CK3_ARATH
ID CK3_ARATH Reviewed; 346 AA.
AC Q9SZ92; Q8L9C6; Q8LF42;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable choline kinase 3;
DE EC=2.7.1.32;
GN OrderedLocusNames=At4g09760; ORFNames=F17A8.110;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION.
RX PubMed=15147879; DOI=10.1016/j.febslet.2004.04.015;
RA Tasseva G., Richard L., Zachowski A.;
RT "Regulation of phosphatidylcholine biosynthesis under salt stress involves
RT choline kinases in Arabidopsis thaliana.";
RL FEBS Lett. 566:115-120(2004).
CC -!- FUNCTION: Involved in phospholipid biosynthesis. Catalyzes the first
CC step in phosphatidylcholine biosynthesis (By similarity).
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from choline: step 1/1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SZ92-1; Sequence=Displayed;
CC -!- INDUCTION: By wounding, and salt and osmotic stresses.
CC {ECO:0000269|PubMed:15147879}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; AL049482; CAB39643.1; -; Genomic_DNA.
DR EMBL; AL161515; CAB78099.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82792.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82793.1; -; Genomic_DNA.
DR EMBL; AY085061; AAM61617.1; -; mRNA.
DR EMBL; AY088512; AAM66047.1; -; mRNA.
DR PIR; T04023; T04023.
DR RefSeq; NP_192714.1; NM_117044.3. [Q9SZ92-1]
DR RefSeq; NP_849350.1; NM_179019.1. [Q9SZ92-1]
DR AlphaFoldDB; Q9SZ92; -.
DR SMR; Q9SZ92; -.
DR STRING; 3702.AT4G09760.1; -.
DR PaxDb; Q9SZ92; -.
DR PRIDE; Q9SZ92; -.
DR ProteomicsDB; 246808; -. [Q9SZ92-1]
DR DNASU; 826564; -.
DR EnsemblPlants; AT4G09760.1; AT4G09760.1; AT4G09760. [Q9SZ92-1]
DR EnsemblPlants; AT4G09760.2; AT4G09760.2; AT4G09760. [Q9SZ92-1]
DR GeneID; 826564; -.
DR Gramene; AT4G09760.1; AT4G09760.1; AT4G09760. [Q9SZ92-1]
DR Gramene; AT4G09760.2; AT4G09760.2; AT4G09760. [Q9SZ92-1]
DR KEGG; ath:AT4G09760; -.
DR Araport; AT4G09760; -.
DR TAIR; locus:2118450; AT4G09760.
DR eggNOG; KOG2686; Eukaryota.
DR HOGENOM; CLU_012712_0_2_1; -.
DR InParanoid; Q9SZ92; -.
DR OMA; MDWLKEY; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; Q9SZ92; -.
DR BRENDA; 2.7.1.32; 399.
DR UniPathway; UPA00753; UER00737.
DR PRO; PR:Q9SZ92; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ92; baseline and differential.
DR Genevisible; Q9SZ92; AT.
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; IBA:GO_Central.
DR GO; GO:0004305; F:ethanolamine kinase activity; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="Probable choline kinase 3"
FT /id="PRO_0000423348"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 64..67
FT /note="RCRK -> QCRN (in Ref. 3; AAM66047)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="I -> T (in Ref. 3; AAM61617)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="T -> S (in Ref. 3; AAM61617)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..183
FT /note="DIE -> CID (in Ref. 3; AAM61617)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="A -> T (in Ref. 3; AAM66047)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="E -> D (in Ref. 3; AAM61617)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="F -> Y (in Ref. 3; AAM61617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 40351 MW; CF5CCA7CF80F5FF7 CRC64;
MAVGIFGLIP SSSPDELRKI LQALSTKWGD VVEDFESLEV KPMKGAMTNE VFMVSWPRKE
TNLRCRKLLV RVYGEGVELF FNRDDEIRTF EYVARHGHGP TLLGRFAGGR VEEFIHARTL
SATDLRDPNI SALVASKLRR FHSIHIPGDR IMLIWDRMRT WVGQAKNLCS NEHSTEFGLD
DIEDEINLLE QEVNNEQEIG FCHNDLQYGN IMIDEETNAI TIIDYEYASY NPIAYDIANH
FCEMAADYHS NTPHILDYTL YPGEEERRRF ICNYLTSSGE EAREEDIEQL LDDIEKYTLA
SHLFWGLWGI ISGYVNKIEF DYIEYSRQRF KQYWLRKPKL LSFFPS
