CDS2_BOVIN
ID CDS2_BOVIN Reviewed; 445 AA.
AC A0JNC1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphatidate cytidylyltransferase 2 {ECO:0000305};
DE EC=2.7.7.41 {ECO:0000250|UniProtKB:O95674};
DE AltName: Full=CDP-DAG synthase 2;
DE AltName: Full=CDP-DG synthase 2;
DE AltName: Full=CDP-diacylglycerol synthase 2;
DE Short=CDS 2;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 2;
DE AltName: Full=CDP-diglyceride synthase 2;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 2;
GN Name=CDS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-
CC diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of
CC phosphatidylglycerol, cardiolipin and phosphatidylinositol (By
CC similarity). Exhibits specificity for the nature of the acyl chains at
CC the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl
CC chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By
CC similarity). Plays an important role in regulating the growth and
CC maturation of lipid droplets which are storage organelles at the center
CC of lipid and energy homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:O95674}.
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:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45648, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77091, ChEBI:CHEBI:85349;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45660, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77098, ChEBI:CHEBI:85352;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + CTP + H(+) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45652, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:72864, ChEBI:CHEBI:85350;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate
CC + CTP + H(+) = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45656,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:77126, ChEBI:CHEBI:85351;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC CTP + H(+) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45664,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:85353;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'-
CC diphosphate + diphosphate; Xref=Rhea:RHEA:45668, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77130,
CC ChEBI:CHEBI:85354; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP +
CC H(+) = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-
CC diphosphate + diphosphate; Xref=Rhea:RHEA:45672, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77128,
CC ChEBI:CHEBI:85355; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) =
CC 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate +
CC diphosphate; Xref=Rhea:RHEA:45676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85356; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q91XU8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95674}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; BC126607; AAI26608.1; -; mRNA.
DR RefSeq; NP_001071514.1; NM_001078046.1.
DR AlphaFoldDB; A0JNC1; -.
DR STRING; 9913.ENSBTAP00000007970; -.
DR PaxDb; A0JNC1; -.
DR PRIDE; A0JNC1; -.
DR Ensembl; ENSBTAT00000007970; ENSBTAP00000007970; ENSBTAG00000006066.
DR GeneID; 614834; -.
DR KEGG; bta:614834; -.
DR CTD; 8760; -.
DR VEuPathDB; HostDB:ENSBTAG00000006066; -.
DR VGNC; VGNC:27156; CDS2.
DR eggNOG; KOG1440; Eukaryota.
DR GeneTree; ENSGT00940000158877; -.
DR HOGENOM; CLU_023471_0_1_1; -.
DR InParanoid; A0JNC1; -.
DR OMA; REVAIMP; -.
DR OrthoDB; 1072976at2759; -.
DR TreeFam; TF313464; -.
DR Reactome; R-BTA-1483148; Synthesis of PG.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006066; Expressed in neutrophil and 106 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..445
FT /note="Phosphatidate cytidylyltransferase 2"
FT /id="PRO_0000304876"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99L43"
SQ SEQUENCE 445 AA; 51357 MW; 788FC1B80D41902E CRC64;
MTELRQRVAR EPEAPPEDKE SESEAKADGE TASDSESRVE AVTQPPSADD TPEVLNRALS
NLSSRWKNWW VRGILTLAMI AFFFIIIYLG PMVLMMIVMC VQIKCFHEII TIGYNVYHSY
DLPWFRTLSW YFLLCVNYFF YGETVTDYFF TLVQREEPLR ILSKYHRFIS FTLYLTGFCM
FVLSLVKKHY RLQFYMFGWT HVTLLIVVTQ SHLVIHNLFE GMIWFIVPIS CVICNDIMAY
MFGFFFGRTP LIKLSPKKTW EGFIGGFFAT VVFGLLLSYV MSGYRCFVCP VEYNNDTNSF
TVDCEPSGLF RLQEYNIPGV IQSIIGWKTV RMYPFQIHSI ALSTFASLIG PFGGFFASGF
KRAFKIKDFA NTIPGHGGIM DRFDCQYLMA TFVNVYIASF IRGPNPSKLV QQFLTLRPDQ
QLHIFNTLKS HLTDKGMLTA ATEDK
