CDS1_ARATH
ID CDS1_ARATH Reviewed; 421 AA.
AC O04928; O48808;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphatidate cytidylyltransferase 1 {ECO:0000303|PubMed:9085581};
DE EC=2.7.7.41 {ECO:0000269|PubMed:20442275};
DE AltName: Full=CDP-DAG synthase 1;
DE AltName: Full=CDP-DG synthase 1;
DE AltName: Full=CDP-diacylglycerol synthase 1;
DE Short=CDS1;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 1;
DE AltName: Full=CDP-diglyceride synthase 1;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 1;
GN Name=CDS1 {ECO:0000303|PubMed:9085581};
GN OrderedLocusNames=At1g62430 {ECO:0000312|Araport:AT1G62430};
GN ORFNames=F24O1.17 {ECO:0000312|EMBL:AAF70845.1};
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 [MRNA].
RC STRAIN=cv. C24; TISSUE=Flower, and Silique;
RX PubMed=9085581; DOI=10.1104/pp.113.3.997;
RA Kopka J., Ludewig M., Mueller-Roeber B.;
RT "Complementary DNAs encoding eukaryotic-type cytidine-5'-diphosphate-
RT diacylglycerol synthases of two plant species.";
RL Plant Physiol. 113:997-1002(1997).
RN [2]
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 [3]
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 [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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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; X94306; CAA63969.1; -; mRNA.
DR EMBL; AC003113; AAF70845.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33967.1; -; Genomic_DNA.
DR PIR; T01455; T01455.
DR RefSeq; NP_176433.2; NM_104923.4.
DR AlphaFoldDB; O04928; -.
DR SMR; O04928; -.
DR STRING; 3702.AT1G62430.1; -.
DR iPTMnet; O04928; -.
DR PaxDb; O04928; -.
DR PRIDE; O04928; -.
DR ProteomicsDB; 223977; -.
DR EnsemblPlants; AT1G62430.1; AT1G62430.1; AT1G62430.
DR GeneID; 842541; -.
DR Gramene; AT1G62430.1; AT1G62430.1; AT1G62430.
DR KEGG; ath:AT1G62430; -.
DR Araport; AT1G62430; -.
DR TAIR; locus:2027144; AT1G62430.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_2_0_1; -.
DR InParanoid; O04928; -.
DR OMA; VFTAAPW; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; O04928; -.
DR BioCyc; MetaCyc:AT1G62430-MON; -.
DR BRENDA; 2.7.7.41; 399.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:O04928; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04928; baseline and differential.
DR Genevisible; O04928; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:TAIR.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0080186; P:developmental vegetative growth; IGI:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; TAS:TAIR.
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..421
FT /note="Phosphatidate cytidylyltransferase 1"
FT /id="PRO_0000090723"
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 206..226
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 421 AA; 48660 MW; 96D238DB4B913AA3 CRC64;
MEEENVTSSP STPVHRLRHR RRSNEVVTDG DKVNASPLLV NDRNKYKSFM VRTYSTLWMI
GGFVLVVYMG HLYITAMVVV IQIFMAKELF NLLRKAPEDK CLPYIKQLNW HFFFTAMLFV
YGRILSQRLA NTMTADQFFY RLVSGLIKYH MAICYLLYII GFMWFILTLK KKMYKYQFGQ
YAWTHMILIV VFTQSSFTVA NIFEGIFWFL LPASLIIIND IFAYIFGFFF GRTPLIKLSP
KKTWEGFIGA SVTTIISAFV LANILGRFPW LTCPRQDLST GWLQCDADPL FKPEPFALPA
WIPEWFPWKE MTILPVQWHA LCLGLFASII APFGGFFASG FKRAFKIKDF GDSIPGHGGI
TDRMDCQMVM AVFAYIYLQS FIVSQSVSVD KILDQILTNL TFEEQQALFV KLGQMLKDKL
S
