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4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate decaprenyltransferase) (COQ2 homolog) (hCOQ2) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase)

 COQ2_HUMAN              Reviewed;         371 AA.
Q96H96; O95331; Q1JQ78; Q684R2;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 130.
RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189};
Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725};
AltName: Full=4-hydroxybenzoate decaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
AltName: Full=COQ2 homolog;
Short=hCOQ2;
AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
Flags: Precursor;
Name=COQ2 {ECO:0000255|HAMAP-Rule:MF_03189}; Synonyms=CL640;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND TISSUE SPECIFICITY.
TISSUE=Liver, and Muscle;
PubMed=15153069; DOI=10.1042/BJ20040261;
Forsgren M., Attersand A., Lake S., Gruenler J., Swiezewska E.,
Dallner G., Climent I.;
"Isolation and functional expression of human COQ2, a gene encoding a
polyprenyl transferase involved in the synthesis of CoQ2.";
Biochem. J. 382:519-526(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Melanoma, and Pancreatic carcinoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-334 (ISOFORM 3).
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
"Full-insert sequence of mapped XREF EST.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-371 (ISOFORM 3).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
CHARACTERIZATION OF VARIANTS COQ10D1 CYS-247, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=17374725; DOI=10.1093/hmg/ddm058;
Lopez-Martin J.M., Salviati L., Trevisson E., Montini G., DiMauro S.,
Quinzii C., Hirano M., Rodriguez-Hernandez A., Cordero M.D.,
Sanchez-Alcazar J.A., Santos-Ocana C., Navas P.;
"Missense mutation of the COQ2 gene causes defects of bioenergetics
and de novo pyrimidine synthesis.";
Hum. Mol. Genet. 16:1091-1097(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND CHARACTERIZATION OF
VARIANTS COQ10D1 VAL-78; ASN-96; ARG-132; HIS-147; SER-178; CYS-247
AND VAL-252.
PubMed=27493029; DOI=10.1093/hmg/ddw257;
Desbats M.A., Morbidoni V., Silic-Benussi M., Doimo M., Ciminale V.,
Cassina M., Sacconi S., Hirano M., Basso G., Pierrel F., Navas P.,
Salviati L., Trevisson E.;
"The COQ2 genotype predicts the severity of coenzyme Q10 deficiency.";
Hum. Mol. Genet. 25:4256-4265(2016).
[8]
VARIANT COQ10D1 CYS-247, CHARACTERIZATION OF VARIANT COQ10D1 CYS-247,
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16400613; DOI=10.1086/500092;
Quinzii C., Naini A., Salviati L., Trevisson E., Navas P., Dimauro S.,
Hirano M.;
"A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2)
causes primary coenzyme Q10 deficiency.";
Am. J. Hum. Genet. 78:345-349(2006).
[9]
VARIANTS COQ10D1 ASN-96; HIS-147; SER-178 AND CYS-247.
PubMed=17855635; DOI=10.1681/ASN.2006080833;
Diomedi-Camassei F., Di Giandomenico S., Santorelli F.M., Caridi G.,
Piemonte F., Montini G., Ghiggeri G.M., Murer L., Barisoni L.,
Pastore A., Muda A.O., Valente M.L., Bertini E., Emma F.;
"COQ2 nephropathy: a newly described inherited mitochondriopathy with
primary renal involvement.";
J. Am. Soc. Nephrol. 18:2773-2780(2007).
[10]
VARIANT COQ10D1 VAL-252.
PubMed=23343605; DOI=10.1016/j.jns.2013.01.004;
Jakobs B.S., van den Heuvel L.P., Smeets R.J., de Vries M.C., Hien S.,
Schaible T., Smeitink J.A., Wevers R.A., Wortmann S.B.,
Rodenburg R.J.;
"A novel mutation in COQ2 leading to fatal infantile multisystem
disease.";
J. Neurol. Sci. 326:24-28(2013).
[11]
VARIANTS MSA1 LEU-29; HIS-49; THR-57; VAL-78; THR-97; SER-107;
PHE-113; ALA-267; CYS-297; GLN-337 AND ALA-343, AND VARIANTS VAL-16;
LEU-22; HIS-69 AND HIS-336.
