Q9NZJ6 (COQ3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial
EC=2.1.1.114

Alternative name(s):
2-polyprenyl-6-hydroxyphenyl methylase
EC=2.1.1.222
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
Short name=DHHB methyltransferase
Short name=DHHB-MT
Short name=DHHB-MTase
3-demethylubiquinone-10 3-methyltransferase
EC=2.1.1.64
Dihydroxyhexaprenylbenzoate methyltransferase

Gene names

Name:	COQ3
ORF Names:	UG0215E05

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate. Ref.6 S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n. Ref.6 S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol. Ref.6
Pathway	Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular location	Mitochondrion matrix Probable.
Sequence similarities	Belongs to the methyltransferase superfamily. UbiG/COQ3 family.
Sequence caution	The sequence AAF66826.1 differs from that shown. Reason: Frameshift at positions 16, 18, 22, 26, 44, 49, 60, 363 and 364.

Ontologies

Keywords
Biological process	Ubiquinone biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycerol metabolic process Inferred from genetic interaction Ref.6. Source: UniProtKB ubiquinone biosynthetic process Inferred from genetic interaction Ref.6. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity Inferred from electronic annotation. Source: InterPro 3-demethylubiquinone-9 3-O-methyltransferase activity Inferred from electronic annotation. Source: EC O-methyltransferase activity Traceable author statement Ref.6. Source: ProtInc hexaprenyldihydroxybenzoate methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 369		Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial		PRO_0000035926
Natural variations
	Natural variant	134	1	K → E. Ref.1 Ref.5 Corresponds to variant rs11548336 [ dbSNP | Ensembl ].		VAR_061925
	Natural variant	272	1	S → G. Ref.1 Ref.3 Ref.5 Ref.6 Corresponds to variant rs6925344 [ dbSNP | Ensembl ].		VAR_020789
	Natural variant	329	1	Y → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Corresponds to variant rs4144164 [ dbSNP | Ensembl ].		VAR_020790
Experimental info
	Sequence conflict	21	1	G → V in CAB66660. Ref.2
	Sequence conflict	180	1	N → D in CAB66660. Ref.2
	Sequence conflict	287 – 289	3	PET → LEP in AAN76515. Ref.1
	Sequence conflict	321	1	N → D in AAN76515. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9NZJ6 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: B257A099D6C06A2D	FASTA	369	41,054
	10 20 30 40 50 60 MWSGRKLGSS GGWFLRVLGP GGCNTKAARP LISSAVYVKN QLSGTLQIKP GVFNEYRTIW 70 80 90 100 110 120 FKSYRTIFSC LNRIKSFRYP WARLYSTSQT TVDSGEVKTF LALAHKWWDE QGVYAPLHSM 130 140 150 160 170 180 NDLRVPFIRD NLLKTIPNHQ PGKPLLGMKI LDVGCGGGLL TEPLGRLGAS VIGIDPVDEN 190 200 210 220 230 240 IKTAQCHKSF DPVLDKRIEY RVCSLEEIVE ETAETFDAVV ASEVVEHVID LETFLQCCCQ 250 260 270 280 290 300 VLKPGGSLFI TTINKTQLSY ALGIVFSEQI ASIVPKGTHT WEKFVSPETL ESILESNGLS 310 320 330 340 350 360 VQTVVGMLYN PFSGYWHWSE NTSLNYAAYA VKSRVQEHPA SAEFVLKGET EELQANACTN PAVHEKLKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of full-length cDNA clones from human fetal brain cDNA library." Xie Y., Mao Y. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-134; GLY-272 AND HIS-329. Tissue: Fetal brain.
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-329. Tissue: Kidney.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLY-272 AND HIS-329. Tissue: Skeletal muscle.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-134; GLY-272 AND HIS-329. Tissue: Brain and Skin.
[6]	"Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis." Jonassen T., Clarke C.F. J. Biol. Chem. 275:12381-12387(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-369, CATALYTIC ACTIVITY, VARIANTS GLY-272 AND HIS-329.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF351615 mRNA. Translation: AAN76515.1. AL136726 mRNA. Translation: CAB66660.1. AK056955 mRNA. Translation: BAG51832.1. AL513550 Genomic DNA. Translation: CAI17193.1. BC015634 mRNA. Translation: AAH15634.2. BC063463 mRNA. Translation: AAH63463.1. AF193016 mRNA. Translation: AAF66826.1. Frameshift.
IPI	IPI00418414.
RefSeq	NP_059117.3. NM_017421.3.
UniGene	Hs.713623.
3D structure databases
ProteinModelPortal	Q9NZJ6.
SMR	Q9NZJ6. Positions 121-299.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000254759.
PTM databases
PhosphoSite	Q9NZJ6.
Polymorphism databases
DMDM	57015321.
Proteomic databases
PaxDb	Q9NZJ6.
PRIDE	Q9NZJ6.
Protocols and materials databases
DNASU	51805.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000254759; ENSP00000254759; ENSG00000132423.
GeneID	51805.
KEGG	hsa:51805.
UCSC	uc003ppk.3. human.
Organism-specific databases
CTD	51805.
GeneCards	GC06M099817.
H-InvDB	HIX0200854.
HGNC	HGNC:18175. COQ3.
HPA	HPA031273. HPA031274.
MIM	605196. gene.
neXtProt	NX_Q9NZJ6.
PharmGKB	PA134934287.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2227.
HOVERGEN	HBG051078.
InParanoid	Q9NZJ6.
KO	K00591.
OMA	QETVESH.
OrthoDB	EOG4W6NWS.
PhylomeDB	Q9NZJ6.
Enzyme and pathway databases
BioCyc	MetaCyc:HS05632-MONOMER.
UniPathway	UPA00232.
Gene expression databases
ArrayExpress	Q9NZJ6.
Bgee	Q9NZJ6.
CleanEx	HS_COQ3.
Genevestigator	Q9NZJ6.
GermOnline	ENSG00000132423. Homo sapiens.
Family and domain databases
InterPro	IPR013216. Methyltransf_11. IPR010233. UbiG_MeTrfase. [Graphical view]
PANTHER	PTHR23134. PTHR23134. 1 hit.
Pfam	PF08241. Methyltransf_11. 1 hit. [Graphical view]
TIGRFAMs	TIGR01983. UbiG. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	51805.
NextBio	55924.
SOURCE	Search...

Entry information

Entry name

COQ3_HUMAN

Accession

Primary (citable) accession number: Q9NZJ6
Secondary accession number(s): B3KPX0 , Q5T061, Q6P4F0, Q8IXG6, Q96BG1, Q9H0N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.