CCT2_ARATH
ID CCT2_ARATH Reviewed; 304 AA.
AC F4JJE0; O23367; Q8L4J8;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Choline-phosphate cytidylyltransferase 2 {ECO:0000305};
DE Short=AtCCT2 {ECO:0000303|PubMed:12461134};
DE EC=2.7.7.15 {ECO:0000269|PubMed:12461134};
DE AltName: Full=CTP:phosphocholine cytidylyltransferase 2 {ECO:0000303|PubMed:19667100};
DE AltName: Full=Phosphorylcholine transferase 2 {ECO:0000303|PubMed:12461134};
GN Name=CCT2 {ECO:0000303|PubMed:12461134};
GN OrderedLocusNames=At4g15130 {ECO:0000312|Araport:AT4G15130};
GN ORFNames=dl3610w {ECO:0000312|EMBL:CAB45996.1},
GN FCAALL.209 {ECO:0000312|EMBL:CAB78555.1};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY COLD.
RC STRAIN=cv. Columbia;
RX PubMed=12461134; DOI=10.1093/pcp/pcf169;
RA Inatsugi R., Nakamura M., Nishida I.;
RT "Phosphatidylcholine biosynthesis at low temperature: differential
RT expression of CTP:phosphorylcholine cytidylyltransferase isogenes in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:1342-1350(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19667100; DOI=10.1093/pcp/pcp115;
RA Inatsugi R., Kawai H., Yamaoka Y., Yu Y., Sekiguchi A., Nakamura M.,
RA Nishida I.;
RT "Isozyme-specific modes of activation of CTP:phosphorylcholine
RT cytidylyltransferase in Arabidopsis thaliana at low temperature.";
RL Plant Cell Physiol. 50:1727-1735(2009).
CC -!- FUNCTION: Plays an important role in the biosynthesis of the
CC phospholipid phosphatidylcholine (PubMed:12461134, PubMed:19667100).
CC Catalyzes the formation of CDP-choline (PubMed:12461134,
CC PubMed:19667100). {ECO:0000269|PubMed:12461134,
CC ECO:0000269|PubMed:19667100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:12461134};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000269|PubMed:12461134};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:12461134};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000305}.
CC -!- INDUCTION: By cold treatment. {ECO:0000269|PubMed:12461134}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19667100}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45996.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78555.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB056715; BAC01276.1; -; Genomic_DNA.
DR EMBL; AB056716; BAC01277.1; -; mRNA.
DR EMBL; Z97338; CAB45996.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78555.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83559.1; -; Genomic_DNA.
DR PIR; B71415; B71415.
DR PIR; E85166; E85166.
DR RefSeq; NP_193249.5; NM_117602.9.
DR AlphaFoldDB; F4JJE0; -.
DR SMR; F4JJE0; -.
DR BioGRID; 12476; 2.
DR STRING; 3702.AT4G15130.1; -.
DR PaxDb; F4JJE0; -.
DR PRIDE; F4JJE0; -.
DR ProteomicsDB; 223938; -.
DR GeneID; 827179; -.
DR KEGG; ath:AT4G15130; -.
DR Araport; AT4G15130; -.
DR TAIR; locus:2129705; AT4G15130.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_916977_0_0_1; -.
DR InParanoid; F4JJE0; -.
DR OrthoDB; 1172502at2759; -.
DR UniPathway; UPA00753; UER00739.
DR PRO; PR:F4JJE0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJE0; baseline and differential.
DR Genevisible; F4JJE0; AT.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IMP:TAIR.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:TAIR.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..304
FT /note="Choline-phosphate cytidylyltransferase 2"
FT /id="PRO_0000423343"
FT REGION 266..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..36
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 66
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 112..113
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 117
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 142..146
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT CONFLICT 181
FT /note="E -> VK (in Ref. 1; BAC01276/BAC01277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34983 MW; 311D0B28182E4E39 CRC64;
MSVNGENKVS GGDSSSSDRP VRVYADGIFD LFHFGHARAI EQAKKSFPNT YLLVGCCNDE
ITNKFKGKTV MTESERYESL RHCKWVDEVI PDAPWVLTTE FLDKHKIDYV AHDALPYADT
SGAGNDVYEF VKSIGKFKET KRTEGISTSD IIMRIVKDYN QYVLRNLDRG YSREELGVSF
EEKRLRVNMR LKKLQEKVKE QQEKIQTVAK TAGMHHDEWL ENADRWVAGF LEMFEEGCHK
MGTAIRDGIQ QRLMRQESEE NRRLLQNGLT ISKDNDDEQM SDDNEFAEED CVNVSNKGIE
TVKK