PubMed=23758206; DOI=10.1056/NEJMoa1212115;
Multiple-System Atrophy Research Collaboration;
"Mutations in COQ2 in familial and sporadic multiple-system atrophy.";
N. Engl. J. Med. 369:233-244(2013).
[12]
VARIANT COQ10D1 ARG-132.
PubMed=25564041; DOI=10.1038/ejhg.2014.277;
Desbats M.A., Vetro A., Limongelli I., Lunardi G., Casarin A.,
Doimo M., Spinazzi M., Angelini C., Cenacchi G., Burlina A.,
Rodriguez Hernandez M.A., Chiandetti L., Clementi M., Trevisson E.,
Navas P., Zuffardi O., Salviati L.;
"Primary coenzyme Q10 deficiency presenting as fatal neonatal
multiorgan failure.";
Eur. J. Hum. Genet. 23:1254-1258(2015).
[13]
VARIANT COQ10D1 ALA-340.
PubMed=28044327; DOI=10.1111/cge.12960;
Gigante M., Diella S., Santangelo L., Trevisson E., Acosta M.J.,
Amatruda M., Finzi G., Caridi G., Murer L., Accetturo M., Ranieri E.,
Ghiggeri G.M., Giordano M., Grandaliano G., Salviati L., Gesualdo L.;
"Further phenotypic heterogeneity of CoQ10 deficiency associated with
steroid resistant nephrotic syndrome and novel COQ2 and COQ6
variants.";
Clin. Genet. 92:224-226(2017).
-!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB)
with an all-trans polyprenyl group. Mediates the second step in
the final reaction sequence of coenzyme Q (CoQ) biosynthesis,
which is the condensation of the polyisoprenoid side chain with
PHB, generating the first membrane-bound Q intermediate.
{ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069,
ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725,
ECO:0000269|PubMed:27493029}.
-!- CATALYTIC ACTIVITY: A polyprenyl diphosphate + 4-hydroxybenzoate =
diphosphate + a 4-hydroxy-3-polyprenylbenzoate.
{ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:15153069,
ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03189};
-!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03189}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:27493029};
Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189};
Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96H96-1; Sequence=Displayed;
Name=3;
IsoId=Q96H96-3; Sequence=VSP_017677, VSP_017678;
-!- TISSUE SPECIFICITY: Widely expressed. Present in all of the
tissues tested. Expressed at higher level in skeletal muscle,
adrenal glands and the heart. {ECO:0000269|PubMed:15153069}.
-!- DISEASE: Coenzyme Q10 deficiency, primary, 1 (COQ10D1)
[MIM:607426]: An autosomal recessive disorder with variable
manifestations consistent with 5 major phenotypes. The phenotypes
include an encephalomyopathic form with seizures and ataxia; a
multisystem infantile form with encephalopathy, cardiomyopathy and
renal failure; a predominantly cerebellar form with ataxia and
cerebellar atrophy; Leigh syndrome with growth retardation; and an
isolated myopathic form. {ECO:0000269|PubMed:16400613,
ECO:0000269|PubMed:17374725, ECO:0000269|PubMed:17855635,
ECO:0000269|PubMed:23343605, ECO:0000269|PubMed:25564041,
ECO:0000269|PubMed:27493029, ECO:0000269|PubMed:28044327}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Multiple system atrophy 1 (MSA1) [MIM:146500]: A
progressive neurodegenerative disorder clinically characterized by
parkinsonism, cerebellar ataxia, and autonomic, urogenital, and
pyramidal dysfunction in various combinations. Pathologically, it
is characterized by degeneration of striatonigral and
olivopontocerebellar structures, and glial cytoplasmic inclusions
that consist of abnormally phosphorylated alpha-synuclein or tau.
{ECO:0000269|PubMed:23758206}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
{ECO:0000255|HAMAP-Rule:MF_03189}.
-!- SEQUENCE CAUTION:
Sequence=AAC72955.1; Type=Frameshift; Positions=172; Evidence={ECO:0000305};
Sequence=AAH20728.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAF18241.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ621061; CAF18241.1; ALT_INIT; mRNA.
