CK1_ARATH
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 03-AUG-2022, entry version 140.
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};
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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.AT1G71697.1; -.
DR iPTMnet; Q9M9H6; -.
DR PaxDb; Q9M9H6; -.
DR PRIDE; Q9M9H6; -.
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; locus:2824546; AT1G71697.
DR eggNOG; KOG2686; Eukaryota.
DR HOGENOM; CLU_012712_0_2_1; -.
DR InParanoid; Q9M9H6; -.
DR OMA; NEKQXVS; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; Q9M9H6; -.
DR BioCyc; ARA:AT1G71697-MON; -.
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 Genevisible; Q9M9H6; 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; ISS:TAIR.
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 GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 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
