CHKA_MOUSE
ID CHKA_MOUSE Reviewed; 453 AA.
AC O54804; G5E853; Q8BPL3; Q8BPW6; Q9CXP3; Q9QX56;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Choline kinase alpha;
DE Short=CK;
DE EC=2.7.1.32 {ECO:0000250|UniProtKB:P35790};
DE AltName: Full=CHETK-alpha;
DE AltName: Full=Ethanolamine kinase;
DE Short=EK;
DE EC=2.7.1.82 {ECO:0000250|UniProtKB:P35790};
GN Name=Chka; Synonyms=Chk;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=9714798; DOI=10.1016/s0005-2760(98)00062-9;
RA Aoyama C., Nakashima K., Ishidate K.;
RT "Molecular cloning of mouse choline kinase and choline/ethanolamine kinase:
RT their sequence comparison to the respective rat homologs.";
RL Biochim. Biophys. Acta 1393:179-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=10706593;
RA Aoyama C., Yamazaki N., Terada H., Ishidate K.;
RT "Structure and characterization of the genes for murine
RT choline/ethanolamine kinase isozymes alpha and beta.";
RL J. Lipid Res. 41:452-464(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-371 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-150 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic eye, Embryonic head, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP SUBUNIT.
RX PubMed=16490392; DOI=10.1016/j.bbalip.2006.01.005;
RA Liao H., Aoyama C., Ishidate K., Teraoka H.;
RT "Deletion and alanine mutation analyses for the formation of active
RT homo- or hetero-dimer complexes of mouse choline kinase-alpha and -beta.";
RL Biochim. Biophys. Acta 1761:111-120(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18029352; DOI=10.1074/jbc.m708766200;
RA Wu G., Aoyama C., Young S.G., Vance D.E.;
RT "Early embryonic lethality caused by disruption of the gene for choline
RT kinase alpha, the first enzyme in phosphatidylcholine biosynthesis.";
RL J. Biol. Chem. 283:1456-1462(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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: Plays a key role in phospholipid biosynthesis by catalyzing
CC the phosphorylation of free choline to phosphocholine, the first step
CC in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine,
CC thereby contributing to phosphatidylethanolamine biosynthesis. Has
CC higher activity with choline. May contribute to tumor cell growth.
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- FUNCTION: [Isoform 1]: This isoform plays a key role in lipolysis of
CC lipid droplets following glucose deprivation (By similarity). In
CC response to glucose deprivation, phosphorylated by AMPK, promoting
CC localization to lipid droplets (By similarity). Phosphorylation is
CC followed by acetylation by KAT5, leading to dissociation of the
CC homodimer into a monomer (By similarity). Monomeric CHKA isoform 1 is
CC converted into a tyrosine-protein kinase, which phosphorylates lipid
CC droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of
CC lipid droplets (By similarity). {ECO:0000250|UniProtKB:P35790}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + choline = ADP + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216;
CC EC=2.7.1.32; Evidence={ECO:0000250|UniProtKB:P35790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000250|UniProtKB:P35790};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000250|UniProtKB:P35790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000250|UniProtKB:P35790};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P35790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC Evidence={ECO:0000250|UniProtKB:P35790};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from choline: step 1/1. {ECO:0000250|UniProtKB:P35790}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- SUBUNIT: Homodimer (PubMed:16490392). Heterodimer with CHKB
CC (PubMed:16490392). {ECO:0000269|PubMed:16490392}.
CC -!- SUBUNIT: [Isoform 1]: Monomer; acetylation by KAT5 promotes
CC dissociation of the homodimer and monomerization.
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet
CC {ECO:0000250|UniProtKB:P35790}. Note=Isoform 1 localizes to lipid
CC droplets following phosphorylation by AMPK.
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CHETK-alpha2 {ECO:0000303|PubMed:10706593}, CHKalpha2
CC {ECO:0000303|PubMed:10706593};
CC IsoId=O54804-1; Sequence=Displayed;
CC Name=2; Synonyms=CHETK-alpha1 {ECO:0000303|PubMed:10706593}, CHKalpha1
CC {ECO:0000303|PubMed:10706593};
CC IsoId=O54804-2; Sequence=VSP_009684;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with the highest level in
CC testis. {ECO:0000269|PubMed:9714798}.
CC -!- PTM: [Isoform 1]: Phosphorylated at Ser-275 by AMPK in response to
CC glucose deprivation, leading to localization to lipid droplets.
CC {ECO:0000250|UniProtKB:P35790}.
CC -!- PTM: [Isoform 1]: Acetylated by KAT5 at Lys-243 following
CC phosphorylation by AMPK, leading to monomerization and conversion into
CC a tyrosine-protein kinase. {ECO:0000250|UniProtKB:P35790}.
