P49586 · PCY1A_MOUSE

  • Protein
    Choline-phosphate cytidylyltransferase A
  • Gene
    Pcyt1a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site84CTP (UniProtKB | ChEBI)
Binding site85CTP (UniProtKB | ChEBI)
Binding site92CTP (UniProtKB | ChEBI)
Binding site122CTP (UniProtKB | ChEBI)
Binding site122phosphocholine (UniProtKB | ChEBI)
Binding site151phosphocholine (UniProtKB | ChEBI)
Binding site168CTP (UniProtKB | ChEBI)
Binding site169CTP (UniProtKB | ChEBI)
Binding site173CTP (UniProtKB | ChEBI)
Binding site195CTP (UniProtKB | ChEBI)
Binding site196CTP (UniProtKB | ChEBI)
Binding site197CTP (UniProtKB | ChEBI)
Binding site200CTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentglycogen granule
Cellular Componentnuclear envelope
Cellular Componentnucleus
Molecular Functioncalmodulin binding
Molecular Functioncholine-phosphate cytidylyltransferase activity
Molecular Functionlipid binding
Molecular Functionmolecular function inhibitor activity
Molecular Functionphosphatidylcholine binding
Molecular Functionprotein homodimerization activity
Biological ProcessB cell proliferation
Biological ProcessCDP-choline pathway
Biological Processisotype switching
Biological Processphosphatidylcholine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Choline-phosphate cytidylyltransferase A
  • EC number
  • Alternative names
    • CCT-alpha
    • CTP:phosphocholine cytidylyltransferase A (CCT A; CT A)
    • Phosphorylcholine transferase A

Gene names

    • Name
      Pcyt1a
    • Synonyms
      Ctpct, Pcyt1

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • 129/J
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P49586
  • Secondary accessions
    • Q542W4

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Membrane
; Peripheral membrane protein
Endoplasmic reticulum membrane
; Peripheral membrane protein
Nucleus
Note: It can interconvert between an inactive cytosolic form and an active membrane-bound form.

Keywords

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).

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.

Go to variant viewer

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00002084541-367Choline-phosphate cytidylyltransferase A
Modified residue8N6-acetyllysine
Modified residue233Phosphoserine
Modified residue315Phosphoserine
Modified residue319Phosphoserine
Modified residue321Phosphoserine
Modified residue322Phosphoserine
Modified residue323Phosphoserine
Modified residue325Phosphothreonine
Modified residue329Phosphoserine
Modified residue331Phosphoserine
Modified residue333Phosphoserine
Modified residue342Phosphothreonine
Modified residue343Phosphoserine
Modified residue345Phosphoserine
Modified residue346Phosphoserine
Modified residue347Phosphoserine
Modified residue350Phosphoserine
Modified residue352Phosphoserine
Modified residue358Phosphothreonine
Modified residue362Phosphoserine

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

Proteomic databases

PTM databases

Expression

Tissue specificity

Brain and liver (at protein level) (PubMed:12842190).
Also found in heart, kidney, spleen, lung, skeletal muscle, ovary and testis (PubMed:12842190).

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, repeat.

TypeIDPosition(s)Description
Region1-32Disordered
Compositional bias7-22Basic and acidic residues
Region228-287Amphipathic
Region272-293Autoinhibitory (AI)
Region298-315Amphipathic
Region313-367Disordered
Compositional bias314-353Polar residues
Repeat319-3241
Region319-3483 X repeats
Repeat329-3332; approximate
Repeat343-3483

Sequence similarities

Belongs to the cytidylyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    367
  • Mass (Da)
    41,667
  • Last updated
    1996-02-01 v1
  • Checksum
    306B656D2EAAA2B3
MDAQSSAKVNSRKRRKEAPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKDAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCRAVTCDISEDEED

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
D3Z3T5D3Z3T5_MOUSEPcyt1a265

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias7-22Basic and acidic residues
Compositional bias314-353Polar residues
Sequence conflict360in Ref. 2; AAA53526

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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