CHKB_MOUSE
ID CHKB_MOUSE Reviewed; 394 AA.
AC O55229;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Choline/ethanolamine kinase;
DE AltName: Full=Choline kinase beta;
DE Short=CK;
DE Short=CKB;
DE EC=2.7.1.32 {ECO:0000250|UniProtKB:Q9Y259};
DE AltName: Full=Ethanolamine kinase;
DE Short=EK;
DE EC=2.7.1.82 {ECO:0000250|UniProtKB:Q9Y259};
DE AltName: Full=choline/ethanolamine kinase beta;
DE Short=CKEKB;
GN Name=Chkb; Synonyms=Chetk, Chkl;
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].
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 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 [3]
RP DISEASE.
RX PubMed=16371353; DOI=10.1074/jbc.m512578200;
RA Sher R.B., Aoyama C., Huebsch K.A., Ji S., Kerner J., Yang Y.,
RA Frankel W.N., Hoppel C.L., Wood P.A., Vance D.E., Cox G.A.;
RT "A rostrocaudal muscular dystrophy caused by a defect in choline kinase
RT beta, the first enzyme in phosphatidylcholine biosynthesis.";
RL J. Biol. Chem. 281:4938-4948(2006).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19236939; DOI=10.1016/j.bbalip.2009.02.006;
RA Wu G., Sher R.B., Cox G.A., Vance D.E.;
RT "Understanding the muscular dystrophy caused by deletion of choline kinase
RT beta in mice.";
RL Biochim. Biophys. Acta 1791:347-356(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and 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: Has a key role in phospholipid metabolism, and catalyzes the
CC first step of phosphatidylethanolamine and phosphatidylcholine
CC biosynthesis. {ECO:0000250|UniProtKB:Q9Y259}.
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:Q9Y259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000250|UniProtKB:Q9Y259};
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:Q9Y259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000250|UniProtKB:Q9Y259};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000250|UniProtKB:Q9Y259}.
CC -!- SUBUNIT: Homodimer, and heterodimer with CHKA.
CC {ECO:0000269|PubMed:16490392}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with the highest level in
CC testis.
CC -!- DISEASE: Note=Defects in Chkb are a cause of rostrocaudal muscular
CC dystrophy (rmd). The disease is characterized by rapidly progressive
CC muscular dystrophy and neonatal forelimb bone deformity. The dystrophy
CC is only evident in skeletal muscle tissues in an unusual rostral-to-
CC caudal gradient. {ECO:0000269|PubMed:16371353}.
CC -!- DISRUPTION PHENOTYPE: Hindlimb muscular dystrophy. Hindlimb skeletal
CC muscle tissue exhibits impaired phosphatidylcholine biosynthesis and
CC increased phosphatidylcholine catabolism, with concomitant accumulation
CC of choline. Mitochondria are abnormally large and exhibit decreased
CC inner membrane potential. {ECO:0000269|PubMed:19236939}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; AB011001; BAA24897.1; -; Transcribed_RNA.
DR EMBL; AB011000; BAA24896.1; -; mRNA.
DR CCDS; CCDS27750.1; -.
DR RefSeq; NP_031718.1; NM_007692.6.
DR AlphaFoldDB; O55229; -.
DR SMR; O55229; -.
DR BioGRID; 198695; 2.
DR IntAct; O55229; 1.
DR STRING; 10090.ENSMUSP00000023289; -.
DR iPTMnet; O55229; -.
DR PhosphoSitePlus; O55229; -.
DR EPD; O55229; -.
DR PaxDb; O55229; -.
DR PeptideAtlas; O55229; -.
DR PRIDE; O55229; -.
DR ProteomicsDB; 281212; -.
DR DNASU; 12651; -.
DR Ensembl; ENSMUST00000023289; ENSMUSP00000023289; ENSMUSG00000022617.
DR GeneID; 12651; -.
DR KEGG; mmu:12651; -.
DR UCSC; uc007xgs.2; mouse.
DR CTD; 1120; -.
DR MGI; MGI:1328313; Chkb.
DR VEuPathDB; HostDB:ENSMUSG00000022617; -.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_2_1_1; -.
DR InParanoid; O55229; -.
DR OMA; CKPRLLE; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; O55229; -.
DR TreeFam; TF313549; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 12651; 0 hits in 74 CRISPR screens.
DR PRO; PR:O55229; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O55229; protein.
DR Bgee; ENSMUSG00000022617; Expressed in islet of Langerhans and 93 other tissues.
DR ExpressionAtlas; O55229; baseline and differential.
DR Genevisible; O55229; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; IMP:MGI.
DR GO; GO:0004305; F:ethanolamine kinase activity; ISO:MGI.
DR GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:MGI.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR026712; Cho/Etha_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603:SF35; PTHR22603:SF35; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y259"
FT CHAIN 2..394
FT /note="Choline/ethanolamine kinase"
FT /id="PRO_0000206223"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 77..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y259"
SQ SEQUENCE 394 AA; 45126 MW; A5EE79EC551D07A2 CRC64;
MAADGTGVVG GGAVGGGLPK DGLQDAKCPE PIPNRRRASS LSRDAQRRAY QWCREYLGGA
WRRARPEELS VCPVSGGLSN LLFRCSLPNH VPSVGGEPRE VLLRLYGAIL QGVDSLVLES
VMFAILAERS LGPQLYGVFP EGRLEQYLPS RPLKTQELRD PVLSGAIATR MARFHGMEMP
FTKEPRWLFG TMERYLKQIQ DLPSTSLPQM NLVEMYSLKD EMNSLRKLLD DTPSPVVFCH
NDIQEGNILL LSEPDSDDNL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTY EEWPFYKARP
TDYPTREQQL HFIRHYLAEV QKGEILSEEE QKKREEELLL EISRYSLASH FFWGLWSTLQ
ASMSTIEFGY LEYAQSRFQF YFQQKGQLTS SPSS
