PCY1A_HUMAN
ID PCY1A_HUMAN Reviewed; 367 AA.
AC P49585; A9LYK9; D3DXB1; Q86Y88;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Choline-phosphate cytidylyltransferase A;
DE EC=2.7.7.15 {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:7918629};
DE AltName: Full=CCT-alpha;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase A;
DE Short=CCT A;
DE Short=CT A;
DE AltName: Full=Phosphorylcholine transferase A;
GN Name=PCYT1A; Synonyms=CTPCT, PCYT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=7918629; DOI=10.1016/0167-4781(94)90056-6;
RA Kalmar G.B., Kay R.J., Lachance A.C., Cornell R.B.;
RT "Primary structure and expression of a human CTP:phosphocholine
RT cytidylyltransferase.";
RL Biochim. Biophys. Acta 1219:328-334(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CIRCULAR DICHROISM, ACTIVITY REGULATION, AND REGION.
RX PubMed=8155650; DOI=10.1021/bi00180a029;
RA Johnson J.E., Cornell R.B.;
RT "Membrane-binding amphipathic alpha-helical peptide derived from
RT CTP:phosphocholine cytidylyltransferase.";
RL Biochemistry 33:4327-4335(1994).
RN [6]
RP CIRCULAR DICHROISM, AND STRUCTURE BY NMR OF 236-268 AND 267-288.
RX PubMed=8810902; DOI=10.1021/bi960821+;
RA Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., Tracey A.S.;
RT "Structure of the membrane binding domain of CTP:phosphocholine
RT cytidylyltransferase.";
RL Biochemistry 35:11975-11984(1996).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10480912; DOI=10.1074/jbc.274.38.26992;
RA Lykidis A., Baburina I., Jackowski S.;
RT "Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms.
RT Identification of a new CCTbeta splice variant.";
RL J. Biol. Chem. 274:26992-27001(1999).
RN [8]
RP IN VITRO INTERCHAIN DISULFIDE BOND, AND MUTAGENESIS OF CYS-37.
RX PubMed=15069071; DOI=10.1074/jbc.m403311200;
RA Xie M., Smith J.L., Ding Z., Zhang D., Cornell R.B.;
RT "Membrane binding modulates the quaternary structure of CTP:phosphocholine
RT cytidylyltransferase.";
RL J. Biol. Chem. 279:28817-28825(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-347; SER-352 AND
RP SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-343;
RP SER-347 AND SER-362, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-315; SER-319;
RP SER-331; THR-342; SER-343 AND SER-347, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-347 AND SER-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP VARIANTS SMDCRD THR-99; VAL-99; LYS-129; ALA-150; LEU-191 AND SER-223.
RX PubMed=24387990; DOI=10.1016/j.ajhg.2013.11.018;
RA Hoover-Fong J., Sobreira N., Jurgens J., Modaff P., Blout C., Moser A.,
RA Kim O.H., Cho T.J., Cho S.Y., Kim S.J., Jin D.K., Kitoh H., Park W.Y.,
RA Ling H., Hetrick K.N., Doheny K.F., Valle D., Pauli R.M.;
RT "Mutations in PCYT1A, encoding a key regulator of phosphatidylcholine
RT metabolism, cause spondylometaphyseal dysplasia with cone-rod dystrophy.";
RL Am. J. Hum. Genet. 94:105-112(2014).
RN [22]
RP VARIANT SMDCRD LYS-129.
RX PubMed=24387991; DOI=10.1016/j.ajhg.2013.11.022;
RA Yamamoto G.L., Baratela W.A., Almeida T.F., Lazar M., Afonso C.L.,
RA Oyamada M.K., Suzuki L., Oliveira L.A., Ramos E.S., Kim C.A.,
RA Passos-Bueno M.R., Bertola D.R.;
RT "Mutations in PCYT1A cause spondylometaphyseal dysplasia with cone-rod
RT dystrophy.";
RL Am. J. Hum. Genet. 94:113-119(2014).
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:7918629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:10480912,
CC ECO:0000269|PubMed:7918629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000305|PubMed:10480912};
CC -!- ACTIVITY REGULATION: By phosphorylation (By similarity). Activated by
CC anionic lipid vesicles and by oleic acid or diacylglycerol-containing
CC phosphatidylcholine vesicles (PubMed:7918629,PubMed:8155650).
