COQ8A_BOVIN
ID COQ8A_BOVIN Reviewed; 648 AA.
AC Q29RI0; Q0V8G9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-648.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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, composed of at
CC least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
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 -!- 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, a number of features are positioned to inhibit the kinase
CC activity: (1) an atypical AAAS motif in an alanine-rich (A-rich) loop
CC that replaces the canonical glycine-rich (G-rich) nucleotide-binding
CC loop and limits ATP binding by establishing an unusual selectivity for
CC ADP and (2) an N-terminal domain, containing the KxGQ motif, that
CC completely occludes the typical substrate binding pocket. Nucleotide-
CC binding opens the substrate binding pocket and flips the active site
CC from inside the hydrophobic core into a catalytically competent,
CC solvent-exposed posture. {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; BC114164; AAI14165.1; -; mRNA.
DR EMBL; BT026249; ABG67088.1; -; mRNA.
DR RefSeq; NP_001039884.1; NM_001046419.2.
DR RefSeq; XP_010811432.1; XM_010813130.2.
DR AlphaFoldDB; Q29RI0; -.
DR SMR; Q29RI0; -.
DR STRING; 9913.ENSBTAP00000029167; -.
DR PaxDb; Q29RI0; -.
DR PRIDE; Q29RI0; -.
DR Ensembl; ENSBTAT00000029167; ENSBTAP00000029167; ENSBTAG00000021880.
DR Ensembl; ENSBTAT00000066937; ENSBTAP00000071794; ENSBTAG00000021880.
DR GeneID; 536925; -.
DR KEGG; bta:536925; -.
DR CTD; 56997; -.
DR VEuPathDB; HostDB:ENSBTAG00000021880; -.
DR VGNC; VGNC:27616; COQ8A.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000156810; -.
DR HOGENOM; CLU_006533_9_1_1; -.
DR InParanoid; Q29RI0; -.
DR OMA; QVERVMN; -.
DR OrthoDB; 525494at2759; -.
DR TreeFam; TF300630; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000021880; Expressed in corpus luteum and 104 other tissues.
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 ATP-binding; Kinase; Membrane; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix; Ubiquinone biosynthesis.
FT TRANSIT 1..162
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT CHAIN 163..648
FT /note="Atypical kinase COQ8A, mitochondrial"
FT /id="PRO_0000271794"
FT TRANSMEM 214..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 329..518
FT /note="Protein kinase"
FT REGION 90..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 276..279
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 337..340
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 445..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
SQ SEQUENCE 648 AA; 72082 MW; 217518E10C95C73D CRC64;
MAAMLGDAIM LIKGFVKLTQ AAVETHLQHL GLSGELLMAV RALQSTATEQ VGMVFGQVQG
QETPEEYYSE SLDDPEGAFH FSGMRAESAS ADVSAASSPE QSPPPWAHAA GSEGPAPAYV
ASAPFREGGV LGQAASPLGR VNGRLFASPR DPFSAPGLQR RVYHQDQSSM GGLTAEDIEK
ARQAKARPES KPHKQALSEH ARERKVPVTR IGRLANFGGL AVGLGFGALA EVAKKSLRPD
DPSGKKAVLD SSPFLSEANA ERIVRTLCKV RGAALKLGQM LSIQDDAFIN PHLAKIFDRV
RQSADFMPLK QMMKTLNNDL GPNWRDKLEY FEERPFAAAS IGQVHLARLK GGREVAMKIQ
YPGVAQSINS DVNNLMTVLN MSNMLPEGLF PEHLIDVLRR ELALECDYQR EAACARRFRE
LLKDHPFFYV PEIVDELCSP HVLTTELVSG FPLDQAEGLS QEIRNEICYN ILVLCLRELF
EFQFMQTDPN WSNFFYDPEL HKVALLDFGA TREFDRSFTD LYIQIIRAAA NQDREAVLKK
SIEMKFLTGY EVKAMEDAHL DAILILGEAF ASEEPFDFGT QSTTEKIHNL IPIMLKHRLV
PPPEETYSLH RKMGGSFLIC SKLKARFPCK AMFEEAYSNY CRRQAEQQ