EMBL; AC114781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008804; AAH08804.1; -; mRNA.
EMBL; BC020728; AAH20728.2; ALT_INIT; mRNA.
EMBL; BC116454; AAI16455.1; -; mRNA.
EMBL; AF091086; AAC72955.1; ALT_FRAME; mRNA.
EMBL; CR456860; CAG33141.1; -; mRNA.
RefSeq; NP_056512.5; NM_015697.7.
UniGene; Hs.144304; -.
UniGene; Hs.729069; -.
ProteinModelPortal; Q96H96; -.
BioGrid; 118083; 16.
STRING; 9606.ENSP00000310873; -.
iPTMnet; Q96H96; -.
PhosphoSitePlus; Q96H96; -.
DMDM; 74731901; -.
MaxQB; Q96H96; -.
PaxDb; Q96H96; -.
PeptideAtlas; Q96H96; -.
PRIDE; Q96H96; -.
DNASU; 27235; -.
Ensembl; ENST00000311469; ENSP00000310873; ENSG00000173085.
Ensembl; ENST00000439031; ENSP00000409275; ENSG00000173085.
GeneID; 27235; -.
KEGG; hsa:27235; -.
UCSC; uc003hog.3; human. [Q96H96-1]
CTD; 27235; -.
DisGeNET; 27235; -.
EuPathDB; HostDB:ENSG00000173085.13; -.
GeneCards; COQ2; -.
H-InvDB; HIX0004341; -.
HGNC; HGNC:25223; COQ2.
HPA; HPA056599; -.
HPA; HPA068727; -.
MalaCards; COQ2; -.
MIM; 146500; phenotype.
MIM; 607426; phenotype.
MIM; 609825; gene.
neXtProt; NX_Q96H96; -.
Orphanet; 255249; Leigh syndrome with nephrotic syndrome.
Orphanet; 227510; Multiple system atrophy, cerebellar type.
Orphanet; 98933; Multiple system atrophy, parkinsonian type.
PharmGKB; PA142672084; -.
eggNOG; KOG1381; Eukaryota.
eggNOG; COG0382; LUCA.
HOGENOM; HOG000003697; -.
HOVERGEN; HBG081302; -.
InParanoid; Q96H96; -.
KO; K06125; -.
OrthoDB; EOG091G0K82; -.
PhylomeDB; Q96H96; -.
TreeFam; TF105873; -.
BioCyc; MetaCyc:ENSG00000173085-MONOMER; -.
BRENDA; 2.5.1.39; 2681.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-2142789; Ubiquinol biosynthesis.
UniPathway; UPA00232; -.
GeneWiki; COQ2; -.
GenomeRNAi; 27235; -.
PRO; PR:Q96H96; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000173085; -.
CleanEx; HS_COQ2; -.
ExpressionAtlas; Q96H96; baseline and differential.
Genevisible; Q96H96; HS.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IMP:UniProtKB.
GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006071; P:glycerol metabolic process; IGI:UniProtKB.
GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:UniProtKB.
HAMAP; MF_01635; UbiA; 1.
InterPro; IPR031103; HB_octoprenylTrfase.
InterPro; IPR006370; HB_polyprenyltransferase.
InterPro; IPR000537; UbiA_prenyltransferase.
InterPro; IPR030470; UbiA_prenylTrfase_CS.
Pfam; PF01040; UbiA; 1.
TIGRFAMs; TIGR01474; ubiA_proteo; 1.
PROSITE; PS00943; UBIA; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Isoprene biosynthesis; Membrane; Mitochondrion;
Mitochondrion inner membrane; Neurodegeneration; Parkinsonism;
Polymorphism; Primary mitochondrial disease; Reference proteome;
Transferase; Transit peptide; Transmembrane; Transmembrane helix;
Ubiquinone biosynthesis.
TRANSIT 1 34 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03189}.
CHAIN 35 371 4-hydroxybenzoate polyprenyltransferase,
mitochondrial. {ECO:0000255|HAMAP-
Rule:MF_03189}.
