LOCUS       NM_017421               1325 bp    mRNA    linear   PRI 19-SEP-2024
DEFINITION  Homo sapiens coenzyme Q3, methyltransferase (COQ3), mRNA; nuclear
            gene for mitochondrial product.
ACCESSION   NM_017421
VERSION     NM_017421.4
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 1325)
  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   2  (bases 1 to 1325)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (bases 1 to 1325)
  AUTHORS   Stefely,J.A. and Pagliarini,D.J.
  TITLE     Biochemistry of Mitochondrial Coenzyme Q Biosynthesis
  JOURNAL   Trends Biochem Sci 42 (10), 824-843 (2017)
   PUBMED   28927698
  REMARK    Review article
REFERENCE   4  (bases 1 to 1325)
  AUTHORS   Floyd,B.J., Wilkerson,E.M., Veling,M.T., Minogue,C.E., Xia,C.,
            Beebe,E.T., Wrobel,R.L., Cho,H., Kremer,L.S., Alston,C.L.,
            Gromek,K.A., Dolan,B.K., Ulbrich,A., Stefely,J.A., Bohl,S.L.,
            Werner,K.M., Jochem,A., Westphall,M.S., Rensvold,J.W., Taylor,R.W.,
            Prokisch,H., Kim,J.P., Coon,J.J. and Pagliarini,D.J.
  TITLE     Mitochondrial Protein Interaction Mapping Identifies Regulators of
            Respiratory Chain Function
  JOURNAL   Mol Cell 63 (4), 621-632 (2016)
   PUBMED   27499296
REFERENCE   5  (bases 1 to 1325)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1325)
  AUTHORS   Franke,B., Vermeulen,S.H., Steegers-Theunissen,R.P., Coenen,M.J.,
            Schijvenaars,M.M., Scheffer,H., den Heijer,M. and Blom,H.J.
  TITLE     An association study of 45 folate-related genes in spina bifida:
            Involvement of cubilin (CUBN) and tRNA aspartic acid
            methyltransferase 1 (TRDMT1)
  JOURNAL   Birth Defects Res A Clin Mol Teratol 85 (3), 216-226 (2009)
   PUBMED   19161160
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (bases 1 to 1325)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (bases 1 to 1325)
  AUTHORS   Jonassen,T. and Clarke,C.F.
  TITLE     Isolation and functional expression of human COQ3, a gene encoding
            a methyltransferase required for ubiquinone biosynthesis
  JOURNAL   J Biol Chem 275 (17), 12381-12387 (2000)
   PUBMED   10777520
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136726.1, BC001534.1 and AL513550.9.
            
            On Nov 22, 2018 this sequence version replaced NM_017421.3.
            
            Summary: Ubiquinone, also known as coenzyme Q, or Q, is a critical
            component of the electron transport pathways of both eukaryotes and
            prokaryotes (Jonassen and Clarke, 2000 [PubMed 10777520]). This
            lipid consists of a hydrophobic isoprenoid tail and a quinone head
            group. The tail varies in length depending on the organism, but its
            purpose is to anchor coenzyme Q to the membrane. The quinone head
            group is responsible for the activity of coenzyme Q in the
            respiratory chain. The S. cerevisiae COQ3 gene encodes an
            O-methyltransferase required for 2 steps in the biosynthetic
            pathway of coenzyme Q. This enzyme methylates an early coenzyme Q
            intermediate, 3,4-dihydroxy-5-polyprenylbenzoic acid, as well as
            the final intermediate in the pathway, converting
            demethyl-ubiquinone to coenzyme Q. The COQ3 gene product is also
            capable of methylating the distinct prokaryotic early intermediate
            2-hydroxy-6-polyprenyl phenol.[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056955.1, BC001534.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254759.8/ ENSP00000254759.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-77                AL136726.1         10-86
            78-1000             BC001534.1         60-982
            1001-1230           AL513550.9         14818-15047         c
            1231-1250           AL136726.1         1240-1259
            1251-1254           BC001534.1         1233-1236
            1255-1325           AL513550.9         14723-14793         c
FEATURES             Location/Qualifiers
     source          1..1325
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.2"
     gene            1..1325
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /note="coenzyme Q3, methyltransferase"
                     /db_xref="GeneID:51805"
                     /db_xref="HGNC:HGNC:18175"
                     /db_xref="MIM:605196"
     exon            1..122
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     CDS             17..1126
