COQ2
entrez
27235
canonical
uniprot
Q96H96
canonical
ensembl
ENSG00000173085
resolver
ensp
ENSP00000310873
resolver
ensp
ENSP00000495761
resolver
genesymbol
COQ2
resolver
genesymbol_syn
CL640
resolver
hgnc
HGNC:25223
resolver
uniprot
A0A1D8H0A6
resolver
uniprot
O95331
resolver
uniprot
Q1JQ78
resolver
uniprot
Q684R2
resolver
uniprot_entry
COQ2_HUMAN
resolver
uniprot_sec
A0A1D8H0A6
resolver
uniprot_sec
O95331
resolver
uniprot_sec
Q1JQ78
resolver
uniprot_sec
Q684R2
resolver
amino_acid_sequence
MLGSRAAGFARGLRAVALAWLPGWRGRSFALARAAGAPHGGDLQPPACPEPRGRQLSLSAAAVVDSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAAEPGCFPDWYMLSLFGTGAILMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYYSIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGALLGWSAIKGSCDPSVCLPLYFSGVMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTKPWLSGFSVAMLGALSLVGVNSGQTAPYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFISNRTLGLIVFLGIVLGNLWKEKKTDKTKKGIENKIEN
uniprot
proteins
disease_involvement
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, ECO:0000269|PubMed:33215859}. Note=The disease is caused by variants 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 variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.5.1.39
uniprot
proteins
function
FUNCTION: Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis (PubMed:15153069, PubMed:16400613, PubMed:17374725, PubMed:20526342). Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-trans-decaprenyl diphosphate) (PubMed:15153069, PubMed:16400613, PubMed:17374725, PubMed:20526342). The length of the polyprenyl side chain varies depending on the species, in humans, the side chain is comprised of 10 isoprenyls (decaprenyl) producing CoQ10 (also known as ubiquinone), whereas rodents predominantly generate CoQ9 (PubMed:15153069, PubMed:16400613). However, this specificity is not complete, human tissues have low amounts of CoQ9 and rodent organs contain some CoQ10 (PubMed:15153069). Plays a central role in the biosynthesis of CoQ10 (PubMed:15153069, PubMed:16400613, PubMed:17374725). CoQ10 is a vital molecule that transports electrons from mitochondrial respiratory chain complexes (PubMed:16400613, PubMed:17374725, PubMed:27493029). CoQs also function as cofactors for uncoupling protein and play a role as regulators of the extracellularly-induced ceramide-dependent apoptotic pathway (PubMed:16400613, PubMed:17374725). Regulates mitochondrial permeability transition pore (mPTP) opening and ROS production (pivotal events in cell death) in a tissue specific manner (By similarity). {ECO:0000250|UniProtKB:Q499N4, ECO:0000269|PubMed:15153069, ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725, ECO:0000269|PubMed:20526342, ECO:0000269|PubMed:27493029, ECO:0000303|PubMed:15153069, ECO:0000303|PubMed:16400613, ECO:0000303|PubMed:17374725}.
uniprot
proteins
mass_dalton
40475
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000269|PubMed:16400613, ECO:0000269|PubMed:17374725, ECO:0000305|PubMed:15153069}.
uniprot
proteins
protein_family
UbiA prenyltransferase family
uniprot
proteins
pubmed
15153069
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16400613
uniprot
proteins
pubmed
17374725
uniprot
proteins
pubmed
17855635
uniprot
proteins
pubmed
20526342
uniprot
proteins
pubmed
23343605
uniprot
proteins
pubmed
23758206
uniprot
proteins
pubmed
25564041
uniprot
proteins
pubmed
27493029
uniprot
proteins
pubmed
28044327
uniprot
proteins
pubmed
33215859
uniprot
proteins
sequence_length
371
uniprot
proteins
subcellular_location
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 84..104; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 109..129; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 149..169; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 173..193; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 204..224; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 232..252; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 278..298; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 301..321; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189"; TRANSMEM 333..353; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03189
uniprot
proteins