COQ8A_DANRE
ID COQ8A_DANRE Reviewed; 619 AA.
AC Q5RGU1; G1K2I4; Q6DH95;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Atypical kinase COQ8A, mitochondrial {ECO:0000305};
DE EC=2.7.-.- {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=Chaperone activity of bc1 complex-like {ECO:0000250|UniProtKB:Q8NI60};
DE Short=Chaperone-ABC1-like {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=Coenzyme Q protein 8A {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=aarF domain-containing protein kinase 3 {ECO:0000250|UniProtKB:Q8NI60};
DE Flags: Precursor;
GN Name=coq8a {ECO:0000250|UniProtKB:Q8NI60};
GN Synonyms=adck3 {ECO:0000250|UniProtKB:Q8NI60},
GN cabc1 {ECO:0000250|UniProtKB:Q8NI60};
GN ORFNames=zgc:92578 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q,
CC also named ubiquinone, an essential lipid-soluble electron transporter
CC for aerobic cellular respiration. Its substrate specificity is unclear:
CC does not show any protein kinase activity. Probably acts as a small
CC molecule kinase, possibly a lipid kinase that phosphorylates a prenyl
CC lipid in the ubiquinone biosynthesis pathway, as suggested by its
CC ability to bind coenzyme Q lipid intermediates. Shows an unusual
CC selectivity for binding ADP over ATP. {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- ACTIVITY REGULATION: Autoinhibited by the N-terminal domain, containing
CC the KxGQ motif, that completely occludes the typical substrate binding
CC pocket. Nucleotide-binding relieves inhibition.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its transmembrane region.
CC Interacts with the multi-subunit COQ enzyme complex.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8NI60}.
CC Membrane {ECO:0000255}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NI60, ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RGU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RGU1-2; Sequence=VSP_022355;
CC -!- DOMAIN: Adopts an atypical protein kinase-like fold: while it adopts a
CC core fold similar to that of well-characterized protein kinase-like
CC domains. The KxGQ motif completely occludes the typical substrate
CC binding pocket. Nucleotide-binding opens the substrate binding pocket
CC and flips the active site from inside the hydrophobic core into a
CC catalytically competent, solvent-exposed posture.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI11905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI12066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX569783; CAI11905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX649588; CAI11905.1; JOINED; Genomic_DNA.
DR EMBL; BX649588; CAI12066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX569783; CAI12066.1; JOINED; Genomic_DNA.
DR EMBL; BC076083; AAH76083.1; -; mRNA.
DR RefSeq; NP_001002728.2; NM_001002728.2. [Q5RGU1-1]
DR AlphaFoldDB; Q5RGU1; -.
DR SMR; Q5RGU1; -.
DR STRING; 7955.ENSDARP00000024635; -.
DR PaxDb; Q5RGU1; -.
DR DNASU; 437001; -.
DR Ensembl; ENSDART00000020153; ENSDARP00000024635; ENSDARG00000020123. [Q5RGU1-1]
DR GeneID; 437001; -.
DR KEGG; dre:437001; -.
DR CTD; 437001; -.
DR ZFIN; ZDB-GENE-040718-487; coq8aa.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000156810; -.
DR HOGENOM; CLU_006533_9_0_1; -.
DR InParanoid; Q5RGU1; -.
DR OMA; LEMGNVH; -.
DR OrthoDB; 525494at2759; -.
DR TreeFam; TF300630; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q5RGU1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000020123; Expressed in muscle tissue and 29 other tissues.
DR ExpressionAtlas; Q5RGU1; baseline and differential.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR CDD; cd13970; ABC1_ADCK3; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR034646; ADCK3_dom.
DR InterPro; IPR034640; COQ8A.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR43851:SF1; PTHR43851:SF1; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Membrane; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transferase; Transit peptide;
KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..619
FT /note="Atypical kinase COQ8A, mitochondrial"
FT /id="PRO_0000271796"
FT TRANSMEM 182..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 298..487
FT /note="Protein kinase"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..248
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 306..309
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT ACT_SITE 457
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 414..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT VAR_SEQ 25..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022355"
FT CONFLICT 404
FT /note="S -> G (in Ref. 2; AAH76083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68951 MW; 10CBFECBDC43BFC0 CRC64;
MAGDMLLLMR GLARLSQAVI ETQANSLRSG GVQTMQMTAE QAMGVAMQKI QEFTGSQQSV
SDFSADMDSK YDFTASEQNF ESAAHGGLDS DSVFRDANTG AANTYSQAQG KSKLFDGYKD
PTSQFTGHTR SYHQDHSSVG GITAEDIEKA REAKQNGSKP HKQMLSERAR ERKVPVTRLG
RLANFGGLAV GLGIGALAEV AKKSLRSEDK NGNKKAVLDS SPFLSEANAE RIVRTLCKVR
GAALKLGQML SIQDDAFINP QLAKIFERVR QSADFMPIKQ MTKALSNDLG PNWRDKLEMF
EERPFAAASI GQVHLARMKD GREVAMKIQY PGVAQSINSD VNNLMTVLSM SNALPEGLFP
EHLIDVMRRE LALECDYIRE AKCARKFKEL LKDHPFFYVP DVISELSSQH VLTTELVPGF
PLDQAEALTQ ELKNEICKNI LNLCLRELFE FRYMQTDPNW SNFFYDPQTH RVALLDFGAT
RGFDESFTDV YIEIIKAAAD GNREGVLKQS IDMKFLTGYE SKAMVNAHVD AVMILGEAFA
SEEPFDFGAQ STTERIHNLI PVMLKQRLIP PPEETYSLHR KMGGSFLICS RLNAKISCKD
MFEAAYSNYW SGRKKGPSQ