CC {ECO:0000250, ECO:0000269|PubMed:7918629, ECO:0000269|PubMed:8155650}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:7918629}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
CC -!- INTERACTION:
CC P49585; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2563309, EBI-11522760;
CC P49585; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2563309, EBI-3918971;
CC P49585; P13807: GYS1; NbExp=3; IntAct=EBI-2563309, EBI-740553;
CC P49585; P43357: MAGEA3; NbExp=3; IntAct=EBI-2563309, EBI-5651459;
CC P49585; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-2563309, EBI-748229;
CC P49585; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-2563309, EBI-9679267;
CC P49585; P49585: PCYT1A; NbExp=5; IntAct=EBI-2563309, EBI-2563309;
CC P49585; Q9Y5K3-3: PCYT1B; NbExp=6; IntAct=EBI-2563309, EBI-12280028;
CC P49585; O76064: RNF8; NbExp=3; IntAct=EBI-2563309, EBI-373337;
CC P49585; O15126: SCAMP1; NbExp=3; IntAct=EBI-2563309, EBI-954338;
CC P49585; O00560: SDCBP; NbExp=3; IntAct=EBI-2563309, EBI-727004;
CC P49585; O95295: SNAPIN; NbExp=3; IntAct=EBI-2563309, EBI-296723;
CC P49585; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-2563309, EBI-1044859;
CC P49585; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-2563309, EBI-11337915;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P19836}. Membrane
CC {ECO:0000250|UniProtKB:P19836}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19836}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:10480912}. Nucleus {ECO:0000269|PubMed:10480912}.
CC Note=It can interconvert between an inactive cytosolic form and an
CC active membrane-bound form. {ECO:0000250|UniProtKB:P19836}.
CC -!- TISSUE SPECIFICITY: Brain, placenta, liver, fetal and adult lung.
CC {ECO:0000269|PubMed:10480912}.
CC -!- PTM: The serine residues of the C-terminus are phosphorylated. The
CC inactive soluble form is stabilized by phosphorylation, the active
CC membrane bound form is promoted by anionic lipids or diacylglycerol,
CC and is stabilized by dephosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:P19836}.
CC -!- PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to
CC proteasomal degradation. {ECO:0000250|UniProtKB:P49586}.
CC -!- DISEASE: Spondylometaphyseal dysplasia with cone-rod dystrophy (SMDCRD)
CC [MIM:608940]: A disorder characterized by postnatal growth deficiency
CC resulting in profound short stature, rhizomelia with bowing of the
CC lower extremities, platyspondyly with anterior vertebral protrusions,
CC progressive metaphyseal irregularity and cupping with shortened tubular
CC bones, and early-onset progressive visual impairment associated with a
CC pigmentary maculopathy and electroretinographic evidence of cone-rod
CC dysfunction. {ECO:0000269|PubMed:24387990,
CC ECO:0000269|PubMed:24387991}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pcyt1a/";
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DR EMBL; L28957; AAA72127.1; -; mRNA.
DR EMBL; EU280320; ABX44666.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53655.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53662.1; -; Genomic_DNA.
DR EMBL; BC046355; AAH46355.1; -; mRNA.
DR CCDS; CCDS3315.1; -.
DR PIR; S50145; S50145.
DR RefSeq; NP_001299602.1; NM_001312673.1.
DR RefSeq; NP_005008.2; NM_005017.3.
DR AlphaFoldDB; P49585; -.
DR SMR; P49585; -.
DR BioGRID; 111157; 65.
DR IntAct; P49585; 31.
DR MINT; P49585; -.
DR STRING; 9606.ENSP00000292823; -.
DR ChEMBL; CHEMBL4105855; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB00709; Lamivudine.
DR GlyGen; P49585; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49585; -.
DR MetOSite; P49585; -.
DR PhosphoSitePlus; P49585; -.
DR BioMuta; PCYT1A; -.
DR DMDM; 166214967; -.
DR EPD; P49585; -.
DR jPOST; P49585; -.
DR MassIVE; P49585; -.
DR MaxQB; P49585; -.
DR PaxDb; P49585; -.
DR PeptideAtlas; P49585; -.
DR PRIDE; P49585; -.
DR ProteomicsDB; 56021; -.
DR Antibodypedia; 33936; 235 antibodies from 30 providers.
DR DNASU; 5130; -.
DR Ensembl; ENST00000292823.6; ENSP00000292823.2; ENSG00000161217.12.
DR Ensembl; ENST00000431016.6; ENSP00000394617.1; ENSG00000161217.12.
DR GeneID; 5130; -.
DR KEGG; hsa:5130; -.
DR MANE-Select; ENST00000431016.6; ENSP00000394617.1; NM_001312673.2; NP_001299602.1.
