CHKB_RAT
ID CHKB_RAT Reviewed; 394 AA.
AC O54783;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
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 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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=9487136; DOI=10.1016/s0005-2760(97)00177-x;
RA Aoyama C., Nakashima K., Matsui M., Ishidate K.;
RT "Complementary DNA sequence for a 42 kDa rat kidney choline/ethanolamine
RT kinase.";
RL Biochim. Biophys. Acta 1390:1-7(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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:0000250|UniProtKB:Q9Y259}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; AB006607; BAA24366.1; -; mRNA.
DR EMBL; BC060515; AAH60515.1; -; mRNA.
DR RefSeq; NP_058873.1; NM_017177.1.
DR AlphaFoldDB; O54783; -.
DR SMR; O54783; -.
DR BioGRID; 248021; 1.
DR STRING; 10116.ENSRNOP00000015374; -.
DR PaxDb; O54783; -.
DR PRIDE; O54783; -.
DR Ensembl; ENSRNOT00000015374; ENSRNOP00000015374; ENSRNOG00000011404.
DR GeneID; 29367; -.
DR KEGG; rno:29367; -.
DR CTD; 1120; -.
DR RGD; 61826; Chkb.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_2_1_1; -.
DR InParanoid; O54783; -.
DR OMA; CKPRLLE; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; O54783; -.
DR TreeFam; TF313549; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-1483213; Synthesis of PE.
DR SABIO-RK; O54783; -.
DR UniPathway; UPA00558; UER00741.
DR PRO; PR:O54783; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000011404; Expressed in pancreas and 19 other tissues.
DR Genevisible; O54783; RN.
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; IDA:RGD.
DR GO; GO:0004305; F:ethanolamine kinase activity; ISO:RGD.
DR GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
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; Direct protein sequencing; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW 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_0000206224"
FT REGION 22..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; 45100 MW; A2E99EB055E3959E CRC64;
MAADGTGVVG GGAVGGPLSK DGLLDAKCPE PIPNRRRSSS LSRDAQRRAY QWCREYLGGA
WRRARPEELS VCPVSGGLSN LLFRCSLPNH VPSMGGEPRE VLLRLYGAIL QGVDSLVLES
VMFAILAERS LGPQLYGVFP EGRLEQYLPS RPLKTQELRD PVLSGAIATK MARFHGMEMP
FTKEPRWLFG TMERYLKQIQ DLPSTSLPQM NLVEMYSLKD EMNHLRTLLD ATPSPVVFCH
NDIQEGNILL LSEPDSDDNL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTY EEWPFYKARP
ADYPTREQQL LFIRHYLAEV QKGEVLSEEE QKKQEEDLLI EISRYALASH FFWGLWSTLQ
ASMSTIEFGY LEYAQSRFQF YFQQKGQLTS FLSP
