ10D1 VAL-78; ASN-96; ARG-132; HIS-147; SER-178; CYS-247 RP AND VAL-252. RX PubMed=27493029; DOI=10.1093/hmg/ddw257; RA Desbats M.A., Morbidoni V., Silic-Benussi M., Doimo M., Ciminale V., RA Cassina M., Sacconi S., Hirano M., Basso G., Pierrel F., Navas P., RA Salviati L., Trevisson E.; RT "The COQ2 genotype predicts the severity of coenzyme Q10 deficiency."; RL Hum. Mol. Genet. 0:0-0(2016). RN [8] RP VARIANT COQ10D1 CYS-247, CHARACTERIZATION OF VARIANT COQ10D1 CYS-247, RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16400613; DOI=10.1086/500092; RA Quinzii C., Naini A., Salviati L., Trevisson E., Navas P., Dimauro S., RA Hirano M.; RT "A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) RT causes primary coenzyme Q10 deficiency."; RL Am. J. Hum. Genet. 78:345-349(2006). RN [9] RP VARIANTS COQ10D1 ASN-96; HIS-147; SER-178 AND CYS-247. RX PubMed=17855635; DOI=10.1681/ASN.2006080833; RA Diomedi-Camassei F., Di Giandomenico S., Santorelli F.M., Caridi G., RA Piemonte F., Montini G., Ghiggeri G.M., Murer L., Barisoni L., RA Pastore A., Muda A.O., Valente M.L., Bertini E., Emma F.; RT "COQ2 nephropathy: a newly described inherited mitochondriopathy with RT primary renal involvement."; RL J. Am. Soc. Nephrol. 18:2773-2780(2007). RN [10] RP VARIANT COQ10D1 VAL-252. RX PubMed=23343605; DOI=10.1016/j.jns.2013.01.004; RA Jakobs B.S., van den Heuvel L.P., Smeets R.J., de Vries M.C., Hien S., RA Schaible T., Smeitink J.A., Wevers R.A., Wortmann S.B., RA Rodenburg R.J.; RT "A novel mutation in COQ2 leading to fatal infantile multisystem RT disease."; RL J. Neurol. Sci. 326:24-28(2013). RN [11] RP VARIANTS MSA1 LEU-29; HIS-49; THR-57; VAL-78; THR-97; SER-107; RP PHE-113; ALA-267; CYS-297; GLN-337 AND ALA-343, AND VARIANTS VAL-16; RP LEU-22; HIS-69 AND HIS-336. RX PubMed=23758206; DOI=10.1056/NEJMoa1212115; RG Multiple-System Atrophy Research Collaboration; RT "Mutations in COQ2 in familial and sporadic multiple-system atrophy."; RL N. Engl. J. Med. 369:233-244(2013). RN [12] RP VARIANT COQ10D1 ARG-132. RX PubMed=25564041; DOI=10.1038/ejhg.2014.277; RA Desbats M.A., Vetro A., Limongelli I., Lunardi G., Casarin A., RA Doimo M., Spinazzi M., Angelini C., Cenacchi G., Burlina A., RA Rodriguez Hernandez M.A., Chiandetti L., Clementi M., Trevisson E., RA Navas P., Zuffardi O., Salviati L.; RT "Primary coenzyme Q10 deficiency presenting as fatal neonatal RT multiorgan failure."; RL Eur. J. Hum. Genet. 23:1254-1258(2015). CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) CC with an all-trans polyprenyl group. Mediates the second step in CC the final reaction sequence of coenzyme Q (CoQ) biosynthesis, CC which is the condensation of the polyisoprenoid side chain with CC PHB, generating the first membrane-bound Q intermediate. CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069, CC ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725, CC ECO:0000269|PubMed:27493029}. CC -!- CATALYTIC ACTIVITY: A polyprenyl diphosphate + 4-hydroxybenzoate = CC diphosphate + a 4-hydroxy-3-polyprenylbenzoate. CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069, CC ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03189}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_03189}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:27493029}; CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; CC Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96H96-1; Sequence=Displayed; CC Name=3; CC IsoId=Q96H96-3; Sequence=VSP_017677, VSP_017678; CC -!- TISSUE SPECIFICITY: Widely expressed. Present in all of the CC tissues tested. Expressed at higher level in skeletal muscle, CC adrenal glands and the heart. {ECO:0000269|PubMed:15153069}. CC -!- DISEASE: Coenzyme Q10 deficiency, primary, 1 (COQ10D1) CC [MIM:607426]: An autosomal recessive disorder with variable CC manifestations consistent with 5 major phenotypes. The phenotypes CC include an encephalomyopathic form with seizures and ataxia; a CC 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:16400613, CC ECO:0000269|PubMed:17374725, ECO:0000269|PubMed:17855635, CC ECO:0000269|PubMed:23343605, ECO:0000269|PubMed:25564041, CC ECO:0000269|PubMed:27493029}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Multiple system atrophy 1 (MSA1) [MIM:146500]: A CC progressive neurodegenerative disorder clinically characterized by CC parkinsonism, cerebellar ataxia, and autonomic, urogenital, and CC pyramidal dysfunction in various combinations. Pathologically, it CC is characterized by degeneration of striatonigral and CC olivopontocerebellar structures, and glial cytoplasmic inclusions CC that consist of abnormally phosphorylated alpha-synuclein or tau. CC {ECO:0000269|PubMed:23758206}. Note=Disease susceptibility is CC associated with variations affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_03189}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72955.1; Type=Frameshift; Positions=172; Evidence={ECO:0000305}; CC Sequence=AAH20728.