COQ8A_RAT
ID COQ8A_RAT Reviewed; 649 AA.
AC Q5BJQ0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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;
DE Flags: Precursor;
GN Name=Coq8a {ECO:0000250|UniProtKB:Q8NI60};
GN Synonyms=Adck3 {ECO:0000312|RGD:1308245},
GN Cabc1 {ECO:0000250|UniProtKB:Q8NI60};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC091388; AAH91388.1; -; mRNA.
DR RefSeq; NP_001013203.1; NM_001013185.1.
DR RefSeq; XP_006250449.1; XM_006250387.1.
DR AlphaFoldDB; Q5BJQ0; -.
DR SMR; Q5BJQ0; -.
DR BioGRID; 262280; 1.
DR STRING; 10116.ENSRNOP00000036948; -.
DR iPTMnet; Q5BJQ0; -.
DR PhosphoSitePlus; Q5BJQ0; -.
DR PaxDb; Q5BJQ0; -.
DR PRIDE; Q5BJQ0; -.
DR Ensembl; ENSRNOT00000030135; ENSRNOP00000036948; ENSRNOG00000043201.
DR GeneID; 360887; -.
DR KEGG; rno:360887; -.
DR CTD; 56997; -.
DR RGD; 1308245; Coq8a.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000156810; -.
DR HOGENOM; CLU_006533_9_1_1; -.
DR InParanoid; Q5BJQ0; -.
DR OMA; QVERVMN; -.
DR OrthoDB; 525494at2759; -.
DR PhylomeDB; Q5BJQ0; -.
DR TreeFam; TF300630; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q5BJQ0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000043201; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5BJQ0; RN.
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..163
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT CHAIN 164..649
FT /note="Atypical kinase COQ8A, mitochondrial"
FT /id="PRO_0000271795"
FT TRANSMEM 215..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 330..519
FT /note="Protein kinase"
FT REGION 84..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..280
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 338..341
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 446..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
SQ SEQUENCE 649 AA; 72226 MW; E7EBC66B6163A9F6 CRC64;
MAAMLGDAIM VAKGLAKLTQ AAVETHLQNL GLGGELILAA RALQSTAVEQ ISMVFGKVQG
QDKHEDSYAT ENFEDLEAEV QFSTPQAAGS SPDFSTASSL DQPLSSSLGH AHREGPAPAY
VSSGPFREAG LSGQATSPLG RVNGRLFVDC RDLFLANSIQ RRFFHQDQAP VGGLTAEDIE
KARQAKARPE SKPHKQMLSE RARERKVPVT RIGRLANFGG LAVGLGFGAL AEVAKKSLRS
ENSTGKKAVL DSSPFLSEAN AERIVSTLCK VRGAALKLGQ MLSIQDDAFI NPHLAKIFER
VRQSADFMPL KQMTKTLNND LGPHWRDKLE YFEERPFAAA SIGQVHLARL KGGREVAMKI
QYPGVAQSIN SDVNNLMAVL NMSNMLPEGL FPEHLIDVLR RELTLECDYQ REAAYAKKFR
ELLKDHPFFY VPEIVDELCS PHVLTTELIT GFPLDQAEGL SQEVRNEICY NILVLCLREL
FEFHVMQTDP NWSNFFYDPQ QHKVALLDFG ATREYDRSFT DLYIQVIRAA ADQDREAVLK
KSIEMKFLTG YEVKAMEDAH LDAILILGEA FASEEPFDFG TQSTTEKIHN LIPIMLKHRL
IPPPEETYSL HRKMGGSFLI CSKLKACFPC KAMFEEAYSN YCRMKSGLQ
