(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 93.
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};
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   IntAct; Q1PE48; 34.
DR   STRING; 3702.AT4G26770.1; -.
DR   iPTMnet; Q1PE48; -.
DR   PaxDb; Q1PE48; -.
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   eggNOG; COG0575; LUCA.
DR   HOGENOM; HOG000209582; -.
DR   InParanoid; Q1PE48; -.
DR   KO; K00981; -.
DR   OMA; QVDCEPS; -.
DR   OrthoDB; 1072976at2759; -.
DR   PhylomeDB; Q1PE48; -.
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;
DR   PRODOM; Q1PE48.
DR   SWISS-2DPAGE; Q1PE48.
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   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
//

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