KICH_YEAST
ID KICH_YEAST Reviewed; 582 AA.
AC P20485; D6VYC8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Choline kinase {ECO:0000305};
DE EC=2.7.1.32 {ECO:0000269|PubMed:10329685, ECO:0000269|PubMed:2536698};
DE AltName: Full=ATP:choline phosphotransferase {ECO:0000303|PubMed:9506987};
GN Name=CKI1 {ECO:0000303|PubMed:2536698}; Synonyms=CKI;
GN OrderedLocusNames=YLR133W; ORFNames=L3130, L9606.8;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2536698; DOI=10.1016/s0021-9258(18)94140-2;
RA Hosaka K., Kodaki T., Yamashita S.;
RT "Cloning and characterization of the yeast CKI gene encoding choline kinase
RT and its expression in Escherichia coli.";
RL J. Biol. Chem. 264:2053-2059(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RX PubMed=9506987; DOI=10.1074/jbc.273.12.6844;
RA Kim K.H., Voelker D.R., Flocco M.T., Carman G.M.;
RT "Expression, purification, and characterization of choline kinase, product
RT of the CKI gene from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:6844-6852(1998).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10329685; DOI=10.1074/jbc.274.21.14857;
RA Kim K., Kim K.-H., Storey M.K., Voelker D.R., Carman G.M.;
RT "Isolation and characterization of the Saccharomyces cerevisiae EKI1 gene
RT encoding ethanolamine kinase.";
RL J. Biol. Chem. 274:14857-14866(1999).
RN [7]
RP PATHWAY.
RX PubMed=11078727; DOI=10.1074/jbc.m003694200;
RA Dowd S.R., Bier M.E., Patton-Vogt J.L.;
RT "Turnover of phosphatidylcholine in Saccharomyces cerevisiae. The role of
RT the CDP-choline pathway.";
RL J. Biol. Chem. 276:3756-3763(2001).
RN [8]
RP PHOSPHORYLATION AT SER-30 AND SER-85, AND MUTAGENESIS OF SER-30 AND SER-85.
RX PubMed=12105205; DOI=10.1074/jbc.m205316200;
RA Yu Y., Sreenivas A., Ostrander D.B., Carman G.M.;
RT "Phosphorylation of Saccharomyces cerevisiae choline kinase on Ser30 and
RT Ser85 by protein kinase A regulates phosphatidylcholine synthesis by the
RT CDP-choline pathway.";
RL J. Biol. Chem. 277:34978-34986(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51 AND THR-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the committed step in the synthesis of
CC phosphatidylcholine by the CDP-choline pathway (PubMed:2536698,
CC PubMed:9506987, PubMed:10329685). Also exhibits ethanolamine kinase
CC activity but it is a poor substrate at 14% efficiency compared with
CC choline (PubMed:2536698, PubMed:9506987). {ECO:0000269|PubMed:10329685,
CC ECO:0000269|PubMed:2536698, ECO:0000269|PubMed:9506987}.
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:0000269|PubMed:10329685,
CC ECO:0000269|PubMed:2536698, ECO:0000269|PubMed:9506987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000305|PubMed:10329685};
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 Evidence={ECO:0000269|PubMed:10329685, ECO:0000269|PubMed:2536698};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000305|PubMed:10329685, ECO:0000305|PubMed:2536698};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9506987};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for ATP {ECO:0000269|PubMed:9506987};
CC KM=0.27 mM for choline {ECO:0000269|PubMed:9506987};
CC Vmax=138.7 umol/min/mg enzyme for choline
CC {ECO:0000269|PubMed:9506987};
CC pH dependence:
CC Optimum pH is 9.5-12. {ECO:0000269|PubMed:9506987};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:9506987};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from choline: step 1/1. {ECO:0000305|PubMed:11078727}.
