CDS2_ARATH
ID CDS2_ARATH Reviewed; 423 AA.
AC O49639;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphatidate cytidylyltransferase 2 {ECO:0000303|PubMed:20442275};
DE EC=2.7.7.41 {ECO:0000269|PubMed:20442275};
DE AltName: Full=CDP-DAG synthase 2;
DE AltName: Full=CDP-DG synthase 2;
DE AltName: Full=CDP-diacylglycerol synthase 2;
DE Short=CDS2;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 2;
DE AltName: Full=CDP-diglyceride synthase 2;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 2;
GN Name=CDS2 {ECO:0000303|PubMed:20442275};
GN OrderedLocusNames=At4g22340 {ECO:0000312|Araport:AT4G22340};
GN ORFNames=T10I14.170 {ECO:0000312|EMBL:CAA16784.1};
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|Proteomes:UP000006548};
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=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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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}.
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DR EMBL; AL021712; CAA16784.1; -; Genomic_DNA.
DR EMBL; AL161557; CAB79189.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84595.1; -; Genomic_DNA.
DR EMBL; AY065310; AAL38786.1; -; mRNA.
DR EMBL; AY091315; AAM14254.1; -; mRNA.
DR EMBL; AY084570; AAM61136.1; -; mRNA.
DR PIR; G85255; G85255.
DR PIR; T04915; T04915.
DR RefSeq; NP_193965.1; NM_118360.3.
DR AlphaFoldDB; O49639; -.
DR STRING; 3702.AT4G22340.3; -.
DR iPTMnet; O49639; -.
DR PaxDb; O49639; -.
DR PRIDE; O49639; -.
DR ProteomicsDB; 220466; -.
DR EnsemblPlants; AT4G22340.1; AT4G22340.1; AT4G22340.
DR GeneID; 828329; -.
DR Gramene; AT4G22340.1; AT4G22340.1; AT4G22340.
DR KEGG; ath:AT4G22340; -.
DR Araport; AT4G22340; -.
DR eggNOG; KOG1440; Eukaryota.
DR BRENDA; 2.7.7.41; 399.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:O49639; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49639; baseline and differential.
DR Genevisible; O49639; 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; IEA:UniProtKB-EC.
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 Acetylation; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..423
FT /note="Phosphatidate cytidylyltransferase 2"
FT /id="PRO_0000431831"
FT TRANSMEM 60..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O04928"
SQ SEQUENCE 423 AA; 48247 MW; 02776A12440FA407 CRC64;
MQKEIAGDAP SAPTTRVRHR KRNSDVGAGA GKPNGNHLLV NDSKKYKSFL IRAYSTFWMI
GGFALIVYLG HLYITAMVVV IQIFMARELF NLLRKTHEDK QLPGFRLLNW HFFFTAMLFV
YGRILSQRLV NTVTPDKVLY RLVTSLIKYH MAICYSLYIS GFVWFILTLK KKMYKYQFSQ
YAWTHMILIV VFTQSSFTVA NIFEGIFWFL LPASLIVIND IFAYICGFFF GRTPLIKLSP
KKTWEGFIGA SITTVISAFL LANIMGRFLW LTCPREDLST GWLLCDPGPL FKQETHALPG
WISDWLPWKE ISILPVQWHA LCLGLFASII APFGGFFASG FKRAFKIKDF GDSIPGHGGI
TDRMDCQMVM AVFAYIYHQS FVVPEVLSVD KLLDQIITSL TLEEQQALLV KLGQMLQEKV
IGS