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /EC_number="2.1.1.114"
                     /EC_number="2.1.1.64"
                     /note="methyltransferase COQ3; dihydroxyhexaprenylbenzoate
                     methyltransferase; 3,4-dihydroxy-5-hexaprenylbenzoate
                     methyltransferase; DHHB methyltransferase;
                     hexaprenyldihydroxybenzoate methyltransferase,
                     mitochondrial; DHHB-MTase; 3-demethylubiquinone-10
                     3-methyltransferase; polyprenyldihydroxybenzoate
                     methyltransferase; 2-polyprenyl-6-hydroxyphenyl methylase;
                     coenzyme Q3 homolog, methyltransferase;
                     2-polyprenyl-6-hydroxyphenol methylase;
                     3-demethylubiquinol 3-O-methyltransferase"
                     /codon_start=1
                     /product="ubiquinone biosynthesis O-methyltransferase,
                     mitochondrial"
                     /protein_id="NP_059117.3"
                     /db_xref="CCDS:CCDS5042.1"
                     /db_xref="GeneID:51805"
                     /db_xref="HGNC:HGNC:18175"
                     /db_xref="MIM:605196"
                     /translation="MWSGRKLGSSGGWFLRVLGPGGCNTKAARPLISSAVYVKNQLSG
                     TLQIKPGVFNEYRTIWFKSYRTIFSCLNRIKSFRYPWARLYSTSQTTVDSGEVKTFLA
                     LAHKWWDEQGVYAPLHSMNDLRVPFIRDNLLKTIPNHQPGKPLLGMKILDVGCGGGLL
                     TEPLGRLGASVIGIDPVDENIKTAQCHKSFDPVLDKRIEYRVCSLEEIVEETAETFDA
                     VVASEVVEHVIDLETFLQCCCQVLKPGGSLFITTINKTQLSYALGIVFSEQIASIVPK
                     GTHTWEKFVSPETLESILESNGLSVQTVVGMLYNPFSGYWHWSENTSLNYAAYAVKSR
                     VQEHPASAEFVLKGETEELQANACTNPAVHEKLKK"
     exon            123..249
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     exon            250..402
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     exon            403..502
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     exon            503..745
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     exon            746..905
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     exon            906..1325
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1231..1236
                     /regulatory_class="polyA_signal_sequence"
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /note="hexamer: AATAAA"
     polyA_site      1254
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /note="major polyA site"
     regulatory      1304..1309
                     /regulatory_class="polyA_signal_sequence"
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
                     /note="hexamer: AATAAA"
     polyA_site      1325
                     /gene="COQ3"
                     /gene_synonym="bA9819.1; DHHBMT; DHHBMTASE; UG0215E05"
ORIGIN      
        1 gggatcgttt gtcgcgatgt ggagtggccg taagctgggc tcctccgggg gttggttttt
       61 aagagtgctg gggcctggag gctgtaatac aaaagctgcg cgtcccttaa tttcctcggc
      121 ggtttatgtg aagaaccagc tcagtgggac tctacagatt aaaccagggg ttttcaatga
      181 atacagaacc atatggttca aatcctacag gacgatcttt tcctgtttga acagaataaa
      241 gagtttcagg tacccttggg cgagactgta cagtacttcc caaaccactg tcgacagcgg
      301 tgaggtaaaa accttcttgg ccctggctca caaatggtgg gatgaacaag gagtatatgc
      361 acctcttcat tccatgaatg acctgagggt gccatttatt agggacaatc ttctgaaaac
      421 aattcctaat caccagccag gaaaaccttt gttggggatg aagattcttg acgttggctg
      481 tggtggtggg ctgttaactg aacctctagg gcggcttggg gcttcagtta ttggaatcga
      541 ccctgtggat gagaacatta aaacagcaca atgccataaa tcatttgatc cagtcctgga
      601 taagagaata gagtacagag tgtgttccct ggaagagatt gtggaagaga ctgcagaaac
      661 atttgatgct gttgtagctt ctgaagttgt agaacatgtg attgatctag aaacattttt
      721 acagtgctgc tgtcaagtgt taaaacccgg tggttcttta ttcattacta caatcaacaa
      781 aacacaactt tcctatgcct tgggaattgt tttttcagag caaattgcaa gtattgtacc
      841 aaaaggtact catacatggg agaagtttgt ttcacctgaa acactagaga gcattctgga
      901 atcaaatggt ctgtcagttc aaacagtggt aggaatgctc tataacccct tctcaggtta
      961 ctggcattgg agtgaaaata ccagccttaa ctatgcagct tatgctgtga aatccagggt
     1021 ccaggaacac ccagcctctg ctgagtttgt tttaaaggga gaaacagaag agctccaagc
     1081 taatgcctgc accaatccag ctgtgcatga aaagctgaag aaatgaattg tttctgagaa
     1141 ctatagtaat atggcttgga tatctgatgt tttcaaatac aaaaatgtac aatttatcct
     1201 ttgagagaga atcatgaaga aaagaaggtc aataaaaagg gctaaaacct tggacaaaag
     1261 tttttgttat ttcgtctaat agctactttc aagggattct gtgaataaaa agttttgtca
     1321 agata
//
