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Protein

Choline-phosphate cytidylyltransferase A

Gene

Pcyt1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls phosphatidylcholine synthesis.

Catalytic activityi

CTP + phosphocholine = diphosphate + CDP-choline.2 Publications

Enzyme regulationi

By phosphorylation.

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylcholine from phosphocholine.2 Publications
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Choline-phosphate cytidylyltransferase A (Pcyt1a), Choline-phosphate cytidylyltransferase B (Pcyt1b)
  2. Choline/ethanolaminephosphotransferase 1 (Cept1), Cholinephosphotransferase 1 (Chpt1)
This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylcholine from phosphocholine, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei122CTPCombined sources1 Publication1
Binding sitei122SubstrateCombined sources1 Publication1
Binding sitei151SubstrateCombined sources1 Publication1
Binding sitei173CTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 92CTPCombined sources1 Publication9
Nucleotide bindingi168 – 169CTPCombined sources1 Publication2
Nucleotide bindingi196 – 200CTPCombined sources1 Publication5

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • choline-phosphate cytidylyltransferase activity Source: UniProtKB
  • lipid binding Source: RGD
  • phosphatidylcholine binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • CDP-choline pathway Source: UniProtKB
  • phosphatidylcholine biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.7.7.15. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.
UniPathwayiUPA00753; UER00739.

Chemistry databases

SwissLipidsiSLP:000001188.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline-phosphate cytidylyltransferase A (EC:2.7.7.152 Publications)
Alternative name(s):
CCT-alpha
CTP:phosphocholine cytidylyltransferase A
Short name:
CCT A
Short name:
CT A
Phosphorylcholine transferase A
Gene namesi
Name:Pcyt1a
Synonyms:Ctpct, Pcyt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi70515. Pcyt1a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: RGD
  • endoplasmic reticulum membrane Source: Ensembl
  • extrinsic component of membrane Source: RGD
  • glycogen granule Source: Ensembl
  • nuclear envelope Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi122K → A: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 500-fold. 1 Publication1
Mutagenesisi122K → R: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 80-fold. 1 Publication1
Mutagenesisi168H → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi173Y → A: Reduced catalytic activity. Reduces affinity for phosphocholine. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084551 – 367Choline-phosphate cytidylyltransferase AAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei8N6-acetyllysineBy similarity1
Modified residuei233PhosphoserineBy similarity1
Modified residuei315Phosphoserine; by PKC1 Publication1
Modified residuei319PhosphoserineCombined sources1 Publication1
Modified residuei321Phosphoserine1 Publication1
Modified residuei322Phosphoserine1 Publication1
Modified residuei323Phosphoserine1 Publication1
Modified residuei325PhosphothreonineBy similarity1
Modified residuei329Phosphoserine1 Publication1
Modified residuei331PhosphoserineCombined sources1 Publication1
Modified residuei333Phosphoserine; by PKC1 Publication1
Modified residuei342PhosphothreonineCombined sources1
Modified residuei343Phosphoserine1 Publication1
Modified residuei345Phosphoserine1 Publication1
Modified residuei346Phosphoserine1 Publication1
Modified residuei347PhosphoserineCombined sources1 Publication1
Modified residuei350Phosphoserine1 Publication1
Modified residuei352Phosphoserine1 Publication1
Modified residuei358PhosphothreonineBy similarity1
Modified residuei362Phosphoserine; by CK2Combined sources1 Publication1

Post-translational modificationi

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.1 Publication
The N-terminus is blocked.
Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19836.
PRIDEiP19836.

PTM databases

iPTMnetiP19836.
PhosphoSitePlusiP19836.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001762.
GenevisibleiP19836. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002403.

Structurei

Secondary structure

1367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi48 – 50Combined sources3
Beta strandi55 – 57Combined sources3
Helixi64 – 69Combined sources6
Beta strandi73 – 75Combined sources3
Beta strandi77 – 83Combined sources7
Helixi90 – 100Combined sources11
Beta strandi102 – 112Combined sources11
Helixi115 – 121Combined sources7
Helixi129 – 137Combined sources9
Beta strandi139 – 141Combined sources3
Beta strandi143 – 148Combined sources6
Helixi155 – 160Combined sources6
Beta strandi165 – 171Combined sources7
Helixi183 – 187Combined sources5
Beta strandi191 – 194Combined sources4
Helixi202 – 214Combined sources13
Turni238 – 240Combined sources3
Beta strandi243 – 245Combined sources3
Helixi248 – 252Combined sources5
Helixi255 – 257Combined sources3
Turni258 – 260Combined sources3
Helixi261 – 267Combined sources7
Helixi270 – 274Combined sources5
Helixi276 – 291Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PEHNMR-A236-268[»]
1PEINMR-A267-288[»]
3HL4X-ray2.20A/B1-236[»]
4MVCX-ray3.00A/B1-312[»]
4MVDX-ray8.00A/B/C/D/E/F/G/H1-312[»]
ProteinModelPortaliP19836.
SMRiP19836.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati319 – 32416
Repeati329 – 3332; approximate5
Repeati343 – 34836