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=CAF18241.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ621061; CAF18241.1; ALT_INIT; mRNA. DR EMBL; AC114781; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008804; AAH08804.1; -; mRNA. DR EMBL; BC020728; AAH20728.2; ALT_INIT; mRNA. DR EMBL; BC116454; AAI16455.1; -; mRNA. DR EMBL; AF091086; AAC72955.1; ALT_FRAME; mRNA. DR EMBL; CR456860; CAG33141.1; -; mRNA. DR RefSeq; NP_056512.5; NM_015697.7. DR UniGene; Hs.144304; -. DR UniGene; Hs.729069; -. DR ProteinModelPortal; Q96H96; -. DR BioGrid; 118083; 16. DR STRING; 9606.ENSP00000310873; -. DR iPTMnet; Q96H96; -. DR PhosphoSitePlus; Q96H96; -. DR DMDM; 74731901; -. DR MaxQB; Q96H96; -. DR PaxDb; Q96H96; -. DR PeptideAtlas; Q96H96; -. DR PRIDE; Q96H96; -. DR DNASU; 27235; -. DR Ensembl; ENST00000311469; ENSP00000310873; ENSG00000173085. DR Ensembl; ENST00000439031; ENSP00000409275; ENSG00000173085. DR GeneID; 27235; -. DR KEGG; hsa:27235; -. DR UCSC; uc003hog.3; human. [Q96H96-1] DR CTD; 27235; -. DR DisGeNET; 27235; -. DR GeneCards; COQ2; -. DR H-InvDB; HIX0004341; -. DR HGNC; HGNC:25223; COQ2. DR HPA; HPA056599; -. DR HPA; HPA068727; -. DR MalaCards; COQ2; -. DR MIM; 146500; phenotype. DR MIM; 607426; phenotype. DR MIM; 609825; gene. DR neXtProt; NX_Q96H96; -. DR Orphanet; 255249; Leigh syndrome with nephrotic syndrome. DR Orphanet; 227510; Multiple system atrophy, cerebellar type. DR Orphanet; 98933; Multiple system atrophy, parkinsonian type. DR PharmGKB; PA142672084; -. DR eggNOG; KOG1381; Eukaryota. DR eggNOG; COG0382; LUCA. DR HOGENOM; HOG000003697; -. DR HOVERGEN; HBG081302; -. DR InParanoid; Q96H96; -. DR KO; K06125; -. DR OrthoDB; EOG091G0K82; -. DR PhylomeDB; Q96H96; -. DR TreeFam; TF105873; -. DR BioCyc; MetaCyc:ENSG00000173085-MONOMER; -. DR BioCyc; ZFISH:ENSG00000173085-MONOMER; -. DR BRENDA; 2.5.1.39; 2681. DR Reactome; R-HSA-1268020; Mitochondrial protein import. DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis. DR UniPathway; UPA00232; -. DR GeneWiki; COQ2; -. DR GenomeRNAi; 27235; -. DR PRO; PR:Q96H96; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000173085; -. DR CleanEx; HS_COQ2; -. DR ExpressionAtlas; Q96H96; baseline and differential. DR Genevisible; Q96H96; HS. DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IMP:UniProtKB. DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006071; P:glycerol metabolic process; IGI:UniProtKB. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:UniProtKB. DR HAMAP; MF_01635; UbiA; 1. DR InterPro; IPR031103; HB_octoprenylTrfase. DR InterPro; IPR006370; HB_polyprenyltransferase. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR030470; UbiA_prenylTrfase_CS. DR Pfam; PF01040; UbiA; 1. DR TIGRFAMs; TIGR01474; ubiA_proteo; 1. DR PROSITE; PS00943; UBIA; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Disease mutation; KW Isoprene biosynthesis; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Neurodegeneration; Parkinsonism; KW Polymorphism; Reference proteome; Transferase; Transit peptide; KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis. FT TRANSIT 1 34 Mitochondrion. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT CHAIN 35 371 4-hydroxybenzoate polyprenyltransferase, FT mitochondrial. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT /FTId=PRO_0000228623. FT TOPO_DOM 35 83 Mitochondrial matrix. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 84 104 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 105 108 Mitochondrial intermembrane. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 109 129 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 130 148 Mitochondrial matrix. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 170 172 Mitochondrial intermembrane. