COQ9
entrez
57017
canonical
uniprot
O75208
canonical
ensembl
ENSG00000088682
resolver
ensp
ENSP00000262507
resolver
genesymbol
COQ9
resolver
genesymbol_syn
C16orf49
resolver
hgnc
HGNC:25302
resolver
uniprot
A8K3L2
resolver
uniprot
Q7L5V7
resolver
uniprot
Q7Z5T6
resolver
uniprot
Q8NBL4
resolver
uniprot
Q9NTJ2
resolver
uniprot
Q9P056
resolver
uniprot_entry
COQ9_HUMAN
resolver
uniprot_sec
A8K3L2
resolver
uniprot_sec
Q7L5V7
resolver
uniprot_sec
Q7Z5T6
resolver
uniprot_sec
Q8NBL4
resolver
uniprot_sec
Q9NTJ2
resolver
uniprot_sec
Q9P056
resolver
amino_acid_sequence
MAAAAVSGALGRAGWRLLQLRCLPVARCRQALVPRAFHASAVGLRSSDEQKQQPPNSFSQQHSETQGAEKPDPESSHSPPRYTDQGGEEEEDYESEEQLQHRILTAALEFVPAHGWTAEAIAEGAQSLGLSSAAASMFGKDGSELILHFVTQCNTRLTRVLEEEQKLVQLGQAEKRKTDQFLRDAVETRLRMLIPYIEHWPRALSILMLPHNIPSSLSLLTSMVDDMWHYAGDQSTDFNWYTRRAMLAAIYNTTELVMMQDSSPDFEDTWRFLENRVNDAMNMGHTAKQVKSTGEALVQGLMGAAVTLKNLTGLNQRR
uniprot
proteins
disease_involvement
DISEASE: Coenzyme Q10 deficiency, primary, 5 (COQ10D5) [MIM:614654]: A form of coenzyme Q10 deficiency, 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:19375058}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to COQ7, therefore facilitating the COQ7-mediated hydroxylase step (PubMed:25339443, PubMed:30661980, PubMed:38425362). Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25339443, PubMed:30661980). {ECO:0000269|PubMed:25339443, ECO:0000269|PubMed:30661980, ECO:0000269|PubMed:38425362}.
uniprot
proteins
mass_dalton
35509
uniprot
proteins
mutagenesis
MUTAGEN 190; /note="L->E: Impairs interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 227; /note="M->E: Impairs interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 237; /note="D->K: Impairs interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 240; /note="W->D,K: Abolishes interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 240; /note="W->K: Disrupts the octameric COQ7:COQ9 complex."; /evidence="ECO:0000269|PubMed:36306796"; MUTAGEN 241; /note="Y->D,K: Abolishes interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 256; /note="L->K: Impairs interaction with COQ7."; /evidence="ECO:0000269|PubMed:25339443"; MUTAGEN 288; /note="K->A: Decreases membrane association; when associated with A-291."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 290; /note="V->A: Significantly decreases membrane association; when associated with A-297; A-298; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 290; /note="V->S: Decreases membrane association by more than 60%; when associated with A-297; A-298; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 291; /note="K->A: Decreases membrane association; when associated with A-288."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 297; /note="L->A: Significantly decreases membrane association; when associated with A-290; A-298; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 297; /note="L->S: Decreases membrane association by more than 60%; when associated with A-290; A-298; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 298; /note="V->A: Significantly decreases membrane association; when associated with A-290; A-297; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 298; /note="V->S: Decreases membrane association by more than 60%; when associated with A-290; A-297; A-301 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 301; /note="L->A: Significantly decreases membrane association; when associated with A-290; A-297; A-298 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 301; /note="L->S: Decreases membrane association by more than 60%; when associated with A-290; A-297; A-298 and A-302."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 302; /note="M->A: Significantly decreases membrane association; when associated with A-290; A-297; A-298 and A-301."; /evidence="ECO:0000269|PubMed:30661980"; MUTAGEN 302; /note="M->S: Decreases membrane association by more than 60%; when associated with A-290; A-297; A-298 and A-301."; /evidence="ECO:0000269|PubMed:30661980
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q8K1Z0}.
uniprot
proteins
post_translational_modification
PTM: In response to mitochondrial stress, the precursor protein is ubiquitinated by the SIFI complex in the cytoplasm before mitochondrial import, leading to its degradation (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). {ECO:0000269|PubMed:38297121}.
uniprot
proteins
protein_family
COQ9 family
uniprot
proteins
pubmed
10493829
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
19375058
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25339443
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30661980
uniprot
proteins
pubmed
36306796
uniprot
proteins
pubmed
38297121
uniprot
proteins
pubmed
38425362
uniprot
proteins
sequence_length
318
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}. Note=Associates with cardiolipin-rich membranes which leads to the lipid bilayer deformation and then accessing to membrane-bound lipids. {ECO:0000269|PubMed:30661980}.
uniprot
proteins