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CDS4_ARATH
ID   CDS4_ARATH              Reviewed;         391 AA.
AC   Q94A03; F4IW27; F4IW28; Q0V7V3;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Phosphatidate cytidylyltransferase 4, chloroplastic {ECO:0000303|PubMed:20442275};
DE            EC=2.7.7.41 {ECO:0000269|PubMed:20442275};
DE   AltName: Full=CDP-DAG synthase 4;
DE   AltName: Full=CDP-DG synthase 4;
DE   AltName: Full=CDP-diacylglycerol synthase 4;
DE            Short=CDS4;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase 4;
DE   AltName: Full=CDP-diglyceride synthase 4;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase 4;
DE   Flags: Precursor;
GN   Name=CDS4 {ECO:0000303|PubMed:20442275};
GN   OrderedLocusNames=At2g45150 {ECO:0000312|Araport:AT2G45150};
GN   ORFNames=T14P1.4;
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:AAK92713.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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] (ISOFORM 1).
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] (ISOFORM 4).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, COFACTOR, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION,
RP   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. Promotes the
CC       biosynthesis of plastidial phosphatidylglycerol (PG) which is required
CC       for structure and function of thylakoid membranes and, hence, for
CC       photoautotrophic growth. {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:0000269|PubMed:20442275};
CC       Note=Requires a divalent cation for activity. Displays highest
CC       activities with MgCl(2). {ECO:0000269|PubMed:20442275};
CC   -!- ACTIVITY REGULATION: Highest activities is obtained at about 30 mM CTP
CC       and 2 mM phosphatidic acid (PA). {ECO:0000269|PubMed:20442275}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:20442275};
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: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:20442275}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q94A03-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94A03-2; Sequence=VSP_057443;
CC       Name=3;
CC         IsoId=Q94A03-3; Sequence=VSP_057443, VSP_057445, VSP_057446;
CC       Name=4;
CC         IsoId=Q94A03-4; Sequence=VSP_057444;
CC   -!- DISRUPTION PHENOTYPE: When associated with the disruption of CDS5,
CC       requires sucrose (Suc) treatment to grow. Pale yellow-green leaves with
CC       reduced chlorophyll levels but an increased chlorophyll a/b ratio.
CC       Reduced plastidial phosphatidylglycerol (PG) biosynthesis leading to
CC       abnormal thylakoid membrane development. {ECO:0000269|PubMed:20442275}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation.
CC       {ECO:0000312|EMBL:AEC10515.1}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Produced by a combination of alternative
CC       splicing and alternative initiation. {ECO:0000312|EMBL:AEC10516.1}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC       {ECO:0000312|EMBL:AEC10517.1}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; CP002685; AEC10515.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10516.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10517.1; -; Genomic_DNA.
DR   EMBL; AY050778; AAK92713.1; -; mRNA.
DR   EMBL; AK316876; BAH19584.1; -; mRNA.
DR   EMBL; BT026467; ABH04574.1; -; mRNA.
DR   EMBL; BX822071; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_566035.2; NM_130078.4. [Q94A03-2]
DR   RefSeq; NP_973691.2; NM_201962.2. [Q94A03-3]
DR   RefSeq; NP_973692.1; NM_201963.2. [Q94A03-4]
DR   AlphaFoldDB; Q94A03; -.
DR   SMR; Q94A03; -.
DR   STRING; 3702.AT2G45150.1; -.
DR   PaxDb; Q94A03; -.
DR   PRIDE; Q94A03; -.
DR   ProteomicsDB; 223972; -. [Q94A03-1]
DR   EnsemblPlants; AT2G45150.1; AT2G45150.1; AT2G45150. [Q94A03-2]
DR   EnsemblPlants; AT2G45150.2; AT2G45150.2; AT2G45150. [Q94A03-3]
DR   EnsemblPlants; AT2G45150.3; AT2G45150.3; AT2G45150. [Q94A03-4]
DR   GeneID; 819123; -.
DR   Gramene; AT2G45150.1; AT2G45150.1; AT2G45150. [Q94A03-2]
DR   Gramene; AT2G45150.2; AT2G45150.2; AT2G45150. [Q94A03-3]
DR   Gramene; AT2G45150.3; AT2G45150.3; AT2G45150. [Q94A03-4]
DR   KEGG; ath:AT2G45150; -.
DR   Araport; AT2G45150; -.
DR   TAIR; locus:2055627; AT2G45150.
DR   eggNOG; KOG1440; Eukaryota.
DR   OMA; HGITEGM; -.
DR   OrthoDB; 1072976at2759; -.
DR   PhylomeDB; Q94A03; -.
DR   BRENDA; 2.7.7.41; 399.
DR   UniPathway; UPA00557; UER00614.
DR   PRO; PR:Q94A03; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q94A03; baseline and differential.
DR   Genevisible; Q94A03; AT.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IMP:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IMP:TAIR.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB.
DR   InterPro; IPR000374; PC_trans.
DR   PROSITE; PS01315; CDS; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; Chloroplast;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Plastid; Reference proteome; Transferase; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..391
FT                   /note="Phosphatidate cytidylyltransferase 4, chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431833"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MTNTNTLFLRHDDDSEILIFQENSVFPLFVFASWGIWRAM (in
FT                   isoform 2 and isoform 3)"
FT                   /id="VSP_057443"
FT   VAR_SEQ         77..85
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_057444"
FT   VAR_SEQ         279..287
FT                   /note="TFGRTPLTS -> VTPRMIPHR (in isoform 3)"
FT                   /id="VSP_057445"
FT   VAR_SEQ         288..391
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_057446"
SQ   SEQUENCE   391 AA;  42159 MW;  3591EB189A89BF03 CRC64;
     MATFAELVLS TSRCTCPCRS FTRKPLIRPP LSGLRLPGDT KPLFRSGLGR ISVSRRFLTA
     VARAESDQLG DDDHSKGIDR IHNLQNVEDK QKKASQLKKR VIFGIGIGLP VGCVVLAGGW
     VFTVALASSV FIGSREYFEL VRSRGIAKGM TPPPRYVSRV CSVICALMPI LTLYFGNIDI
     LVTSAAFVVA IALLVQRGSP RFAQLSSTMF GLFYCGYLPS FWVKLRCGLA APALNTGIGR
     TWPILLGGQA HWTVGLVATL ISFSGVIATD TFAFLGGKTF GRTPLTSISP KKTWEGTIVG
     LVGCIAITIL LSKYLSWPQS LFSSVAFGFL NFFGSVFGDL TESMIKRDAG VKDSGSLIPG
     HGGILDRVDS YIFTGALAYS FIKTSLKLYG V
 
 
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