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni228 – 287AmphipathicSequence analysisAdd BLAST60
Regioni256 – 2883 X 11 AA approximate tandem repeatsAdd BLAST33
Regioni298 – 315AmphipathicSequence analysisAdd BLAST18
Regioni319 – 3483 X repeatsAdd BLAST30

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2804. Eukaryota.
COG0615. LUCA.
GeneTreeiENSGT00390000000269.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiP19836.
KOiK00968.
OMAiSKMPRCA.
OrthoDBiEOG091G0DDW.
PhylomeDBiP19836.
TreeFamiTF106336.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

P19836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAQSSAKVN SRKRRKEVPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE
60 70 80 90 100
IEVDFSKPYV RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK
110 120 130 140 150
NLFPNTYLIV GVCSDELTHN FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP
160 170 180 190 200
WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD VYKHIKEAGM FAPTQRTEGI
210 220 230 240 250
STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY HLQERVDKVK
260 270 280 290 300
KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
310 320 330 340 350
HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS
360
LSRCKAVTCD ISEDEED
Length:367
Mass (Da):41,681
Last modified:February 1, 1996 - v2
Checksum:i44DFFFC0F1608969
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91G → S in AAA40995 (PubMed:2166941).Curated1
Sequence conflicti114S → C in AAA40995 (PubMed:2166941).Curated1
Sequence conflicti116 – 117EL → DV in AAB60489 (Ref. 2) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36071 mRNA. Translation: AAA40995.1.
U03490 mRNA. Translation: AAB60489.1.
L13245 mRNA. Translation: AAB59683.1.
BC085713 mRNA. Translation: AAH85713.1.
PIRiA36001.
RefSeqiNP_511177.2. NM_078622.2.
XP_006248506.1. XM_006248444.3.
XP_008766916.1. XM_008768694.2.
UniGeneiRn.81192.

Genome annotation databases

EnsembliENSRNOT00000002403; ENSRNOP00000002403; ENSRNOG00000001762.
GeneIDi140544.
KEGGirno:140544.
UCSCiRGD:70515. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36071 mRNA. Translation: AAA40995.1.
U03490 mRNA. Translation: AAB60489.1.
L13245 mRNA. Translation: AAB59683.1.
BC085713 mRNA. Translation: AAH85713.1.
PIRiA36001.
RefSeqiNP_511177.2. NM_078622.2.
XP_006248506.1. XM_006248444.3.
XP_008766916.1. XM_008768694.2.
UniGeneiRn.81192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PEHNMR-A236-268[»]
1PEINMR-A267-288[»]
3HL4X-ray2.20A/B1-236[»]
4MVCX-ray3.00A/B1-312[»]
4MVDX-ray8.00A/B/C/D/E/F/G/H1-312[»]
ProteinModelPortaliP19836.
SMRiP19836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002403.

Chemistry databases

SwissLipidsiSLP:000001188.

PTM databases

iPTMnetiP19836.
PhosphoSitePlusiP19836.

Proteomic databases

PaxDbiP19836.
PRIDEiP19836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002403; ENSRNOP00000002403; ENSRNOG00000001762.
GeneIDi140544.
KEGGirno:140544.
UCSCiRGD:70515. rat.

Organism-specific databases

CTDi5130.
RGDi70515. Pcyt1a.

Phylogenomic databases

eggNOGiKOG2804. Eukaryota.
COG0615. LUCA.
GeneTreeiENSGT00390000000269.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiP19836.
KOiK00968.
OMAiSKMPRCA.
OrthoDBiEOG091G0DDW.
PhylomeDBiP19836.
TreeFamiTF106336.

Enzyme and pathway databases

UniPathwayiUPA00753; UER00739.
BRENDAi2.7.7.15. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.

Miscellaneous databases

EvolutionaryTraceiP19836.
PROiP19836.

Gene expression databases

BgeeiENSRNOG00000001762.
GenevisibleiP19836. RN.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPCY1A_RAT
AccessioniPrimary (citable) accession number: P19836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The cytidylyltransferase may interact with membranes through its amphipathic helix.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.