COQ8B_MOUSE
ID COQ8B_MOUSE Reviewed; 533 AA.
AC Q566J8; Q5XJH7; Q91WT5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Atypical kinase COQ8B, mitochondrial {ECO:0000305};
DE EC=2.7.-.- {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=AarF domain-containing protein kinase 4 {ECO:0000312|MGI:MGI:1924139};
DE AltName: Full=Coenzyme Q protein 8B {ECO:0000250|UniProtKB:Q96D53};
GN Name=Coq8b {ECO:0000250|UniProtKB:Q96D53};
GN Synonyms=Adck4 {ECO:0000312|MGI:MGI:1924139};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Required for podocyte
CC migration. {ECO:0000250|UniProtKB:Q8NI60,
CC ECO:0000250|UniProtKB:Q96D53}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its transmembrane region.
CC Interacts with COQ6 and COQ7. Interacts with the multi-subunit COQ
CC enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and
CC COQ9. {ECO:0000250|UniProtKB:Q96D53}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q96D53}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96D53}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96D53}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96D53}.
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=AAH13485.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC013485; AAH13485.1; ALT_INIT; mRNA.
DR EMBL; BC083324; AAH83324.1; -; mRNA.
DR EMBL; BC093498; AAH93498.1; -; mRNA.
DR CCDS; CCDS39847.1; -.
DR AlphaFoldDB; Q566J8; -.
DR SMR; Q566J8; -.
DR STRING; 10090.ENSMUSP00000003860; -.
DR PhosphoSitePlus; Q566J8; -.
DR EPD; Q566J8; -.
DR MaxQB; Q566J8; -.
DR PaxDb; Q566J8; -.
DR PRIDE; Q566J8; -.
DR ProteomicsDB; 283496; -.
DR MGI; MGI:1924139; Coq8b.
DR eggNOG; KOG1234; Eukaryota.
DR InParanoid; Q566J8; -.
DR PhylomeDB; Q566J8; -.
DR PRO; PR:Q566J8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q566J8; protein.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR034638; COQ8B.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR43851:SF4; PTHR43851:SF4; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..533
FT /note="Atypical kinase COQ8B, mitochondrial"
FT /id="PRO_0000271798"
FT TRANSMEM 93..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 192..424
FT /note="Protein kinase"
FT MOTIF 156..159
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 217..220
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 325..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT CONFLICT 289
FT /note="R -> C (in Ref. 1; AAH83324)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..304
FT /note="KLLAD -> SAFSS (in Ref. 1; AAH83324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59232 MW; 72B8FC097972E290 CRC64;
MWLELGAMLR RTCGPLGRAV RLPCGGALGP RPHWWGPCRS CLAQSVHQDQ PGRGLSEDDI
RRAREARLRK APRPQLSDRS RERKVPASRI SRLASFGGLA VGLGLGALAE VTKKSLPGGS
LQHEGVSGLG SSPFLSEANA ERIVQTLCTV RGAALKIGQM LSIQDNSFIS PQLQRIFERV
RQSADFMPRW QMMRVLEEEL GKDWQDKVAS LEEVPFAAAS IGQVHQGLLK DGTEVAVKIQ
YPGVAQSIQS DVENLLALLK MSVGLPEGLF AEQSLQTLQQ ELAWECDYRR EAACAQTFRK
LLADDPFFRV PAVVQELCTT RVLGMELAGG IPLDQCQGLS QDIRNQICFQ LLRLCLRELF
EFRFMQTDPN WANFLYDASS HQVTLLDFGA SRAFGTEFTD HYIEVVKAAA DGDRDRVLQK
SQDLKFLTGF ETKAFSDAHV EAVMILGEPF AASGPYDFGA GETARRIQGL IPVLLRHRLR
PPPEETYALH RKLAGAFLAC ARLHAHIACR DLFQDTYHRY WASRQTLPLP AAS
