ID Q544J2_MOUSE Unreviewed; 412 AA.
AC Q544J2;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=Pdk4 {ECO:0000313|MGI:MGI:1351481};
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 {ECO:0000313|EMBL:BAC29590.1};
RN [1] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAB23359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB23359.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1};
RA Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [6] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Vagina {ECO:0000313|EMBL:BAC29590.1};
RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA Hayashizaki Y.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [8] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [9] {ECO:0000313|EMBL:BAC29590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC29590.1};
RC TISSUE=Lung {ECO:0000313|EMBL:BAB23359.1}, and Vagina
RC {ECO:0000313|EMBL:BAC29590.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [10] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036431};
CC -!- SUBUNIT: Homodimer. Interacts with the pyruvate dehydrogenase complex
CC subunit DLAT, and is part of the multimeric pyruvate dehydrogenase
CC complex that contains multiple copies of pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
CC dehydrogenase (DLD, E3). {ECO:0000256|ARBA:ARBA00038845}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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DR EMBL; AK004543; BAB23359.1; -; mRNA.
DR EMBL; AK036818; BAC29590.1; -; mRNA.
DR RefSeq; NP_038771.1; NM_013743.2.
DR AlphaFoldDB; Q544J2; -.
DR SMR; Q544J2; -.
DR MaxQB; Q544J2; -.
DR Antibodypedia; 15901; 678 antibodies from 36 providers.
DR DNASU; 27273; -.
DR GeneID; 27273; -.
DR KEGG; mmu:27273; -.
DR AGR; MGI:1351481; -.
DR CTD; 5166; -.
DR MGI; MGI:1351481; Pdk4.
DR VEuPathDB; HostDB:ENSMUSG00000019577; -.
DR HOGENOM; CLU_023861_1_1_1; -.
DR OMA; HQENCPS; -.
DR OrthoDB; 3058550at2759; -.
DR BioGRID-ORCS; 27273; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Pdk4; mouse.
DR ExpressionAtlas; Q544J2; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; IEA:Ensembl.
DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR CDD; cd16929; HATPase_PDK-like; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947:SF22; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE ISOZYME 4, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 245..368
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 412 AA; 46596 MW; 74815502E711054C CRC64;
MKAARFVMRS ASSLSSASLV PREVELFSRY SPSPLSMKQL LDFGSENACE RTSFAFLRQE
LPVRLANILK EIDILPDRLV NTPSVQLVKS WYIQSLMDLV EFHEKSPEDQ KALSEFVDTL
VKVRNRHHNV VPTMAQGILE YKDTCTVDPV TNQNLQYFLD RFYMNRISTR MLMNQHILIF
SDSKTGNPSH IGSIDPNCDV VAVVQDAFEC AKMLCDQYYL TSPELNLTQV NGKFPGQPIH
IVYVPSHLHH MLFELFKNAM RATVEHQENR PSLTPVEATV VLGKEDLTIK ISDRGGGVPL
RITDRLFSYT YSTAPTPVMD NSRNAPLAGF GYGLPISRLY AKYFQGDLNL YSMSGYGTDA
IIYLKALSSE SVEKLPVFNK SAFKHYQMSS EADDWCIPSR EPKNLAKEKL AV
//
