View source for Choline-phosphate cytidylyltransferase A (Rattus norvegicus)

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{{#invoke:InfoboxforTarget|run|CCT-alpha, CCT-A, PCYT1A|[https://www.uniprot.org/uniprot/P19836 P19836]|Rattus norvegicus|Cys37|[http://pfam.xfam.org/family/PF01467 Cytidylyltransferase-like family]|[[:Category:Choline-phosphate cytidylyltransferase A (Rattus norvegicus)|Ligand list]]|Metabolic enzyme}}
==Summary==

===Protein Function ===
Choline-phosphate cytidylyltransferase (EC 2.7.7.15) is an enzyme that catalyzes the chemical reaction:<br/>
CTP + choline phosphate ↔ diphosphate + CDP-choline<br/>
It is responsible for regulating phosphatidylcholine content in membranes.<br/>
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism. (From Wikipedia)<br/>
The main pathway for Phosphatidylcholine (PtdCho) biosynthesis in mammalian cells is the Kennedy or CDP-choline pathway, which is regulated by the activity of CCT. CCT activity is essential for cell survival as inhibition of CCT activity leading to decreased PtdCho synthesis impairs cell proliferation, induces apoptosiss, and reduces pulmonary surfactant biosynthesis. (PMID: 18614529)
<br/>

===Cys Function & Property===
CCT-alpha exists as an inactive soluble form and a membrane-associated active form. Both soluble and membrane-bound forms are present in cells as a noncovalently associated dimer comprised of a 42-kDa monomer. A pair of Cys37 residues, located within the aminoterminal domain, are thought to be within disulfide bond distance in the soluble form of the enzyme, but after binding activatinglipids, these  Cys37 residues shift slightly with increased separation in the lipid-bound dimer. (PMID: 18614529) <br/>

* Hydrophobic property:
:[[File:518-hydro.png||600px]]
* SASA：
:Cys37: Unknown A^2<br/>

==Protein Sequence==
<font face="Courier">
MDAQSSAKVN SRKRRKEVPG PNGATEEDGI PSKVQR<span style="background:#ffff00">'''C'''</span>AVG LRQPAPFSDE <br/>
IEVDFSKPYV RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK <br/>
NLFPNTYLIV GVCSDELTHN FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP <br/>
WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD VYKHIKEAGM FAPTQRTEGI <br/>
STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY HLQERVDKVK <br/>
KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK <br/>
HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS <br/>
LSRCKAVTCD ISEDEED                                            <br/> 
</font>

==Structural Information==
*Known structure with covalent ligand: <br/>
:Unknown<br/> 

*Protein structure:
:Unknown<br/>

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00440 Phosphonate and phosphinate metabolism] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko00564 Glycerophospholipid metabolism] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko01100 Metabolic pathways] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko05231 Choline metabolism in cancer] <br/>
	
==Experimental Evidence==
:Homologous Analysis of Sequence, Enzymatic Assay  

==Reference==
# Weinhold P A, Rounsifer M E, Feldman D A. '''The purification and characterization of CTP: phosphorylcholine cytidylyltransferase from rat liver[J].''' Journal of Biological Chemistry, 1986, 261(11): 5104-5110. [https://www.ncbi.nlm.nih.gov/pubmed/?term=3007491 3007491]<br/>

[[Category:Targets|Targets]]
[[Category:Rattus norvegicus|Rattus norvegicus]]
[[Category:Metabolic enzyme|Metabolic enzyme]]
[[Category:Cytidylyltransferase family|Cytidylyltransferase family]]
[[Category:Phosphonate and phosphinate metabolism|Phosphonate and phosphinate metabolism]]
[[Category:Glycerophospholipid metabolism|Glycerophospholipid metabolism]]
[[Category:Metabolic pathways|Metabolic pathways]]
[[Category:Choline metabolism in cancer|Choline metabolism in cancer]]