DR UCSC; uc003fwf.2; human.
DR CTD; 5130; -.
DR DisGeNET; 5130; -.
DR GeneCards; PCYT1A; -.
DR HGNC; HGNC:8754; PCYT1A.
DR HPA; ENSG00000161217; Low tissue specificity.
DR MalaCards; PCYT1A; -.
DR MIM; 123695; gene.
DR MIM; 608940; phenotype.
DR neXtProt; NX_P49585; -.
DR OpenTargets; ENSG00000161217; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 85167; Spondylometaphyseal dysplasia-cone-rod dystrophy syndrome.
DR PharmGKB; PA33099; -.
DR VEuPathDB; HostDB:ENSG00000161217; -.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000157384; -.
DR HOGENOM; CLU_034585_4_2_1; -.
DR InParanoid; P49585; -.
DR OMA; RWPFSAK; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; P49585; -.
DR TreeFam; TF106336; -.
DR BioCyc; MetaCyc:HS08577-MON; -.
DR BRENDA; 2.7.7.15; 2681.
DR PathwayCommons; P49585; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR SignaLink; P49585; -.
DR SIGNOR; P49585; -.
DR UniPathway; UPA00753; UER00739.
DR BioGRID-ORCS; 5130; 453 hits in 1094 CRISPR screens.
DR ChiTaRS; PCYT1A; human.
DR GeneWiki; PCYT1A; -.
DR GenomeRNAi; 5130; -.
DR Pharos; P49585; Tchem.
DR PRO; PR:P49585; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P49585; protein.
DR Bgee; ENSG00000161217; Expressed in sural nerve and 186 other tissues.
DR ExpressionAtlas; P49585; baseline and differential.
DR Genevisible; P49585; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0042587; C:glycogen granule; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cone-rod dystrophy; Cytoplasm; Disease variant; Dwarfism;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Nucleus; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation.
FT CHAIN 1..367
FT /note="Choline-phosphate cytidylyltransferase A"
FT /id="PRO_0000208453"
FT REPEAT 319..324
FT /note="1"
FT REPEAT 329..333
FT /note="2; approximate"
FT REPEAT 343..348
FT /note="3"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..287
FT /note="Amphipathic"
FT /evidence="ECO:0000255"
FT REGION 256..288
FT /note="3 X 11 AA approximate tandem repeats; mediates
FT binding and activation by anionic lipid vesicles"
FT /evidence="ECO:0000269|PubMed:8155650"
FT REGION 313..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="3 X repeats"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84..92
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 168..169
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 196..200
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49586"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VARIANT 99
FT /note="A -> T (in SMDCRD; dbSNP:rs587777191)"
FT /evidence="ECO:0000269|PubMed:24387990"
FT /id="VAR_071083"
FT VARIANT 99
FT /note="A -> V (in SMDCRD; dbSNP:rs587777189)"
FT /evidence="ECO:0000269|PubMed:24387990"
FT /id="VAR_071084"
FT VARIANT 129
FT /note="E -> K (in SMDCRD; dbSNP:rs587777194)"
FT /evidence="ECO:0000269|PubMed:24387990,
FT ECO:0000269|PubMed:24387991"
FT /id="VAR_071085"
FT VARIANT 150
FT /note="P -> A (in SMDCRD; dbSNP:rs587777190)"
FT /evidence="ECO:0000269|PubMed:24387990"
FT /id="VAR_071086"
FT VARIANT 191
FT /note="F -> L (in SMDCRD; dbSNP:rs587777195)"
FT /evidence="ECO:0000269|PubMed:24387990"
FT /id="VAR_071087"
FT VARIANT 223
FT /note="R -> S (in SMDCRD; dbSNP:rs540053239)"
FT /evidence="ECO:0000269|PubMed:24387990"
FT /id="VAR_071088"
FT MUTAGEN 37
FT /note="C->S: Abolishes formation of the interchain
FT disulfide that can be observed when the enzyme is treated
FT with copper phenanthrolene (in vitro)."
FT /evidence="ECO:0000269|PubMed:15069071"
FT CONFLICT 251
FT /note="K -> E (in Ref. 1; AAA72127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41731 MW; 38CE9D5CF2E2AEE2 CRC64;
MDAQCSAKVN ARKRRKEAPG PNGATEEDGV PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV
RVTMEEASRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN
FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD
VYKHIKEAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
HMLKEGKGRM LQAISPKQSP SSSPTRERSP SPSFRWPFSG KTSPPCSPAN LSRHKAAAYD
ISEDEED