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 173 193 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 194 203 Mitochondrial matrix. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 204 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 225 231 Mitochondrial intermembrane. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 232 252 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 253 277 Mitochondrial matrix. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 278 298 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 299 300 Mitochondrial intermembrane. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 301 321 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 322 332 Mitochondrial matrix. FT {ECO:0000305|PubMed:27493029}. FT TRANSMEM 333 353 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03189}. FT TOPO_DOM 354 371 Mitochondrial intermembrane. FT {ECO:0000269|PubMed:27493029}. FT REGION 122 144 Allylic polyprenyl diphosphate-binding FT site. {ECO:0000255|HAMAP-Rule:MF_03189}. FT VAR_SEQ 318 334 IYTLDIHRPEDCWNKFI -> KWGLEILPRLV (in FT isoform 3). {ECO:0000303|Ref.4, FT ECO:0000303|Ref.5}. FT /FTId=VSP_017677. FT VAR_SEQ 335 371 Missing (in isoform 3). FT {ECO:0000303|Ref.4, ECO:0000303|Ref.5}. FT /FTId=VSP_017678. FT VARIANT 16 16 L -> V (in dbSNP:rs6818847). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070237. FT VARIANT 22 22 P -> L. {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070238. FT VARIANT 29 29 F -> L (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070239. FT VARIANT 49 49 P -> H (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070240. FT VARIANT 57 57 S -> T (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070241. FT VARIANT 69 69 R -> H. {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070242. FT VARIANT 78 78 M -> V (in MSA1; associated with disease FT susceptibility; decreased ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:23758206, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_070243. FT VARIANT 96 96 S -> N (in COQ10D1; decreased ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:17855635, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_068161. FT VARIANT 97 97 I -> T (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070244. FT VARIANT 107 107 P -> S (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070245. FT VARIANT 113 113 S -> F (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070246. FT VARIANT 132 132 M -> R (in COQ10D1; decreased ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:25564041, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_076913. FT VARIANT 147 147 R -> H (in COQ10D1; loss of ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:17855635, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_068162. FT VARIANT 178 178 N -> S (in COQ10D1; decreased ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:17855635, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_068163. FT VARIANT 247 247 Y -> C (in COQ10D1; decreased 4- FT hydroxybenzoate decaprenyltransferase FT activity). {ECO:0000269|PubMed:16400613, FT ECO:0000269|PubMed:17374725, FT ECO:0000269|PubMed:17855635, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_025701. FT VARIANT 252 252 A -> V (in COQ10D1; loss of ubiquinone FT biosynthesis). FT {ECO:0000269|PubMed:23343605, FT ECO:0000269|PubMed:27493029}. FT /FTId=VAR_076914. FT VARIANT 267 267 T -> A (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070247. FT VARIANT 297 297 S -> C (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070248. FT VARIANT 336 336 N -> H. {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070249. FT VARIANT 337 337 R -> Q (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070250. FT VARIANT 343 343 V -> A (in MSA1; associated with disease FT susceptibility). FT {ECO:0000269|PubMed:23758206}. FT /FTId=VAR_070251. SQ SEQUENCE 371 AA; 40489 MW; 92371F0DD373A732 CRC64; MLGSRAAGFA RGLRALALAW LPGWRGRSFA LARAAGAPHG GDLQPPACPE PRGRQLSLSA AAVVDSAPRP LQPYLRLMRL DKPIGTWLLY LPCTWSIGLA AEPGCFPDWY MLSLFGTGAI LMRGAGCTIN DMWDQDYDKK VTRTANRPIA AGDISTFQSF VFLGGQLTLA LGVLLCLNYY SIALGAGSLL LVITYPLMKR ISYWPQLALG LTFNWGALLG WSAIKGSCDP SVCLPLYFSG VMWTLIYDTI YAHQDKRDDV LIGLKSTALR FGENTKPWLS GFSVAMLGAL SLVGVNSGQT APYYAALGAV GAHLTHQIYT LDIHRPEDCW NKFISNRTLG LIVFLGIVLG NLWKEKKTDK TKKGIENKIE N //