Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221CTPCombined sources1 Publication
Binding sitei122 – 1221SubstrateCombined sources1 Publication
Binding sitei151 – 1511SubstrateCombined sources1 Publication
Binding sitei173 – 1731CTPCombined sources1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi84 – 929CTPCombined sources1 Publication
Nucleotide bindingi168 – 1692CTPCombined sources1 Publication
Nucleotide bindingi196 – 2005CTPCombined sources1 Publication

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221K → A: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 500-fold. 1 Publication
Mutagenesisi122 – 1221K → R: Nearly abolishes enzyme activity. Decreases affinity for phosphocholine about 80-fold. 1 Publication
Mutagenesisi168 – 1681H → A: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi173 – 1731Y → A: Reduced catalytic activity. Reduces affinity for phosphocholine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Choline-phosphate cytidylyltransferase APRO_0000208455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei315 – 3151Phosphoserine; by PKC1 Publication
Modified residuei319 – 3191PhosphoserineCombined sources1 Publication
Modified residuei321 – 3211Phosphoserine1 Publication
Modified residuei322 – 3221Phosphoserine1 Publication
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei325 – 3251PhosphothreonineBy similarity
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei331 – 3311PhosphoserineCombined sources1 Publication
Modified residuei333 – 3331Phosphoserine; by PKC1 Publication
Modified residuei342 – 3421PhosphothreonineCombined sources
Modified residuei343 – 3431Phosphoserine1 Publication
Modified residuei345 – 3451Phosphoserine1 Publication
Modified residuei346 – 3461Phosphoserine1 Publication
Modified residuei347 – 3471PhosphoserineCombined sources1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei358 – 3581PhosphothreonineBy similarity
Modified residuei362 – 3621Phosphoserine; by CK2Combined sources1 Publication

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.
PhosphoSiteiP19836.

Expressioni

Gene expression databases

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

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503Combined sources
Beta strandi55 – 573Combined sources
Helixi64 – 696Combined sources
Beta strandi73 – 753Combined sources
Beta strandi77 – 837Combined sources
Helixi90 – 10011Combined sources
Beta strandi102 – 11211Combined sources
Helixi115 – 1217Combined sources
Helixi129 – 1379Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1486Combined sources
Helixi155 – 1606Combined sources
Beta strandi165 – 1717Combined sources
Helixi183 – 1875Combined sources
Beta strandi191 – 1944Combined sources
Helixi202 – 21413Combined sources
Turni238 – 2403Combined sources
Beta strandi243 – 2453Combined sources
Helixi248 – 2525Combined sources
Helixi255 – 2573Combined sources
Turni258 – 2603Combined sources
Helixi261 – 2677Combined sources
Helixi270 – 2745Combined sources
Helixi276 – 29116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 236-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati319 – 32461
Repeati329 – 33352; approximate
Repeati343 – 34863

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni228 – 28760AmphipathicSequence analysisAdd
BLAST
Regioni256 – 288333 X 11 AA approximate tandem repeatsAdd
BLAST
Regioni298 – 31518AmphipathicSequence analysisAdd
BLAST
Regioni319 – 348303 X repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2804. Eukaryota.
COG0615. LUCA.
GeneTreeiENSGT00390000000269.
HOGENOMiHOG000230945.
HOVERGENiHBG053531.
InParanoidiP19836.
KOiK00968.
OMAiSKMPRCA.
OrthoDBiEOG7X9G6S.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911G → S in AAA40995 (PubMed:2166941).Curated
Sequence conflicti114 – 1141S → C in AAA40995 (PubMed:2166941).Curated
Sequence conflicti116 – 1172EL → DV in AAB60489 (Ref. 2) Curated

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_006248444.2.
XP_008766916.1. XM_008768694.1.
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_006248444.2.
XP_008766916.1. XM_008768694.1.
UniGeneiRn.81192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 236-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002403.

Chemistry

SwissLipidsiSLP:000001188.

PTM databases

iPTMnetiP19836.
PhosphoSiteiP19836.

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.
OrthoDBiEOG7X9G6S.
PhylomeDBiP19836.
TreeFamiTF106336.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP19836.
NextBioi620489.
PROiP19836.

Gene expression databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: an amphipathic protein that controls phosphatidylcholine synthesis."
    Kalmar G.B., Kay R.J., Lachance A., Aebersold R., Cornell R.B.
    Proc. Natl. Acad. Sci. U.S.A. 87:6029-6033(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Hogan M., Zimmermann L.J., Wang J., Kuliszewski M., Liu J., Buch S., Post M.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Lung.
  3. "Baculovirus-mediated expression of rat liver CTP:phosphocholine cytidylyltransferase."
    Macdonald J.I.S., Kent C.
    Protein Expr. Purif. 4:1-7(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "Immunological studies on CTP:phosphocholine cytidylyltransferase from the livers of normal and choline-deficient rats."
    Choy P.C., Schneider W.J., Vance D.E.
    Eur. J. Biochem. 85:189-193(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Identification of phosphorylation sites in rat liver CTP: phosphocholine cytidylyltransferase."
    McDonald J.I.S., Kent C.
    J. Biol. Chem. 269:10529-10537(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-315; SER-319; SER-321; SER-322; SER-323; SER-329; SER-331; SER-333; SER-343; SER-345; SER-346; SER-347; SER-350; SER-352 AND SER-362.
    Tissue: Liver.
  7. "Identification of lysine 122 and arginine 196 as important functional residues of rat CTP:phosphocholine cytidylyltransferase alpha."
    Helmink B.A., Braker J.D., Kent C., Friesen J.A.
    Biochemistry 42:5043-5051(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-122.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-331; THR-342; SER-347 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase."
    Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., Tracey A.S.
    Biochemistry 35:11975-11984(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 236-268.
    Tissue: Liver.
  10. "Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold."
    Lee J., Johnson J., Ding Z., Paetzel M., Cornell R.B.
    J. Biol. Chem. 284:33535-33548(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-236 IN COMPLEX WITH CDP-CHOLINE, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-168 AND TYR-173, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

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: March 16, 2016
This is version 143 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.