P19836 · PCY1A_RAT
- ProteinCholine-phosphate cytidylyltransferase A
- GenePcyt1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids367 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
Miscellaneous
The cytidylyltransferase may interact with membranes through its amphipathic helix.
Catalytic activity
- CTP + H+ + phosphocholine = CDP-choline + diphosphateThis reaction proceeds in the forward direction.
Activity regulation
Interconverts between an inactive cytosolic form and an active membrane-bound form (PubMed:24275660).
Activation involves disruption of an inhibitory interaction between helices at the base of the active site and the autoinhibitory (AI) region (PubMed:24275660).
Activated by N-methylethanolamine (PubMed:8185307).
Activated by oleic acid-containing phosphatidylcholine vesicles (PubMed:8381041).
Activation involves disruption of an inhibitory interaction between helices at the base of the active site and the autoinhibitory (AI) region (PubMed:24275660).
Activated by N-methylethanolamine (PubMed:8185307).
Activated by oleic acid-containing phosphatidylcholine vesicles (PubMed:8381041).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.41 μM | CTP | |||||
0.47 μM | phosphocholine |
Pathway
Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 84 | CTP (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 85 | CTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 92 | CTP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 122 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 122 | phosphocholine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 151 | phosphocholine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 168 | CTP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 169 | CTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 173 | CTP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 195 | CTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 196 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 197 | CTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 200 | CTP (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | extrinsic component of membrane | |
Cellular Component | glycogen granule | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleus | |
Molecular Function | calmodulin binding | |
Molecular Function | choline-phosphate cytidylyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | lipid binding | |
Molecular Function | molecular function inhibitor activity | |
Molecular Function | phosphatidylcholine binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | B cell proliferation | |
Biological Process | CDP-choline pathway | |
Biological Process | isotype switching | |
Biological Process | phosphatidylcholine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameCholine-phosphate cytidylyltransferase A
- 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 > Rattus
Accessions
- Primary accessionP19836
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Endoplasmic reticulum membrane ; Peripheral membrane protein
Note: It can interconvert between an inactive cytosolic form and an active membrane-bound form.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 122 | Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 500-fold. | ||||
Sequence: K → A | ||||||
Mutagenesis | 122 | Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 80-fold. | ||||
Sequence: K → R | ||||||
Mutagenesis | 168 | Strongly reduced catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 173 | Reduced catalytic activity. Reduces affinity for phosphocholine. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 362 | No loss of enzyme activity and nuclear localization. | ||||
Sequence: S → A or C |
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000208455 | 1-367 | Choline-phosphate cytidylyltransferase A | |||
Sequence: MDAQSSAKVNSRKRRKEVPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCKAVTCDISEDEED | ||||||
Modified residue | 8 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 233 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 315 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Modified residue | 319 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 321 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 322 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 323 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 325 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 329 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 331 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 333 | Phosphoserine; by PKC | ||||
Sequence: S | ||||||
Modified residue | 342 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 343 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 347 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 350 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 352 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 358 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 362 | Phosphoserine; by CK2 | ||||
Sequence: S |
Post-translational modification
The serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation.
The N-terminus is blocked.
Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MDAQSSAKVNSRKRRKEVPGPNGATEEDGIP | ||||||
Compositional bias | 7-22 | Basic and acidic residues | ||||
Sequence: AKVNSRKRRKEVPGPN | ||||||
Region | 228-287 | Amphipathic | ||||
Sequence: KELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIG | ||||||
Region | 272-293 | Autoinhibitory (AI) | ||||
Sequence: IDLIQKWEEKSREFIGSFLEMF | ||||||
Region | 298-315 | Amphipathic | ||||
Sequence: ALKHMLKEGKGRMLQAIS | ||||||
Region | 313-367 | Disordered | ||||
Sequence: AISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCKAVTCDISEDEED | ||||||
Compositional bias | 314-353 | Polar residues | ||||
Sequence: ISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSR | ||||||
Repeat | 319-324 | 1 | ||||
Sequence: SPSSSP | ||||||
Region | 319-348 | 3 X repeats | ||||
Sequence: SPSSSPTHERSPSPSFRWPFSGKTSPSSSP | ||||||
Repeat | 329-333 | 2; approximate | ||||
Sequence: SPSPS | ||||||
Repeat | 343-348 | 3 | ||||
Sequence: SPSSSP |
Sequence similarities
Belongs to the cytidylyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)41,681
- Last updated1996-02-01 v2
- Checksum44DFFFC0F1608969
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-22 | Basic and acidic residues | ||||
Sequence: AKVNSRKRRKEVPGPN | ||||||
Sequence conflict | 91 | in Ref. 1; AAA40995 | ||||
Sequence: G → S | ||||||
Sequence conflict | 114 | in Ref. 1; AAA40995 | ||||
Sequence: S → C | ||||||
Sequence conflict | 116-117 | in Ref. 2; AAB60489 | ||||
Sequence: EL → DV | ||||||
Compositional bias | 314-353 | Polar residues | ||||
Sequence: ISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M36071 EMBL· GenBank· DDBJ | AAA40995.1 EMBL· GenBank· DDBJ | mRNA | ||
U03490 EMBL· GenBank· DDBJ | AAB60489.1 EMBL· GenBank· DDBJ | mRNA | ||
L13245 EMBL· GenBank· DDBJ | AAB59683.1 EMBL· GenBank· DDBJ | mRNA | ||
BC085713 EMBL· GenBank· DDBJ | AAH85713.1 EMBL· GenBank· DDBJ | mRNA |