/FTId=PRO_0000228623.
TOPO_DOM 35 83 Mitochondrial matrix.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 84 104 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 105 108 Mitochondrial intermembrane.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 109 129 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 130 148 Mitochondrial matrix.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 170 172 Mitochondrial intermembrane.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 173 193 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 194 203 Mitochondrial matrix.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 204 224 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 225 231 Mitochondrial intermembrane.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 232 252 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 253 277 Mitochondrial matrix.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 278 298 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 299 300 Mitochondrial intermembrane.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 301 321 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 322 332 Mitochondrial matrix.
{ECO:0000305|PubMed:27493029}.
TRANSMEM 333 353 Helical. {ECO:0000255|HAMAP-
Rule:MF_03189}.
TOPO_DOM 354 371 Mitochondrial intermembrane.
{ECO:0000269|PubMed:27493029}.
REGION 122 144 Allylic polyprenyl diphosphate-binding
site. {ECO:0000255|HAMAP-Rule:MF_03189}.
VAR_SEQ 318 334 IYTLDIHRPEDCWNKFI -> KWGLEILPRLV (in
isoform 3). {ECO:0000303|Ref.4,
ECO:0000303|Ref.5}.
/FTId=VSP_017677.
VAR_SEQ 335 371 Missing (in isoform 3).
{ECO:0000303|Ref.4, ECO:0000303|Ref.5}.
/FTId=VSP_017678.
VARIANT 16 16 L -> V (in dbSNP:rs6818847).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070237.
VARIANT 22 22 P -> L. {ECO:0000269|PubMed:23758206}.
/FTId=VAR_070238.
VARIANT 29 29 F -> L (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070239.
VARIANT 49 49 P -> H (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070240.
VARIANT 57 57 S -> T (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070241.
VARIANT 69 69 R -> H. {ECO:0000269|PubMed:23758206}.
/FTId=VAR_070242.
VARIANT 78 78 M -> V (in MSA1; associated with disease
susceptibility; decreased ubiquinone
biosynthesis).
{ECO:0000269|PubMed:23758206,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_070243.
VARIANT 96 96 S -> N (in COQ10D1; decreased ubiquinone
biosynthesis).
{ECO:0000269|PubMed:17855635,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_068161.
VARIANT 97 97 I -> T (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070244.
VARIANT 107 107 P -> S (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070245.
VARIANT 113 113 S -> F (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070246.
VARIANT 132 132 M -> R (in COQ10D1; decreased ubiquinone
biosynthesis).
{ECO:0000269|PubMed:25564041,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_076913.
VARIANT 147 147 R -> H (in COQ10D1; loss of ubiquinone
biosynthesis).
{ECO:0000269|PubMed:17855635,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_068162.
VARIANT 178 178 N -> S (in COQ10D1; decreased ubiquinone
biosynthesis).
{ECO:0000269|PubMed:17855635,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_068163.
VARIANT 247 247 Y -> C (in COQ10D1; decreased 4-
hydroxybenzoate decaprenyltransferase
activity). {ECO:0000269|PubMed:16400613,
ECO:0000269|PubMed:17374725,
ECO:0000269|PubMed:17855635,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_025701.
VARIANT 252 252 A -> V (in COQ10D1; loss of ubiquinone
biosynthesis).
{ECO:0000269|PubMed:23343605,
ECO:0000269|PubMed:27493029}.
/FTId=VAR_076914.
VARIANT 267 267 T -> A (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070247.
VARIANT 297 297 S -> C (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070248.
VARIANT 336 336 N -> H. {ECO:0000269|PubMed:23758206}.
/FTId=VAR_070249.
VARIANT 337 337 R -> Q (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070250.
VARIANT 340 340 G -> A (in COQ10D1; unknown pathological
significance).
{ECO:0000269|PubMed:28044327}.
/FTId=VAR_078121.
VARIANT 343 343 V -> A (in MSA1; associated with disease
susceptibility).
{ECO:0000269|PubMed:23758206}.
/FTId=VAR_070251.
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


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