PCY1A_MOUSE
ID PCY1A_MOUSE Reviewed; 367 AA.
AC P49586; Q542W4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Choline-phosphate cytidylyltransferase A;
DE EC=2.7.7.15 {ECO:0000269|PubMed:12842190};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8307580; DOI=10.1016/s0888-7543(05)80377-5;
RA Rutherford M.S., Rock C.O., Jenkins N.A., Gilbert D.J., Tessner T.G.,
RA Copeland N.G., Jackowski S.;
RT "The gene for murine CTP:phosphocholine cytidylyltransferase (Ctpct) is
RT located on mouse chromosome 16.";
RL Genomics 18:698-701(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/J;
RX PubMed=9148929; DOI=10.1074/jbc.272.20.13146;
RA Tang W., Keesler G.A., Tabas I.;
RT "The structure of the gene for murine CTP:phosphocholine
RT cytidylyltransferase, Ctpct. Relationship of exon structure to functional
RT domains and identification of transcriptional start sites and potential
RT upstream regulatory elements.";
RL J. Biol. Chem. 272:13146-13151(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=12842190; DOI=10.1016/s1388-1981(03)00067-2;
RA Karim M., Jackson P., Jackowski S.;
RT "Gene structure, expression and identification of a new CTP:phosphocholine
RT cytidylyltransferase beta isoform.";
RL Biochim. Biophys. Acta 1633:1-12(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-323;
RP THR-325; SER-331; THR-342; SER-343; SER-347; THR-358 AND SER-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP UBIQUITINATION BY SCF(FBXL2).
RX PubMed=21343341; DOI=10.1128/mcb.00723-10;
RA Chen B.B., Coon T.A., Glasser J.R., Mallampalli R.K.;
RT "Calmodulin antagonizes a calcium-activated SCF ubiquitin E3 ligase
RT subunit, FBXL2, to regulate surfactant homeostasis.";
RL Mol. Cell. Biol. 31:1905-1920(2011).
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:12842190}.
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:12842190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000269|PubMed:12842190};
CC -!- ACTIVITY REGULATION: By phosphorylation. {ECO:0000250}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000269|PubMed:12842190}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19836}.
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:0000250|UniProtKB:P49585}. Nucleus {ECO:0000250|UniProtKB:P49585}.
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 and liver (at protein level)
CC (PubMed:12842190). Also found in heart, kidney, spleen, lung, skeletal
CC muscle, ovary and testis (PubMed:12842190).
CC {ECO:0000269|PubMed:12842190}.
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:0000269|PubMed:21343341}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; Z12302; CAA78172.1; -; mRNA.
DR EMBL; L28956; AAA53526.1; -; mRNA.
DR EMBL; U84207; AAB63446.1; -; Genomic_DNA.
DR EMBL; U84200; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84201; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84202; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84203; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84204; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84205; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; U84206; AAB63446.1; JOINED; Genomic_DNA.
DR EMBL; AK076050; BAC36148.1; -; mRNA.
DR EMBL; AK076830; BAC36497.1; -; mRNA.
DR EMBL; BC018313; AAH18313.1; -; mRNA.
DR CCDS; CCDS28120.1; -.
DR PIR; A49366; S24935.
DR RefSeq; NP_001156631.1; NM_001163159.1.
DR RefSeq; NP_001156632.1; NM_001163160.1.
DR RefSeq; NP_034111.1; NM_009981.4.
DR AlphaFoldDB; P49586; -.
DR SMR; P49586; -.
DR BioGRID; 198967; 4.
DR IntAct; P49586; 1.
DR MINT; P49586; -.
DR STRING; 10090.ENSMUSP00000130056; -.
DR iPTMnet; P49586; -.
DR PhosphoSitePlus; P49586; -.
DR EPD; P49586; -.
DR jPOST; P49586; -.
DR MaxQB; P49586; -.
DR PaxDb; P49586; -.
DR PeptideAtlas; P49586; -.
DR PRIDE; P49586; -.
DR ProteomicsDB; 287980; -.
DR Antibodypedia; 33936; 235 antibodies from 30 providers.
DR DNASU; 13026; -.
DR Ensembl; ENSMUST00000079791; ENSMUSP00000078721; ENSMUSG00000005615.
DR Ensembl; ENSMUST00000104893; ENSMUSP00000130056; ENSMUSG00000005615.
DR Ensembl; ENSMUST00000115140; ENSMUSP00000110793; ENSMUSG00000005615.
DR GeneID; 13026; -.
DR KEGG; mmu:13026; -.
DR UCSC; uc007yyw.2; mouse.
DR CTD; 5130; -.
DR MGI; MGI:88557; Pcyt1a.
DR VEuPathDB; HostDB:ENSMUSG00000005615; -.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000157384; -.
DR HOGENOM; CLU_034585_4_2_1; -.
DR InParanoid; P49586; -.
DR OMA; RWPFSAK; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; P49586; -.
DR TreeFam; TF106336; -.
DR BRENDA; 2.7.7.15; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR BioGRID-ORCS; 13026; 21 hits in 77 CRISPR screens.
DR ChiTaRS; Pcyt1a; mouse.
DR PRO; PR:P49586; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P49586; protein.
DR Bgee; ENSMUSG00000005615; Expressed in small intestine Peyer's patch and 257 other tissues.
DR ExpressionAtlas; P49586; baseline and differential.
DR Genevisible; P49586; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0042587; C:glycogen granule; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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; Cytoplasm; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleotidyltransferase; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation.
FT CHAIN 1..367
FT /note="Choline-phosphate cytidylyltransferase A"
FT /id="PRO_0000208454"
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..32
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"
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..353
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:0000250|UniProtKB:P49585"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:21183079"
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:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49585"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 360
FT /note="D -> V (in Ref. 2; AAA53526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41667 MW; 306B656D2EAAA2B3 CRC64;
MDAQSSAKVN SRKRRKEAPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV
RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN
FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD
VYKHIKDAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS LSRCRAVTCD
ISEDEED
