COQ2_HUMAN
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 03-AUG-2022, entry version 158.
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:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725};
DE AltName: Full=4-hydroxybenzoate decaprenyltransferase {ECO:0000303|PubMed:15153069};
DE AltName: Full=COQ2 homolog;
DE Short=hCOQ2 {ECO:0000303|PubMed:15153069};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000303|PubMed:16400613};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND PATHWAY.
RC TISSUE=Liver, and Muscle;
RX PubMed=15153069; DOI=10.1042/bj20040261;
RA Forsgren M., Attersand A., Lake S., Gruenler J., Swiezewska E., Dallner G.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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 project:
RT 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, CATALYTIC ACTIVITY,
RP AND PATHWAY.
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 and de
RT novo pyrimidine synthesis.";
RL Hum. Mol. Genet. 16:1091-1097(2007).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20526342; DOI=10.1038/nchembio.372;
RA Forsman U., Sjoeberg M., Turunen M., Sindelar P.J.;
RT "4-Nitrobenzoate inhibits coenzyme Q biosynthesis in mammalian cell
RT cultures.";
RL Nat. Chem. Biol. 6:515-517(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, CHARACTERIZATION OF VARIANTS
RP COQ10D1 VAL-78; ASN-96; ARG-132; HIS-147; SER-178; CYS-247 AND VAL-252, AND
RP CATALYTIC ACTIVITY.
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. 25:4256-4265(2016).
RN [9]
RP VARIANT COQ10D1 CYS-247, CHARACTERIZATION OF VARIANT COQ10D1 CYS-247,
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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) causes
RT primary coenzyme Q10 deficiency.";
RL Am. J. Hum. Genet. 78:345-349(2006).
RN [10]
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., Pastore A.,
RA 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 [11]
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., Rodenburg R.J.;
RT "A novel mutation in COQ2 leading to fatal infantile multisystem disease.";
RL J. Neurol. Sci. 326:24-28(2013).
RN [12]
RP VARIANTS MSA1 LEU-29; HIS-49; THR-57; VAL-78; THR-97; SER-107; PHE-113;
RP ALA-267; CYS-297; GLN-337 AND ALA-343, AND VARIANTS VAL-16; LEU-22; HIS-69
RP 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 [13]
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., Doimo M.,
RA 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 multiorgan
RT failure.";
RL Eur. J. Hum. Genet. 23:1254-1258(2015).
RN [14]
RP VARIANT COQ10D1 ALA-340.
RX PubMed=28044327; DOI=10.1111/cge.12960;
RA Gigante M., Diella S., Santangelo L., Trevisson E., Acosta M.J.,
RA Amatruda M., Finzi G., Caridi G., Murer L., Accetturo M., Ranieri E.,
RA Ghiggeri G.M., Giordano M., Grandaliano G., Salviati L., Gesualdo L.;
RT "Further phenotypic heterogeneity of CoQ10 deficiency associated with
RT steroid resistant nephrotic syndrome and novel COQ2 and COQ6 variants.";
RL Clin. Genet. 92:224-226(2017).
CC -!- FUNCTION: Mediates the second step in the final reaction sequence of
CC coenzyme Q (CoQ) biosynthesis (PubMed:15153069, PubMed:17374725,
CC PubMed:16400613, PubMed:20526342). Catalyzes the prenylation of para-
CC hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-
CC trans-decaprenyl diphosphate) (PubMed:15153069, PubMed:17374725,
CC PubMed:16400613, PubMed:20526342). The length of the polyprenyl side
CC chain varies depending on the species, in humans, the side chain is
CC comprised of 10 isoprenyls (decaprenyl) producing CoQ10 (also known as
CC ubiquinone), whereas rodents predominantly generate CoQ9
CC (PubMed:15153069, PubMed:16400613). However, this specificity is not
CC complete, human tissues have low amounts of CoQ9 and rodent organs
CC contain some CoQ10 (PubMed:15153069). Plays a central role in the
CC biosynthesis of CoQ10 (PubMed:15153069, PubMed:17374725,
CC PubMed:16400613). CoQ10 is a vital molecule that transports electrons
CC from mitochondrial respiratory chain complexes (PubMed:17374725,
CC PubMed:27493029, PubMed:16400613). CoQs also function as cofactors for
CC uncoupling protein and play a role as regulators of the
CC extracellularly-induced ceramide-dependent apoptotic pathway
CC (PubMed:17374725, PubMed:16400613). Regulates mitochondrial
CC permeability transition pore (mPTP) opening and ROS production (pivotal
CC events in cell death) in a tissue specific manner (By similarity).
