UniProt functional annotation for P19836



	UniProt functional annotation for P19836

UniProt code: P19836.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. {ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652, ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816, ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.

Catalytic activity: Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate; Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975; EC=2.7.7.15; Evidence={ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652, ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816, ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998; Evidence={ECO:0000305|PubMed:19783652};

Activity regulation: By phosphorylation. Activated by N- methylethanolamine (PubMed:8185307). Activated by oleic acid-containing phosphatidylcholine vesicles (PubMed:8381041). {ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.

Biophysicochemical properties: Kinetic parameters: KM=0.41 uM for CTP {ECO:0000269|PubMed:8185307}; KM=0.47 uM for phosphocholine {ECO:0000269|PubMed:8185307};

Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000269|PubMed:12718547, ECO:0000269|PubMed:19783652, ECO:0000269|PubMed:2166941, ECO:0000269|PubMed:639816, ECO:0000269|PubMed:8185307, ECO:0000269|PubMed:8381041}.

Subunit: Homodimer. {ECO:0000269|PubMed:19783652}.

Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:639816}. Membrane {ECO:0000269|PubMed:639816}; Peripheral membrane protein {ECO:0000269|PubMed:639816}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P49585}. Nucleus {ECO:0000269|PubMed:8185307}. Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form.

Ptm: 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. {ECO:0000269|PubMed:8144639}.

Ptm: The N-terminus is blocked. {ECO:0000269|PubMed:2166941}.

Ptm: Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P49586}.

Miscellaneous: The cytidylyltransferase may interact with membranes through its amphipathic helix.

Similarity: Belongs to the cytidylyltransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. {ECO:0000269\|PubMed:12718547, ECO:0000269\|PubMed:19783652, ECO:0000269\|PubMed:2166941, ECO:0000269\|PubMed:639816, ECO:0000269\|PubMed:8185307, ECO:0000269\|PubMed:8381041}.


Catalytic activity:		Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate; Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975; EC=2.7.7.15; Evidence={ECO:0000269\|PubMed:12718547, ECO:0000269\|PubMed:19783652, ECO:0000269\|PubMed:2166941, ECO:0000269\|PubMed:639816, ECO:0000269\|PubMed:8185307, ECO:0000269\|PubMed:8381041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998; Evidence={ECO:0000305\|PubMed:19783652};
Activity regulation:		By phosphorylation. Activated by N- methylethanolamine (PubMed:8185307). Activated by oleic acid-containing phosphatidylcholine vesicles (PubMed:8381041). {ECO:0000269\|PubMed:8185307, ECO:0000269\|PubMed:8381041}.
Biophysicochemical properties:		Kinetic parameters: KM=0.41 uM for CTP {ECO:0000269\|PubMed:8185307}; KM=0.47 uM for phosphocholine {ECO:0000269\|PubMed:8185307};
Pathway:		Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000269\|PubMed:12718547, ECO:0000269\|PubMed:19783652, ECO:0000269\|PubMed:2166941, ECO:0000269\|PubMed:639816, ECO:0000269\|PubMed:8185307, ECO:0000269\|PubMed:8381041}.
Subunit:		Homodimer. {ECO:0000269\|PubMed:19783652}.
Subcellular location:		Cytoplasm, cytosol {ECO:0000269\|PubMed:639816}. Membrane {ECO:0000269\|PubMed:639816}; Peripheral membrane protein {ECO:0000269\|PubMed:639816}. Endoplasmic reticulum {ECO:0000250\|UniProtKB:P49585}. Nucleus {ECO:0000269\|PubMed:8185307}. Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form.
Ptm:		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. {ECO:0000269\|PubMed:8144639}.
Ptm:		The N-terminus is blocked. {ECO:0000269\|PubMed:2166941}.
Ptm:		Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. {ECO:0000250\|UniProtKB:P49586}.
Miscellaneous:		The cytidylyltransferase may interact with membranes through its amphipathic helix.
Similarity:		Belongs to the cytidylyltransferase family. {ECO:0000305}.