Q99L43 · CDS2_MOUSE
- ProteinPhosphatidate cytidylyltransferase 2
- GeneCds2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids444 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (By similarity).
Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity).
Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540).
Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity).
Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H+ = a CDP-1,2-diacyl-sn-glycerol + diphosphateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H+ = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H+ = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H+ = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CTP + H+ = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H+ = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CTP + H+ = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H+ = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H+ = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphateThis reaction proceeds in the forward direction.
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | phosphatidate cytidylyltransferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | glycosylation | |
Biological Process | lipid droplet formation | |
Biological Process | phototransduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidate cytidylyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99L43
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 78-98 | Helical | ||||
Sequence: MIAFFFIIIYLGPMVLMMIVM | ||||||
Transmembrane | 129-149 | Helical | ||||
Sequence: WYFLLCVNYFFYGETVTDYFF | ||||||
Transmembrane | 165-185 | Helical | ||||
Sequence: HRFISFALYLTGFCMFVLSLV | ||||||
Transmembrane | 212-232 | Helical | ||||
Sequence: LVIHNLFEGMIWFIVPISCVI | ||||||
Transmembrane | 261-281 | Helical | ||||
Sequence: GFIGGFFATVVFGLLLSYVMS | ||||||
Transmembrane | 339-359 | Helical | ||||
Sequence: IALSTFASLIGPFGGFFASGF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090717 | 1-444 | Phosphatidate cytidylyltransferase 2 | |||
Sequence: MTELRQRVVREDAPPEDKESESEAKLDGETASDSESRAETAPLPTSVDDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFALYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSAIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLKSHLTDKGILTSALEDE | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 30 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 32 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 34 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 50 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Expressed in the ganglion cell layer and inner nuclear layer of the retina.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-34 | Basic and acidic residues | ||||
Sequence: MTELRQRVVREDAPPEDKESESEAKLDGETASDS | ||||||
Region | 1-48 | Disordered | ||||
Sequence: MTELRQRVVREDAPPEDKESESEAKLDGETASDSESRAETAPLPTSVD |
Sequence similarities
Belongs to the CDS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length444
- Mass (Da)51,314
- Last updated2001-06-01 v1
- Checksum6A3568A7E90A6C53
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-34 | Basic and acidic residues | ||||
Sequence: MTELRQRVVREDAPPEDKESESEAKLDGETASDS | ||||||
Sequence conflict | 43 | in Ref. 3; AAH69879 | ||||
Sequence: L → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY159802 EMBL· GenBank· DDBJ | AAO17790.1 EMBL· GenBank· DDBJ | mRNA | ||
AK036328 EMBL· GenBank· DDBJ | BAC29384.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147541 EMBL· GenBank· DDBJ | BAE27984.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166001 EMBL· GenBank· DDBJ | BAE38511.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003852 EMBL· GenBank· DDBJ | AAH03852.1 EMBL· GenBank· DDBJ | mRNA | ||
BC069879 EMBL· GenBank· DDBJ | AAH69879.1 EMBL· GenBank· DDBJ | mRNA |