CK2_ARATH
ID CK2_ARATH Reviewed; 350 AA.
AC Q8L518; Q9C916;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable choline kinase 2;
DE EC=2.7.1.32;
GN OrderedLocusNames=At1g74320; ORFNames=F1O17.1;
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 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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC020579; AAG52400.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35577.1; -; Genomic_DNA.
DR EMBL; AY094430; AAM19803.1; -; mRNA.
DR EMBL; AY140093; AAM98234.1; -; mRNA.
DR EMBL; BT008737; AAP42750.1; -; mRNA.
DR PIR; G96771; G96771.
DR RefSeq; NP_177572.2; NM_106092.4.
DR AlphaFoldDB; Q8L518; -.
DR SMR; Q8L518; -.
DR STRING; 3702.AT1G74320.1; -.
DR PaxDb; Q8L518; -.
DR PRIDE; Q8L518; -.
DR ProteomicsDB; 246869; -.
DR EnsemblPlants; AT1G74320.1; AT1G74320.1; AT1G74320.
DR GeneID; 843772; -.
DR Gramene; AT1G74320.1; AT1G74320.1; AT1G74320.
DR KEGG; ath:AT1G74320; -.
DR Araport; AT1G74320; -.
DR TAIR; locus:2019612; AT1G74320.
DR eggNOG; KOG2686; Eukaryota.
DR HOGENOM; CLU_012712_0_2_1; -.
DR InParanoid; Q8L518; -.
DR OMA; HEWTADY; -.
DR OrthoDB; 1469912at2759; -.
DR PhylomeDB; Q8L518; -.
DR BioCyc; ARA:AT1G74320-MON; -.
DR BRENDA; 2.7.1.32; 399.
DR UniPathway; UPA00753; UER00737.
DR PRO; PR:Q8L518; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L518; baseline and differential.
DR Genevisible; Q8L518; 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 ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Probable choline kinase 2"
FT /id="PRO_0000423347"
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 350 AA; 41017 MW; 2C38393ADA5D2465 CRC64;
MTMGGTEKNV ENKQYRLPRE VKEALQAIAS EWEDVIDSKA LQVIPLKGAM TNEVFQIKWP
TREKGPSRKV LVRIYGEGVE IFFDREDEIR TFEFMSKHGH GPLLLGRFGN GRIEEFLHAR
TLSACDLRDP EISGRIATRM KEFHGLEMPG AKKALLWDRL RNWLTACKRL ASPEEAKSFR
LDVMEMEINM LEKSLFDNDE NIGFCHNDLQ YGNIMMDEET KAITIIDYEY SCYNPVAYDI
ANHFCEMAAD YHTETPHIMD YSKYPGVEER QRFLKTYMSY SDEKPSDTMV KKLLEDVEKY
TLASHLIWGL WGIISEHVNE IDFDYMEYAR QRFEQYWLTK PRLLAASEHK
