COQ8B_RAT
ID COQ8B_RAT Reviewed; 528 AA.
AC Q6AY19;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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|RGD:1311356};
DE AltName: Full=Coenzyme Q protein 8B {ECO:0000250|UniProtKB:Q96D53};
GN Name=Coq8b {ECO:0000250|UniProtKB:Q96D53};
GN Synonyms=Adck4 {ECO:0000312|RGD:1311356};
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=Testis;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24270420; DOI=10.1172/jci69000;
RA Ashraf S., Gee H.Y., Woerner S., Xie L.X., Vega-Warner V., Lovric S.,
RA Fang H., Song X., Cattran D.C., Avila-Casado C., Paterson A.D.,
RA Nitschke P., Bole-Feysot C., Cochat P., Esteve-Rudd J., Haberberger B.,
RA Allen S.J., Zhou W., Airik R., Otto E.A., Barua M., Al-Hamed M.H.,
RA Kari J.A., Evans J., Bierzynska A., Saleem M.A., Bockenhauer D., Kleta R.,
RA El Desoky S., Hacihamdioglu D.O., Gok F., Washburn J., Wiggins R.C.,
RA Choi M., Lifton R.P., Levy S., Han Z., Salviati L., Prokisch H.,
RA Williams D.S., Pollak M., Clarke C.F., Pei Y., Antignac C., Hildebrandt F.;
RT "ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ10
RT biosynthesis disruption.";
RL J. Clin. Invest. 123:5179-5189(2013).
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 -!- TISSUE SPECIFICITY: In the kidney, expressed in glomeruli,
CC predominantly in podocyte foot precesses, as well as in proximal
CC tubules and collecting ducts (at protein level).
CC {ECO:0000269|PubMed:24270420}.
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}.
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DR EMBL; BC079227; AAH79227.1; -; mRNA.
DR RefSeq; NP_001012065.1; NM_001012065.1.
DR RefSeq; XP_017444608.1; XM_017589119.1.
DR AlphaFoldDB; Q6AY19; -.
DR SMR; Q6AY19; -.
DR IntAct; Q6AY19; 2.
DR STRING; 10116.ENSRNOP00000028290; -.
DR PaxDb; Q6AY19; -.
DR PRIDE; Q6AY19; -.
DR Ensembl; ENSRNOT00000028290; ENSRNOP00000028290; ENSRNOG00000020848.
DR GeneID; 308453; -.
DR KEGG; rno:308453; -.
DR UCSC; RGD:1311356; rat.
DR CTD; 79934; -.
DR RGD; 1311356; Coq8b.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000158965; -.
DR HOGENOM; CLU_006533_9_0_1; -.
DR InParanoid; Q6AY19; -.
DR OMA; KFHQDGP; -.
DR OrthoDB; 525494at2759; -.
DR PRO; PR:Q6AY19; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020848; Expressed in testis and 20 other tissues.
DR Genevisible; Q6AY19; RN.
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: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..528
FT /note="Atypical kinase COQ8B, mitochondrial"
FT /id="PRO_0000271799"
FT TRANSMEM 93..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 187..419
FT /note="Protein kinase"
FT MOTIF 151..154
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 212..215
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 320..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
SQ SEQUENCE 528 AA; 58905 MW; 6ECBC3DD231B16B7 CRC64;
MWLELGAMLR TTCGPLGRAV RLPCAGALRL RPHWWGPCRD CLAQRVHQDQ PGRGLTEDEI
RRAREARLRK APRPQLSDRS RERKVPASRI SRLASFGGLA VGLGLGALAE VTKKSLPGGS
LQHEGSSPFL TEANAERIVQ TLCTVRGAAL KIGQMLSIQD NSLISPQLQR VFERVRQSAD
FMPRWQMMKV LEEELGKDWQ DKVASLEEVP FAAASIGQVH QGVLKDGTEV AVKIQYPGVA
ESIQSDVQNL LALLKMSVGL PEGLFAEQSL QTLQQELAWE CDYRREAACA QTFKKLLADD
PFFRVPAVVE ELCTTRVLGM ELAGGIPLDQ CQGLSQDIRN QICFQLLRLC LRELFEFRFM
QTDPNWANFL YDASSHKVTL LDFGASRAFG TEFTDHYIEV VKAAADGDRD RVLQKSQDLK
FLTGFETKAF SDAHVEAVMI LGEPFAASGS YDFGAGETAR RIQGLIPVLL RHRLRPPPEE
TYALHRKLAG AFLACARLHA HIACRDLFQD TYHRYWASRQ TLPLPAAS