CC {ECO:0000250|UniProtKB:Q499N4, ECO:0000269|PubMed:15153069,
CC ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725,
CC ECO:0000269|PubMed:20526342, ECO:0000269|PubMed:27493029,
CC ECO:0000303|PubMed:15153069, ECO:0000303|PubMed:16400613,
CC ECO:0000303|PubMed:17374725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC ChEBI:CHEBI:78396; EC=2.5.1.39;
CC Evidence={ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613,
CC ECO:0000269|PubMed:17374725, ECO:0000305|PubMed:20526342,
CC ECO:0000305|PubMed:27493029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44505;
CC Evidence={ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613,
CC ECO:0000269|PubMed:17374725, ECO:0000305|PubMed:20526342,
CC ECO:0000305|PubMed:27493029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-decaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39;
CC Evidence={ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613,
CC ECO:0000269|PubMed:17374725, ECO:0000305|PubMed:20526342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565;
CC Evidence={ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613,
CC ECO:0000269|PubMed:17374725, ECO:0000305|PubMed:20526342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-nonaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-nonaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:17709, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58391, ChEBI:CHEBI:84502; EC=2.5.1.39;
CC Evidence={ECO:0000269|PubMed:15153069};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17710;
CC Evidence={ECO:0000269|PubMed:15153069};
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:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725,
CC ECO:0000305|PubMed:15153069}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03189, ECO:0000269|PubMed:27493029}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side
CC {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 tissues
CC tested. Expressed at higher level in skeletal muscle, adrenal glands
CC and the heart. {ECO:0000269|PubMed:15153069}.
CC -!- DISEASE: Coenzyme Q10 deficiency, primary, 1 (COQ10D1) [MIM:607426]: An
CC autosomal recessive disorder with variable manifestations consistent
CC with 5 major phenotypes. The phenotypes include an encephalomyopathic
CC form with seizures and ataxia; a multisystem infantile form with
CC encephalopathy, cardiomyopathy and renal failure; a predominantly
CC cerebellar form with ataxia and cerebellar atrophy; Leigh syndrome with
CC growth retardation; and an isolated myopathic form.
CC {ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725,
CC ECO:0000269|PubMed:17855635, ECO:0000269|PubMed:23343605,
CC ECO:0000269|PubMed:25564041, ECO:0000269|PubMed:27493029,
CC ECO:0000269|PubMed:28044327}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Multiple system atrophy 1 (MSA1) [MIM:146500]: A progressive
CC neurodegenerative disorder clinically characterized by parkinsonism,
CC cerebellar ataxia, and autonomic, urogenital, and pyramidal dysfunction
CC in various combinations. Pathologically, it is characterized by
CC degeneration of striatonigral and olivopontocerebellar structures, and
CC glial cytoplasmic inclusions that consist of abnormally phosphorylated
CC alpha-synuclein or tau. {ECO:0000269|PubMed:23758206}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this 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; Evidence={ECO:0000305};
CC Sequence=AAH20728.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAF18241.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS87234.1; -. [Q96H96-1]
DR AlphaFoldDB; Q96H96; -.
DR SMR; Q96H96; -.
DR BioGRID; 118083; 90.
DR IntAct; Q96H96; 89.
DR STRING; 9606.ENSP00000310873; -.
DR iPTMnet; Q96H96; -.
DR PhosphoSitePlus; Q96H96; -.
DR BioMuta; COQ2; -.
DR DMDM; 74731901; -.
DR EPD; Q96H96; -.
DR MassIVE; Q96H96; -.
DR MaxQB; Q96H96; -.
DR PaxDb; Q96H96; -.
DR PeptideAtlas; Q96H96; -.
DR PRIDE; Q96H96; -.
DR ProteomicsDB; 76713; -. [Q96H96-1]
DR ProteomicsDB; 76714; -. [Q96H96-3]
DR Antibodypedia; 25200; 60 antibodies from 18 providers.
DR DNASU; 27235; -.
DR Ensembl; ENST00000311469.9; ENSP00000310873.4; ENSG00000173085.15.
DR UCSC; uc003hog.3; human. [Q96H96-1]
DR GeneCards; COQ2; -.
DR GeneReviews; COQ2; -.
DR HGNC; HGNC:25223; COQ2.
DR HPA; ENSG00000173085; Tissue enhanced (tongue).
