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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
 
 
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