ID CK1_ARATH Reviewed; 346 AA. AC Q9M9H6; Q9C9J3; DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 147. DE RecName: Full=Probable choline kinase 1; DE Short=AtCK1; DE EC=2.7.1.32; GN Name=CK1; Synonyms=CK; OrderedLocusNames=At1g71697; GN ORFNames=F14O23.8, F26A9.3; 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=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). 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]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING. RX PubMed=9342878; DOI=10.1104/pp.115.2.817; RA Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.; RT "Jasmonic acid-dependent and -independent signaling pathways control wound- RT induced gene activation in Arabidopsis thaliana."; RL Plant Physiol. 115:817-826(1997). RN [6] 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 -!- TISSUE SPECIFICITY: Expressed in roots. Expressed at low levels in CC cauline leaves and flowers. {ECO:0000269|PubMed:9342878}. CC -!- INDUCTION: By wounding, and salt and osmotic stresses. CC {ECO:0000269|PubMed:15147879, ECO:0000269|PubMed:9342878}. CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG51828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC012654; AAF43223.1; -; Genomic_DNA. DR EMBL; AC016163; AAG51828.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE35220.1; -; Genomic_DNA. DR EMBL; BT008311; AAP37670.1; -; mRNA. DR EMBL; AK229787; BAF01619.1; -; mRNA. DR EMBL; AK230407; BAF02205.1; -; mRNA. DR PIR; C96739; C96739. DR RefSeq; NP_177315.1; NM_105828.4. DR AlphaFoldDB; Q9M9H6; -. DR SMR; Q9M9H6; -. DR BioGRID; 28720; 1. DR STRING; 3702.Q9M9H6; -. DR iPTMnet; Q9M9H6; -. DR PaxDb; 3702-AT1G71697-1; -. DR ProteomicsDB; 246868; -. DR EnsemblPlants; AT1G71697.1; AT1G71697.1; AT1G71697. DR GeneID; 843500; -. DR Gramene; AT1G71697.1; AT1G71697.1; AT1G71697. DR KEGG; ath:AT1G71697; -. DR Araport; AT1G71697; -. DR TAIR; AT1G71697; CK1. DR eggNOG; KOG2686; Eukaryota. DR HOGENOM; CLU_012712_0_2_1; -. DR InParanoid; Q9M9H6; -. DR OMA; YECKPRL; -. DR OrthoDB; 144299at2759; -. DR PhylomeDB; Q9M9H6; -. DR BioCyc; ARA:AT1G71697-MONOMER; -. DR BRENDA; 2.7.1.32; 399. DR UniPathway; UPA00753; UER00737. DR PRO; PR:Q9M9H6; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9M9H6; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004103; F:choline kinase activity; ISS:TAIR. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009611; P:response to wounding; IEP:TAIR. DR CDD; cd05157; ETNK_euk; 1. DR Gene3D; 3.90.1200.10; -; 1. DR InterPro; IPR007521; Choline_kin_N. DR InterPro; IPR011009; Kinase-like_dom_sf. DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1. DR PANTHER; PTHR22603:SF93; RE24176P; 1. DR Pfam; PF04428; Choline_kin_N; 1. DR Pfam; PF01633; Choline_kinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR Genevisible; Q9M9H6; AT. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1..346 FT /note="Probable choline kinase 1" FT /id="PRO_0000423346" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" SQ SEQUENCE 346 AA; 40016 MW; 3FABBAAAB09B5597 CRC64; MAIKTKTSLI PSCSSPEDLK RVLQTLGSSW GDVVEDLERL EVVPLKGAMT NEVYQINWPT LNGEDVHRKV LVRIYGDGVD LFFNRGDEIK TFECMSHHGY GPKLLGRFSD GRLEEFIHAR TLSADDLRVA ETSDFIAAKL REFHKLDMPG PKNVLLWERL RTWLKEAKNL ASPIEMDKYR LEGLENEINL LEERLTRDDQ EIGFCHNDLQ YGNVMIDEVT NAITIIDYEY SSFNPIAYDI ANHFCEMAAN YHSDTPHVLD YTLYPGEGER RRFISTYLGS TGNATSDKEV ERLLKDAESY TLANHIFWGL WGIISGHVNK IEFDYMEYAR QRFEQYWLRK PLLLEG //