LOCUS       NM_001358921            1525 bp    mRNA    linear   PRI 12-OCT-2024
DEFINITION  Homo sapiens coenzyme Q2, polyprenyltransferase (COQ2), transcript
            variant 2, mRNA; nuclear gene for mitochondrial product.
ACCESSION   NM_001358921
VERSION     NM_001358921.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1525)
  AUTHORS   Li,M., Zhang,C.L., Zhou,D.S., Chan,S.H., Liu,X.Q., Chen,S.N.,
            Yang,Z.Y., Ju,F.E., Sang,X.Y., Liu,Z.X., Zhang,Q.X., Pan,Y.M.,
            Deng,S.S., Wang,X.M., Zhong,L., Zhang,X.D. and Du,X.
  TITLE     Identification of COQ2 as a regulator of proliferation and lipid
            peroxidation through genome-scale CRISPR-Cas9 screening in myeloma
            cells
  JOURNAL   Br J Haematol 204 (4), 1307-1324 (2024)
   PUBMED   38462771
  REMARK    GeneRIF: Identification of COQ2 as a regulator of proliferation and
            lipid peroxidation through genome-scale CRISPR-Cas9 screening in
            myeloma cells.
REFERENCE   2  (bases 1 to 1525)
  AUTHORS   Kuo,M.C., Lu,Y.C., Tai,C.H., Soong,B.W., Hu,F.C., Chen,M.L.,
            Lin,C.H. and Wu,R.M.
  TITLE     COQ2 and SNCA polymorphisms interact with environmental factors to
            modulate the risk of multiple system atrophy and subtype
            disposition
  JOURNAL   Eur J Neurol 29 (10), 2956-2966 (2022)
   PUBMED   35748722
  REMARK    GeneRIF: COQ2 and SNCA polymorphisms interact with environmental
            factors to modulate the risk of multiple system atrophy and subtype
            disposition.
REFERENCE   3  (bases 1 to 1525)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (bases 1 to 1525)
  AUTHORS   Li,M., Yue,Z., Lin,H., Wang,H., Chen,H. and Sun,L.
  TITLE     COQ2 mutation associated isolated nephropathy in two siblings from
            a Chinese pedigree
  JOURNAL   Ren Fail 43 (1), 97-101 (2021)
   PUBMED   33397173
  REMARK    GeneRIF: COQ2 mutation associated isolated nephropathy in two
            siblings from a Chinese pedigree.
REFERENCE   5  (bases 1 to 1525)
  AUTHORS   Buron,M.I., Herman,M.D., Alcain,F.J. and Villalba,J.M.
  TITLE     Stimulation of polyprenyl 4-hydroxybenzoate transferase activity by
            sodium cholate and
            3-[(cholamidopropyl)dimethylammonio]-1-propanesulfonate
  JOURNAL   Anal Biochem 353 (1), 15-21 (2006)
   PUBMED   16643834
  REMARK    GeneRIF: We have found that both
            3-[(cholamidopropyl)dimethylammonio]-1-propanesulfonate and sodium
            cholate, but not sodium deoxycholate, lysophosphatidyl choline, or
            octylglucoside, significantly stimulate ubiquinone activity over
            that measured with Triton X-100.
REFERENCE   6  (bases 1 to 1525)
  AUTHORS   Quinzii,C., Naini,A., Salviati,L., Trevisson,E., Navas,P.,
            Dimauro,S. and Hirano,M.
  TITLE     A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2)
            causes primary coenzyme Q10 deficiency
  JOURNAL   Am J Hum Genet 78 (2), 345-349 (2006)
   PUBMED   16400613
  REMARK    GeneRIF: Substitution of a highly conserved tyrosine to cysteine at
            amino acid 297 of COQ2 is the first molecular cause of primary
            CoQ(10) deficiency.
REFERENCE   7  (bases 1 to 1525)
  AUTHORS   Esaka,Y., Nagahara,Y., Hasome,Y., Nishio,R. and Ikekita,M.
  TITLE     Coenzyme Q2 induced p53-dependent apoptosis
  JOURNAL   Biochim Biophys Acta 1724 (1-2), 49-58 (2005)
   PUBMED   15905035
  REMARK    GeneRIF: Treatment with CoQs having shorter isoprenoid chains,
            especially CoQ2, induced apoptosis in p53-point mutated BALL-1
            cells, whereas treatment with longer isoprenoid chains did not.
REFERENCE   8  (bases 1 to 1525)
  AUTHORS   Forsgren,M., Attersand,A., Lake,S., Grunler,J., Swiezewska,E.,
            Dallner,G. and Climent,I.
  TITLE     Isolation and functional expression of human COQ2, a gene encoding
            a polyprenyl transferase involved in the synthesis of CoQ
  JOURNAL   Biochem J 382 (Pt 2), 519-526 (2004)
   PUBMED   15153069
REFERENCE   9  (bases 1 to 1525)
  AUTHORS   Salviati,L., Trevisson,E., Agosto,C., Doimo,M. and Navas,P.
  TITLE     Primary Coenzyme Q10 Deficiency Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28125198
REFERENCE   10 (bases 1 to 1525)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114781.2, KU877220.1 and
            AA825250.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 30, 2019 this sequence version replaced NM_001358921.1.
