P49586

SS
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
Mus musculus (Mouse)
KEGG Pathway
mmu:13026
EC number
2.7.7.15: Nucleotidyltransferases
Protein Class

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)

275-295 (autoinhibitory segment in the M domain) SS

Target domain

202-223 (alphaE helices within the catalytic domain)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P49586

Entry ID Method Resolution Chain Position Source
AF-P49586-F1 Predicted AlphaFoldDB

10 variants for P49586

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389410948 51 I>V No EVA
rs3389414943 138 H>N No EVA
rs3552263524 162 R>W No EVA
rs3389379306 170 D>N No EVA
rs3389402136 204 D>G No EVA
rs3389393055 308 G>S No EVA
rs3389379234 314 I>T No EVA
rs3389393094 342 T>I No EVA
rs3389419403 353 R>S No EVA
rs3406804246 366 E>K No EVA

No associated diseases with P49586

2 regional properties for P49586

Type Name Position InterPro Accession
domain Cytidyltransferase-like domain 78 - 208 IPR004821
domain CTP:phosphocholine cytidylyltransferase domain 75 - 224 IPR041723

Functions

Description
EC Number 2.7.7.15 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm, cytosol
  • Membrane ; Peripheral membrane protein
  • Endoplasmic reticulum
  • Nucleus
  • It can interconvert between an inactive cytosolic form and an active membrane-bound form
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 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.
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.

6 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
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
Q9QZC4 Pcyt1b Choline-phosphate cytidylyltransferase B Rattus norvegicus (Rat) PR
P19836 Pcyt1a Choline-phosphate cytidylyltransferase A Rattus norvegicus (Rat) EV
F4JJE0 CCT2 Choline-phosphate cytidylyltransferase 2 Arabidopsis thaliana (Mouse-ear cress) SS
10 20 30 40 50 60
MDAQSSAKVN SRKRRKEAPG 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
VYKHIKDAGM 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 LSRCRAVTCD
ISEDEED