P19836
Gene name |
Pcyt1a (Ctpct, Pcyt1) |
Protein name |
Choline-phosphate cytidylyltransferase A |
Names |
EC 2.7.7.15 , CCT-alpha , CTP:phosphocholine cytidylyltransferase A , CCT A , CT A , Phosphorylcholine transferase A |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:140544 |
EC number |
2.7.7.15: Nucleotidyltransferases |
Protein Class |
CYTIDYLYLTRANSFERASE (PTHR10739) |
Descriptions
Phosphocholine cytidylyltransferase (CCT) interconverts between an inactive soluble and active membrane-bound form in response to changes in membrane lipid composition. Activation involves disruption of an inhibitory interaction between the alphaE helices at the base of the active site and an autoinhibitory (AI) segment in the regulatory M domain and membrane insertion of the M domain as an amphipathic helix.
Autoinhibitory domains (AIDs)
Target domain |
202-223 (alphaE helices within the catalytic domain) |
Relief mechanism |
Others |
Assay |
Deletion assay, Mutagenesis experiment, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
No variants for P19836
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P19836 | |||||
No associated diseases with P19836
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.15 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR10739 | CYTIDYLYLTRANSFERASE |
| PANTHER Subfamily | PTHR10739:SF19 | CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE A |
| PANTHER Protein Class |
transferase
metabolite interconversion enzyme |
|
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| extrinsic component of membrane | The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
| glycogen granule | Cytoplasmic bead-like structures of animal cells, visible by electron microscope. Each granule is a functional unit with the biosynthesis and catabolism of glycogen being catalyzed by enzymes bound to the granule surface. |
| nuclear envelope | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| choline-phosphate cytidylyltransferase activity | Catalysis of the reaction |
| identical protein binding | Binding to an identical protein or proteins. |
| lipid binding | Binding to a lipid. |
| molecular function inhibitor activity | A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target. |
| phosphatidylcholine binding | Binding to a phosphatidylcholine, a glycophospholipid in which a phosphatidyl group is esterified to the hydroxyl group of choline. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| CDP-choline pathway | The phosphatidylcholine biosynthetic process that begins with the phosphorylation of choline and ends with the combination of CDP-choline with diacylglycerol to form phosphatidylcholine. |
| phosphatidylcholine biosynthetic process | The chemical reactions and pathways resulting in the formation of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9Y5K3 | PCYT1B | Choline-phosphate cytidylyltransferase B | Homo sapiens (Human) | PR |
| P49585 | PCYT1A | Choline-phosphate cytidylyltransferase A | Homo sapiens (Human) | SS |
| Q811Q9 | Pcyt1b | Choline-phosphate cytidylyltransferase B | Mus musculus (Mouse) | SS |
| P49586 | Pcyt1a | Choline-phosphate cytidylyltransferase A | Mus musculus (Mouse) | SS |
| Q9QZC4 | Pcyt1b | Choline-phosphate cytidylyltransferase B | Rattus norvegicus (Rat) | PR |
| F4JJE0 | CCT2 | Choline-phosphate cytidylyltransferase 2 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDAQSSAKVN | SRKRRKEVPG | PNGATEEDGI | PSKVQRCAVG | LRQPAPFSDE | IEVDFSKPYV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RVTMEEACRG | TPCERPVRVY | ADGIFDLFHS | GHARALMQAK | NLFPNTYLIV | GVCSDELTHN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FKGFTVMNEN | ERYDAVQHCR | YVDEVVRNAP | WTLTPEFLAE | HRIDFVAHDD | IPYSSAGSDD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VYKHIKEAGM | FAPTQRTEGI | STSDIITRIV | RDYDVYARRN | LQRGYTAKEL | NVSFINEKKY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HLQERVDKVK | KKVKDVEEKS | KEFVQKVEEK | SIDLIQKWEE | KSREFIGSFL | EMFGPEGALK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HMLKEGKGRM | LQAISPKQSP | SSSPTHERSP | SPSFRWPFSG | KTSPSSSPAS | LSRCKAVTCD |
| ISEDEED |