CDS3_ARATH
ID CDS3_ARATH Reviewed; 471 AA.
AC Q1PE48; A0MF99; Q9SZ17;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Phosphatidate cytidylyltransferase 3 {ECO:0000303|PubMed:20442275};
DE EC=2.7.7.41 {ECO:0000269|PubMed:20442275};
DE AltName: Full=CDP-DAG synthase 3;
DE AltName: Full=CDP-DG synthase 3;
DE AltName: Full=CDP-diacylglycerol synthase 3;
DE Short=CDS3;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 3;
DE AltName: Full=CDP-diglyceride synthase 3;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 3;
GN Name=CDS3 {ECO:0000303|PubMed:20442275};
GN OrderedLocusNames=At4g26770 {ECO:0000312|Araport:AT4G26770};
GN ORFNames=F10M23.110 {ECO:0000312|EMBL:CAB36523.1};
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 {ECO:0000312|EMBL:ABE66091.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20442275; DOI=10.1104/pp.110.156422;
RA Haselier A., Akbari H., Weth A., Baumgartner W., Frentzen M.;
RT "Two closely related genes of Arabidopsis encode plastidial
RT cytidinediphosphate diacylglycerol synthases essential for photoautotrophic
RT growth.";
RL Plant Physiol. 153:1372-1384(2010).
CC -!- FUNCTION: May be involved in the synthesis of minor phospholipids and
CC in modulation of IP3-mediated signal transduction.
CC {ECO:0000269|PubMed:20442275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000269|PubMed:20442275};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q94A03};
CC Note=Requires a divalent cation for activity.
CC {ECO:0000250|UniProtKB:Q94A03};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000269|PubMed:20442275}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28650.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB36523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035440; CAB36523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85250.1; -; Genomic_DNA.
DR EMBL; DQ446870; ABE66091.1; -; mRNA.
DR EMBL; DQ653225; ABK28650.1; ALT_SEQ; mRNA.
DR PIR; T04800; T04800.
DR RefSeq; NP_194407.5; NM_118811.7.
DR AlphaFoldDB; Q1PE48; -.
DR SMR; Q1PE48; -.
DR IntAct; Q1PE48; 34.
DR STRING; 3702.AT4G26770.1; -.
DR iPTMnet; Q1PE48; -.
DR PaxDb; Q1PE48; -.
DR PRIDE; Q1PE48; -.
DR ProteomicsDB; 224389; -.
DR EnsemblPlants; AT4G26770.1; AT4G26770.1; AT4G26770.
DR GeneID; 828784; -.
DR Gramene; AT4G26770.1; AT4G26770.1; AT4G26770.
DR KEGG; ath:AT4G26770; -.
DR Araport; AT4G26770; -.
DR TAIR; locus:2116272; AT4G26770.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_2_0_1; -.
DR InParanoid; Q1PE48; -.
DR OMA; REVAIMP; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; Q1PE48; -.
DR BRENDA; 2.7.7.41; 399.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:Q1PE48; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q1PE48; baseline and differential.
DR Genevisible; Q1PE48; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IMP:TAIR.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PTHR13773; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..471
FT /note="Phosphatidate cytidylyltransferase 3"
FT /id="PRO_0000431832"
FT TRANSMEM 97..116
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..139
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 325
FT /note="L -> F (in Ref. 1; CAB36523/CAB79532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 54924 MW; FE217D1D047CB807 CRC64;
MAMEKDLSPN SPRIRKLRDT SYPTTPTSRM NTNNQRDNHY PNIPNSPRDY NYTPSSPTAR
IRHRRRSSEN LAEVNRSNVS RVSNLLLGDK NKYRSMWIRT CSSLWMLGGV VFIIYMGHLY
IWAMVVVIQI FMAKELFFLR RRAHEERRLP GFWLLNWHFF FTAMLFVYGR IIQQQLVNTV
SSDRFIYKLV SGLIKYQMVI CYFLYIAGLI WFILTLKNKM YKYQFGQYAW THMILIVVFT
QSSFTVANIF EGIFWFLLPA ALIAMNDVAA YFFGFYFGKT PLIKLSPKKT WEGFIGASVA
TIISAFIFAN VLGQFQWLTC PRKDLSTGWL HCDPGPLFRP EYYPFPSWIT PFSPWKGIST
LPVQWHAFSL GLFASIMAPF GGFFASGFKR AFKIKDFGDS IPGHGGFTDR MDCQMVMAVF
AYIYIQSFIV NRDYSVEMIL DQISRSLGHE EQKMLYEKLG DILQHKLQGR F