            
            Summary: This gene encodes an enzyme that functions in the final
            steps in the biosynthesis of CoQ (ubiquinone), a redox carrier in
            the mitochondrial respiratory chain and a lipid-soluble
            antioxidant. This enzyme, which is part of the coenzyme Q10
            pathway, catalyzes the prenylation of parahydroxybenzoate with an
            all-trans polyprenyl group. Mutations in this gene cause coenzyme
            Q10 deficiency, a mitochondrial encephalomyopathy, and also COQ2
            nephropathy, an inherited form of mitochondriopathy with primary
            renal involvement. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            a downstrean in-frame start codon, compared to variant 1. It
            encodes isoform 2, which has a shorter N-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KU877220.1, BC008804.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000647002.2/
                                                  ENSP00000495761.2
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-3                 AC114781.2         49197-49199         c
            4-1514              KU877220.1         1-1511
            1515-1525           AA825250.1         16-26               c
FEATURES             Location/Qualifiers
     source          1..1525
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.23"
     gene            1..1525
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /note="coenzyme Q2, polyprenyltransferase"
                     /db_xref="GeneID:27235"
                     /db_xref="HGNC:HGNC:25223"
                     /db_xref="MIM:609825"
     exon            1..287
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     CDS             35..1150
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /EC_number="2.5.1.39"
                     /note="isoform 2 is encoded by transcript variant 2;
                     para-hydroxybenzoate-polyprenyltransferase, mitochondrial;
                     PHB:polyprenyltransferase; 4-hydroxybenzoate
                     polyprenyltransferase, mitochondrial; coenzyme Q2 homolog,
                     prenyltransferase; 4-HB polyprenyltransferase;
                     4-hydroxybenzoate decaprenyltransferase; coenzyme Q2
                     4-hydroxybenzoate polyprenyltransferase"
                     /codon_start=1
                     /product="4-hydroxybenzoate polyprenyltransferase,
                     mitochondrial isoform 2"
                     /protein_id="NP_001345850.1"
                     /db_xref="CCDS:CCDS87234.1"
                     /db_xref="GeneID:27235"
                     /db_xref="HGNC:HGNC:25223"
                     /db_xref="MIM:609825"
                     /translation="MLGSRAAGFARGLRAVALAWLPGWRGRSFALARAAGAPHGGDLQ
                     PPACPEPRGRQLSLSAAAVVDSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAAE
                     PGCFPDWYMLSLFGTGAILMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSF
                     VFLGGQLTLALGVLLCLNYYSIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGAL
                     LGWSAIKGSCDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTK
                     PWLSGFSVAMLGALSLVGVNSGQTAPYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFI
                     SNRTLGLIVFLGIVLGNLWKEKKTDKTKKGIENKIEN"
     exon            288..454
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     exon            455..576
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     exon            577..662
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     exon            663..796
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     exon            797..985
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     exon            986..1525
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1506..1511
                     /regulatory_class="polyA_signal_sequence"
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /note="hexamer: AATAAA"
     polyA_site      1525
                     /gene="COQ2"
                     /gene_synonym="CL640; COQ10D1; MSA1; PHB:PPT"
                     /note="major polyA site"
ORIGIN      
        1 gtcaatccga gctcgtcccg gcctcaccag cgccatgctg ggctcgcgag ccgcggggtt
       61 cgcgcggggc ctgcgggctg tggcactggc gtggctgccg ggctggcggg gccgctcctt
      121 cgccctggcg cgtgcggcag gcgcgcccca cggtggtgac ttgcagcccc ccgcctgtcc
      181 cgagccgcgc gggcgccagc tcagtttgtc cgcggcggcg gtggtggact ctgcgccccg
      241 ccccctgcag ccgtacttgc gcctcatgcg gttggacaag cccattggaa cctggcttct
      301 gtatttacca tgtacctgga gcattggttt ggcagctgaa ccaggttgtt ttccagattg
      361 gtacatgctc tccctctttg gcactggagc tattctgatg cgtggagcag gctgtactat
      421 taatgacatg tgggaccagg actatgataa aaaggttaca agaacagcca atcgtccaat
      481 agccgctgga gacatttcaa cttttcagtc ctttgttttt cttgggggac agctaaccct
      541 ggcactgggt gttcttctgt gtctaaatta ctacagtata gctctgggag caggatcctt
      601 acttcttgtc atcacctacc cactaatgaa aagaatttca tactggcctc aactagcctt
      661 gggcttgaca tttaattggg gagcgttact tggatggtct gctatcaagg gttcctgtga
      721 tccatctgtt tgcctgcctc tttatttttc tggagttatg tggacactaa tatatgatac
      781 tatttatgcc catcaggaca aaagagatga tgttttgatt ggtcttaagt caacggctct
      841 gcggttcgga gaaaatacca agccgtggct cagcggcttc agtgttgcaa tgctgggggc
      901 actgagccta gtgggtgtga acagtggaca gactgctccc tactacgctg ccctgggtgc
      961 tgtaggagcc catctgactc accagattta cactctagac atccacagac ctgaggattg
     1021 ttggaataaa tttatctcca accgaacact gggactaata gtttttttag ggattgtcct
     1081 tgggaatttg tggaaagaaa agaagacaga caaaacaaag aagggtatag agaataaaat
     1141 agaaaattaa tgaatgaaat ttatctagga atttttaaaa cattttttac aaaatataat
     1201 tagatttgaa tacaaaatct gatacaatat gttaaagaat taagaacctg aagatgaaga
     1261 tttagagcat atttacctgg attttactta tttgctagca aaattccccc ttgtcacaga
     1321 aaccagggac tcttcaggat ttgagatggc cttgagtatt ttagttgata cattcttctg
     1381 cccattataa ttctcacctg aagttatggg gattgcacgg gttttggcac tttagaaaaa
     1441 gcctgatgtg ggtcttacat aaatgaatgt ctgtataaga aaatggactc ttttttttag
     1501 ggaaaaataa aagcaactat gggaa
//
