P49586 · PCY1A_MOUSE
- 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.
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. Activation involves disruption of an inhibitory interaction between helices at the base of the active site and the autoinhibitory (AI) region.
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 | glycogen granule | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleus | |
Molecular Function | calmodulin binding | |
Molecular Function | choline-phosphate cytidylyltransferase activity | |
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
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 > Mus > Mus
Accessions
- Primary accessionP49586
- Secondary accessions
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
Disruption phenotype
Early embryonic lethality: zygotes do not form blastocysts, do not develop past 3.5 days post coitum (dpc), and fail to implant (PubMed:15798219).
Mice with a conditional deletion in B-cells show defects in B-cell proliferation and class switch recombination (PubMed:19139091).
Mice with a conditional deletion in B-cells show defects in B-cell proliferation and class switch recombination (PubMed:19139091).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000208454 | 1-367 | Choline-phosphate cytidylyltransferase A | |||
Sequence: MDAQSSAKVNSRKRRKEAPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCRAVTCDISEDEED | ||||||
Modified residue | 8 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 233 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 315 | Phosphoserine | ||||
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 | ||||
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 | ||||
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 (By similarity).
Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MDAQSSAKVNSRKRRKEAPGPNGATEEDGIPS | ||||||
Compositional bias | 7-22 | Basic and acidic residues | ||||
Sequence: AKVNSRKRRKEAPGPN | ||||||
Region | 228-287 | Amphipathic | ||||
Sequence: KELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIG | ||||||
Region | 272-293 | Autoinhibitory (AI) | ||||
Sequence: IDLIQKWEEKSREFIGSFLEMF | ||||||
Region | 298-315 | Amphipathic | ||||
Sequence: ALKHMLKEGKGRMLQAIS | ||||||
Region | 313-367 | Disordered | ||||
Sequence: AISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCRAVTCDISEDEED | ||||||
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)41,667
- Last updated1996-02-01 v1
- Checksum306B656D2EAAA2B3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3Z3T5 | D3Z3T5_MOUSE | Pcyt1a | 265 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-22 | Basic and acidic residues | ||||
Sequence: AKVNSRKRRKEAPGPN | ||||||
Compositional bias | 314-353 | Polar residues | ||||
Sequence: ISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSR | ||||||
Sequence conflict | 360 | in Ref. 2; AAA53526 | ||||
Sequence: D → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z12302 EMBL· GenBank· DDBJ | CAA78172.1 EMBL· GenBank· DDBJ | mRNA | ||
L28956 EMBL· GenBank· DDBJ | AAA53526.1 EMBL· GenBank· DDBJ | mRNA | ||
U84207 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84200 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84201 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84202 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84203 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84204 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84205 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U84206 EMBL· GenBank· DDBJ | AAB63446.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK076050 EMBL· GenBank· DDBJ | BAC36148.1 EMBL· GenBank· DDBJ | mRNA | ||
AK076830 EMBL· GenBank· DDBJ | BAC36497.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018313 EMBL· GenBank· DDBJ | AAH18313.1 EMBL· GenBank· DDBJ | mRNA |