CC -!- SUBUNIT: Monomer. Interacts with NAP1. {ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P20485; P25293: NAP1; NbExp=5; IntAct=EBI-9699, EBI-11850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; J04454; AAA34499.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62646.1; -; Genomic_DNA.
DR EMBL; Z73305; CAA97704.1; -; Genomic_DNA.
DR EMBL; U53881; AAB82396.1; -; Genomic_DNA.
DR EMBL; AY692779; AAT92798.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09444.1; -; Genomic_DNA.
DR PIR; A32034; A32034.
DR RefSeq; NP_013234.1; NM_001182020.1.
DR AlphaFoldDB; P20485; -.
DR SMR; P20485; -.
DR BioGRID; 31402; 121.
DR DIP; DIP-2617N; -.
DR IntAct; P20485; 7.
DR MINT; P20485; -.
DR STRING; 4932.YLR133W; -.
DR SwissLipids; SLP:000000066; -.
DR iPTMnet; P20485; -.
DR MaxQB; P20485; -.
DR PaxDb; P20485; -.
DR PRIDE; P20485; -.
DR EnsemblFungi; YLR133W_mRNA; YLR133W; YLR133W.
DR GeneID; 850824; -.
DR KEGG; sce:YLR133W; -.
DR SGD; S000004123; CKI1.
DR VEuPathDB; FungiDB:YLR133W; -.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_4_2_1; -.
DR InParanoid; P20485; -.
DR OMA; EREGGPM; -.
DR BioCyc; MetaCyc:YLR133W-MON; -.
DR BioCyc; YEAST:YLR133W-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR UniPathway; UPA00753; UER00737.
DR PRO; PR:P20485; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P20485; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; IDA:SGD.
DR GO; GO:0004305; F:ethanolamine kinase activity; IMP:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR007521; Choline_kin_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF04428; Choline_kin_N; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9506987"
FT CHAIN 2..582
FT /note="Choline kinase"
FT /id="PRO_0000206226"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:12105205"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:12105205"
FT MUTAGEN 30
FT /note="S->A: Decrease in activity and in phosphorylation by
FT PKA. No phosphorylation by PKA, and strong decrease in
FT activity; when associated with A-85."
FT /evidence="ECO:0000269|PubMed:12105205"
FT MUTAGEN 85
FT /note="S->A: No phosphorylation by PKA, and strong decrease
FT in activity; when associated with A-30."
FT /evidence="ECO:0000269|PubMed:12105205"
SQ SEQUENCE 582 AA; 66317 MW; 68C395B9CC120A0E CRC64;
MVQESRPGSV RSYSVGYQAR SRSSSQRRHS LTRQRSSQRL IRTISIESDV SNITDDDDLR
AVNEGVAGVQ LDVSETANKG PRRASATDVT DSLGSTSSEY IEIPFVKETL DASLPSDYLK
QDILNLIQSL KISKWYNNKK IQPVAQDMNL VKISGAMTNA IFKVEYPKLP SLLLRIYGPN
IDNIIDREYE LQILARLSLK NIGPSLYGCF VNGRFEQFLE NSKTLTKDDI RNWKNSQRIA
RRMKELHVGV PLLSSERKNG SACWQKINQW LRTIEKVDQW VGDPKNIENS LLCENWSKFM
DIVDRYHKWL ISQEQGIEQV NKNLIFCHND AQYGNLLFTA PVMNTPSLYT APSSTSLTSQ
SSSLFPSSSN VIVDDIINPP KQEQSQDSKL VVIDFEYAGA NPAAYDLANH LSEWMYDYNN
AKAPHQCHAD RYPDKEQVLN FLYSYVSHLR GGAKEPIDEE VQRLYKSIIQ WRPTVQLFWS
LWAILQSGKL EKKEASTAIT REEIGPNGKK YIIKTEPESP EEDFVENDDE PEAGVSIDTF
DYMAYGRDKI AVFWGDLIGL GIITEEECKN FSSFKFLDTS YL