CC -!- DISRUPTION PHENOTYPE: Death at an early embryonic stage. Embryos die
CC after 3 to 5 days of development. {ECO:0000269|PubMed:18029352}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56758.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAA88154.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB29191.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC34841.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC35539.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB011002; BAA24898.1; -; mRNA.
DR EMBL; AB030621; BAA88153.1; -; Genomic_DNA.
DR EMBL; AB030621; BAA88154.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL32956.1; -; Genomic_DNA.
DR EMBL; BC056758; AAH56758.1; ALT_SEQ; mRNA.
DR EMBL; BC060218; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK014174; BAB29191.1; ALT_SEQ; mRNA.
DR EMBL; AK052056; BAC34841.1; ALT_SEQ; mRNA.
DR EMBL; AK053818; BAC35539.1; ALT_SEQ; mRNA.
DR CCDS; CCDS29400.1; -. [O54804-2]
DR CCDS; CCDS70913.1; -. [O54804-1]
DR RefSeq; NP_001258425.1; NM_001271496.1. [O54804-1]
DR RefSeq; NP_038518.2; NM_013490.4. [O54804-2]
DR AlphaFoldDB; O54804; -.
DR SMR; O54804; -.
DR BioGRID; 198701; 1.
DR STRING; 10090.ENSMUSP00000071933; -.
DR iPTMnet; O54804; -.
DR PhosphoSitePlus; O54804; -.
DR EPD; O54804; -.
DR MaxQB; O54804; -.
DR PaxDb; O54804; -.
DR PeptideAtlas; O54804; -.
DR PRIDE; O54804; -.
DR ProteomicsDB; 281669; -. [O54804-1]
DR ProteomicsDB; 281670; -. [O54804-2]
DR Antibodypedia; 16639; 234 antibodies from 29 providers.
DR DNASU; 12660; -.
DR Ensembl; ENSMUST00000025760; ENSMUSP00000025760; ENSMUSG00000024843. [O54804-1]
DR Ensembl; ENSMUST00000072055; ENSMUSP00000071933; ENSMUSG00000024843. [O54804-2]
DR GeneID; 12660; -.
DR KEGG; mmu:12660; -.
DR UCSC; uc008fxg.2; mouse. [O54804-2]
DR UCSC; uc008fxh.2; mouse. [O54804-1]
DR CTD; 1119; -.
DR MGI; MGI:107760; Chka.
DR VEuPathDB; HostDB:ENSMUSG00000024843; -.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_2_1_1; -.
DR InParanoid; O54804; -.
DR OMA; HEWTADY; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; O54804; -.
DR TreeFam; TF313549; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR UniPathway; UPA00753; UER00737.
DR BioGRID-ORCS; 12660; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Chka; mouse.
DR PRO; PR:O54804; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O54804; protein.
DR Bgee; ENSMUSG00000024843; Expressed in prostate gland ventral lobe and 253 other tissues.
DR ExpressionAtlas; O54804; baseline and differential.
DR Genevisible; O54804; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0033265; F:choline binding; ISO:MGI.
DR GO; GO:0004103; F:choline kinase activity; IDA:MGI.
DR GO; GO:0004104; F:cholinesterase activity; IDA:MGI.
DR GO; GO:0004305; F:ethanolamine kinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0019695; P:choline metabolic process; ISO:MGI.
DR GO; GO:0006580; P:ethanolamine metabolic process; ISO:MGI.
DR GO; GO:1905691; P:lipid droplet disassembly; ISS:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:MGI.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..453
FT /note="Choline kinase alpha"
FT /id="PRO_0000206220"
FT REGION 22..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT BINDING 115..117
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT BINDING 203..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01134"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35790"
FT VAR_SEQ 151..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9714798"
FT /id="VSP_009684"
FT CONFLICT 193
FT /note="F -> Y (in Ref. 1; BAA24898 and 2; BAA88154/
FT BAA88153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51985 MW; 66042FEE92C333D4 CRC64;
MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR TQPLALPPPP
PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR GLREDQFHIS VIRGGLSNML
FQCSLPDSIA SVGDEPRKVL LRLYGAILKM RSCNKEGSEQ AQNENEFQGA EAMVLESVMF
AILAERSLGP KLFGIFPQGR LEQFIPSRRL DTEELRLPDI SAEIAEKMAT FHGMKMPFNK
EPKWLFGTME KYLNQVLRLK FSREARVQQL HKILSYNLPL ELENLRSLLQ YTRSPVVFCH
NDCQEGNILL LEGQENSERR KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY TYEKYPFFRA
NIQKYPSRKQ QLHFISSYLT TFQNDFESLS SEEQFATKED MLLEVNRFAL ASHFLWGLWS
IVQAKISSIE FGYMEYAQAR FEAYFDQKRK LGV