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 VEuPathDB; HostDB:ENSG00000173085; -.
DR eggNOG; KOG1381; Eukaryota.
DR InParanoid; Q96H96; -.
DR OrthoDB; 1343847at2759; -.
DR PhylomeDB; Q96H96; -.
DR TreeFam; TF105873; -.
DR BioCyc; MetaCyc:ENSG00000173085-MON; -.
DR BRENDA; 2.5.1.39; 2681.
DR PathwayCommons; Q96H96; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis.
DR SignaLink; Q96H96; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 27235; 298 hits in 1080 CRISPR screens.
DR ChiTaRS; COQ2; human.
DR GeneWiki; COQ2; -.
DR GenomeRNAi; 27235; -.
DR Pharos; Q96H96; Tbio.
DR PRO; PR:Q96H96; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96H96; protein.
DR Bgee; ENSG00000173085; Expressed in skeletal muscle tissue of biceps brachii and 196 other tissues.
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:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; IGI:MGI.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IGI:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:UniProtKB.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
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; Disease variant; Isoprene biosynthesis; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Neurodegeneration;
KW Parkinsonism; Primary mitochondrial disease; Reference proteome;
KW Transferase; Transit peptide; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 35..371
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000228623"
FT TOPO_DOM 35..83
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 105..108
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 130..148
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 170..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 194..203
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 225..231
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 253..277
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 299..300
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 322..332
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:27493029"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 354..371
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27493029"
FT VAR_SEQ 318..334
FT /note="IYTLDIHRPEDCWNKFI -> KWGLEILPRLV (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_017677"
FT VAR_SEQ 335..371
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_017678"
FT VARIANT 16
FT /note="L -> V (in dbSNP:rs6818847)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070237"
FT VARIANT 22
FT /note="P -> L"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070238"
FT VARIANT 29
FT /note="F -> L (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070239"
FT VARIANT 49
FT /note="P -> H (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070240"
FT VARIANT 57
FT /note="S -> T (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070241"
FT VARIANT 69
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070242"
FT VARIANT 78
FT /note="M -> V (in MSA1; associated with disease
FT susceptibility; decreased ubiquinone biosynthesis)"
FT /evidence="ECO:0000269|PubMed:23758206,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_070243"
FT VARIANT 96
FT /note="S -> N (in COQ10D1; decreased ubiquinone
FT biosynthesis)"
FT /evidence="ECO:0000269|PubMed:17855635,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_068161"
FT VARIANT 97
FT /note="I -> T (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070244"
FT VARIANT 107
FT /note="P -> S (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070245"
FT VARIANT 113
FT /note="S -> F (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070246"
FT VARIANT 132
FT /note="M -> R (in COQ10D1; decreased ubiquinone
FT biosynthesis)"
FT /evidence="ECO:0000269|PubMed:25564041,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_076913"
FT VARIANT 147
FT /note="R -> H (in COQ10D1; loss of ubiquinone
FT biosynthesis)"
FT /evidence="ECO:0000269|PubMed:17855635,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_068162"
FT VARIANT 178
FT /note="N -> S (in COQ10D1; decreased ubiquinone
FT biosynthesis)"
FT /evidence="ECO:0000269|PubMed:17855635,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_068163"
FT VARIANT 247
FT /note="Y -> C (in COQ10D1; decreased 4-hydroxybenzoate
FT decaprenyltransferase activity)"
FT /evidence="ECO:0000269|PubMed:16400613,
FT ECO:0000269|PubMed:17374725, ECO:0000269|PubMed:17855635,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_025701"
FT VARIANT 252
FT /note="A -> V (in COQ10D1; loss of ubiquinone
FT biosynthesis)"
FT /evidence="ECO:0000269|PubMed:23343605,
FT ECO:0000269|PubMed:27493029"
FT /id="VAR_076914"
FT VARIANT 267
FT /note="T -> A (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070247"
FT VARIANT 297
FT /note="S -> C (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070248"
FT VARIANT 336
FT /note="N -> H"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070249"
FT VARIANT 337
FT /note="R -> Q (in MSA1; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="VAR_070250"
FT VARIANT 340
FT /note="G -> A (in COQ10D1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28044327"
FT /id="VAR_078121"
FT VARIANT 343
FT /note="V -> A (in MSA1; associated with disease
FT susceptibility; dbSNP:rs397514727)"
FT /evidence="ECO:0000269|PubMed:23758206"
FT /id="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
