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CDS1_SOLTU
ID   CDS1_SOLTU              Reviewed;         424 AA.
AC   O04940;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Phosphatidate cytidylyltransferase 1 {ECO:0000303|PubMed:9085581};
DE            EC=2.7.7.41 {ECO:0000269|PubMed:9085581};
DE   AltName: Full=CDP-DAG synthase;
DE   AltName: Full=CDP-DG synthase;
DE   AltName: Full=CDP-diacylglycerol synthase;
DE            Short=CDS;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase;
DE   AltName: Full=CDP-diglyceride synthase;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN   Name=CDS1 {ECO:0000303|PubMed:9085581};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
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).
CC   -!- FUNCTION: May be involved in the synthesis of minor phospholipids and
CC       in modulation of IP3-mediated signal transduction.
CC       {ECO:0000269|PubMed:9085581}.
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:9085581};
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:9085581}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Roots and sink leaves.
CC       {ECO:0000269|PubMed:9085581}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; X91909; CAA63004.1; -; mRNA.
DR   PIR; T07366; T07366.
DR   RefSeq; NP_001275147.1; NM_001288218.1.
DR   AlphaFoldDB; O04940; -.
DR   EnsemblPlants; RHC03H1G0115.2.1; RHC03H1G0115.2.1; RHC03H1G0115.2.
DR   GeneID; 102597765; -.
DR   Gramene; RHC03H1G0115.2.1; RHC03H1G0115.2.1; RHC03H1G0115.2.
DR   KEGG; sot:102597765; -.
DR   InParanoid; O04940; -.
DR   OrthoDB; 1072976at2759; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
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   Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..424
FT                   /note="Phosphatidate cytidylyltransferase 1"
FT                   /id="PRO_0000090724"
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..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  49178 MW;  43B556B12F082638 CRC64;
     MHNDSNSGAP GTPSGRIRRR RGSNEVPPEV VKANGNHLLV NDRSKYKSML IRAYSSVWMI
     GGFAFIIYMG HLYIWAMVVV IQIFMAKELF NLLRRAHEDR HLPGFRLLNW HFFFTAMLFV
     YGRMLSQRLV NTVTLDKFLY KLVGRFVKYH MVTCYFFYIA GFMWFILTLK KKMYKYQFSQ
     YAWTHMILIV VFTQSAFTVA NIFEGIFWFL LPASLIVIND IAAYFFGFFF GRTPLIKLSP
     KKTWEGFIGA SITTIISAFL LANMFGRFQW LTCPRKDLST GWLDCDPGPL FKPEYFTLPE
     WFPAWFLSRE IAVLPVQWHA LLLGLFASII APFGGFFASG FKRAFKIKDF GDSIPGHGGM
     TDRMDCQMVM AVFAYIYHQS FIVPQNLSIE MILDQIILNL TFEEQLAVYK KLGQIIQERT
     FGES
 
 
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