COQ8A
entrez
56997
canonical
uniprot
Q8NI60
canonical
ensembl
ENSG00000163050
resolver
ensp
ENSP00000355739
resolver
ensp
ENSP00000543752
resolver
ensp
ENSP00000543753
resolver
ensp
ENSP00000543759
resolver
ensp
ENSP00000543761
resolver
ensp
ENSP00000543763
resolver
ensp
ENSP00000543765
resolver
ensp
ENSP00000543766
resolver
ensp
ENSP00000543777
resolver
ensp
ENSP00000620339
resolver
genesymbol
COQ8A
resolver
genesymbol_syn
ADCK3
resolver
genesymbol_syn
CABC1
resolver
hgnc
HGNC:16812
resolver
uniprot
Q5T7A5
resolver
uniprot
Q63HK0
resolver
uniprot
Q8NCJ6
resolver
uniprot
Q9HBQ1
resolver
uniprot
Q9NQ67
resolver
uniprot_entry
COQ8A_HUMAN
resolver
uniprot_sec
Q5T7A5
resolver
uniprot_sec
Q63HK0
resolver
uniprot_sec
Q8NCJ6
resolver
uniprot_sec
Q9HBQ1
resolver
uniprot_sec
Q9NQ67
resolver
activity_regulation
ACTIVITY REGULATION: Autoinhibited by the N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket (PubMed:25498144, PubMed:27499294). Nucleotide-binding relieves inhibition (PubMed:27499294). Specifically inhibited by 4-anilinoquinoline compound TPP-UNC-CA157 (PubMed:36302899). {ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:27499294, ECO:0000269|PubMed:36302899}.
uniprot
proteins
amino_acid_sequence
MAAILGDTIMVAKGLVKLTQAAVETHLQHLGIGGELIMAARALQSTAVEQIGMFLGKVQGQDKHEEYFAENFGGPEGEFHFSVPHAAGASTDFSSASAPDQSAPPSLGHAHSEGPAPAYVASGPFREAGFPGQASSPLGRANGRLFANPRDSFSAMGFQRRFFHQDQSPVGGLTAEDIEKARQAKARPENKQHKQTLSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVAKKSLRSEDPSGKKAVLGSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPHLAKIFERVRQSADFMPLKQMMKTLNNDLGPNWRDKLEYFEERPFAAASIGQVHLARMKGGREVAMKIQYPGVAQSINSDVNNLMAVLNMSNMLPEGLFPEHLIDVLRRELALECDYQREAACARKFRDLLKGHPFFYVPEIVDELCSPHVLTTELVSGFPLDQAEGLSQEIRNEICYNILVLCLRELFEFHFMQTDPNWSNFFYDPQQHKVALLDFGATREYDRSFTDLYIQIIRAAADRDRETVRAKSIEMKFLTGYEVKVMEDAHLDAILILGEAFASDEPFDFGTQSTTEKIHNLIPVMLRHRLVPPPEETYSLHRKMGGSFLICSKLKARFPCKAMFEEAYSNYCKRQAQQ
uniprot
proteins
disease_involvement
DISEASE: Coenzyme Q10 deficiency, primary, 4 (COQ10D4) [MIM:612016]: An autosomal recessive disorder characterized by childhood-onset of cerebellar ataxia and exercise intolerance. Patient manifest gait ataxia and cerebellar atrophy with slow progression. Additional features include brisk tendon reflexes and Hoffmann sign, variable psychomotor retardation and variable seizures. {ECO:0000269|PubMed:18319072, ECO:0000269|PubMed:18319074, ECO:0000269|PubMed:20580948, ECO:0000269|PubMed:22036850, ECO:0000269|PubMed:24048965, ECO:0000269|PubMed:24218524, ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:26818466, ECO:0000269|PubMed:27106809}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.-.-
uniprot
proteins
function
FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:21296186, PubMed:25498144, PubMed:25540914, PubMed:27499294, PubMed:36302899, PubMed:38425362). Its substrate specificity is still unclear: may act as a protein kinase that mediates phosphorylation of COQ3 (By similarity). According to other reports, acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (PubMed:25498144, PubMed:27499294). However, the small molecule kinase activity was not confirmed by another publication (By similarity). Shows an unusual selectivity for binding ADP over ATP (PubMed:25498144). {ECO:0000250|UniProtKB:Q96D53, ECO:0000269|PubMed:21296186, ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:25540914, ECO:0000269|PubMed:27499294, ECO:0000269|PubMed:36302899, ECO:0000269|PubMed:38425362}.
uniprot
proteins
mass_dalton
71950
uniprot
proteins
mutagenesis
MUTAGEN 214; /note="L->A,I,L,F: Strongly impairs homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 214; /note="L->I,F,G,V: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 215; /note="A->I,L,G: Does not impair homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 216; /note="N->A,L,F,M: Does not impair homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 217; /note="F->A: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 218; /note="G->I,L,F: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 219; /note="G->A,F: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 219; /note="G->I: Strongly impairs homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 220; /note="L->G: Impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 221; /note="A->L: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 222; /note="V->A: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 223; /note="G->A,I,L,F: Strongly impairs homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 224; /note="L->V: Impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 225; /note="G->L: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 226; /note="F->A: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 227; /note="G->V,F,L,I: Strongly impairs homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 228; /note="A->I,L,F: Does not impair homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 229; /note="L->A: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 230; /note="A->I: Slightly impaired homodimerization."; /evidence="ECO:0000269|PubMed:25216398"; MUTAGEN 276; /note="K->R,H: Does not affect selectivity for binding ADP or ATP. Impaired multi-subunit COQ enzyme complex."; /evidence="ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:27499294"; MUTAGEN 279; /note="Q->R,H: Does not affect selectivity for binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 339; /note="A->G: Enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 358; /note="K->R: Abolishes binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 405; /note="E->A,Q: Slightly affects selectivity for binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 411; /note="E->Q: Impaired binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 488; /note="D->N: Impaired binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 493; /note="N->A: Impaired binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144"; MUTAGEN 495; /note="F->A,L: Decreased binding to UNC-CA157 inhibitor."; /evidence="ECO:0000269|PubMed:36302899"; MUTAGEN 507; /note="D->N: Strongly impairs binding ADP or ATP. Impaired multi-subunit COQ enzyme complex."; /evidence="ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:27499294"; MUTAGEN 611; /note="R->A,Q: Does not affect selectivity for binding ADP or ATP."; /evidence="ECO:0000269|PubMed:25498144
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:36302899}.
uniprot
proteins
protein_family
ADCK protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11888884
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18319072
uniprot
proteins
pubmed
18319074
uniprot
proteins
pubmed
20580948
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21296186
uniprot
proteins
pubmed
22036850
uniprot
proteins
pubmed
24048965
uniprot
proteins
pubmed
24218524
uniprot
proteins
pubmed
24270420
uniprot
proteins
pubmed
25216398
uniprot
proteins
pubmed
25498144
uniprot
proteins
pubmed
25540914
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26818466
uniprot
proteins
pubmed
27106809
uniprot
proteins
pubmed
27499294
uniprot
proteins
pubmed
27499296
uniprot
proteins
pubmed
33988507
uniprot
proteins
pubmed
36302899
uniprot
proteins
pubmed
38425362
uniprot
proteins
sequence_length
647
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:11888884, ECO:0000269|PubMed:25498144, ECO:0000269|PubMed:33988507}; Single-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:25216398}.
uniprot
proteins
transmembrane_region
TRANSMEM 214..230; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:25216398
uniprot
proteins