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 13-NOV-2013, entry version 122. DE RecName: Full=Choline-phosphate cytidylyltransferase A; DE EC=2.7.7.15; 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; 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) RT is 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 RT functional domains and identification of transcriptional start sites RT and potential 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASS RP SPECTROMETRY. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS RP SPECTROMETRY. 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 RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] 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: Controls phosphatidylcholine synthesis. CC -!- CATALYTIC ACTIVITY: CTP + phosphocholine = diphosphate + CDP- CC choline. CC -!- ENZYME REGULATION: By phosphorylation (By similarity). CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine CC biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). CC Membrane; Peripheral membrane protein (By similarity). Note=It can CC interconvert between an inactive cytosolic form and an active CC membrane-bound form (By similarity). 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 CC diacylglycerol, and is stabilized by dephosphorylation (By CC similarity). CC -!- PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to CC proteasomal degradation. CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00115490; -. 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 UniGene; Mm.98775; -. DR ProteinModelPortal; P49586; -. DR SMR; P49586; 40-216. DR IntAct; P49586; 2. DR MINT; MINT-4106778; -. DR STRING; 10090.ENSMUSP00000110793; -. DR PhosphoSite; P49586; -. DR PaxDb; P49586; -. DR PRIDE; P49586; -. 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 eggNOG; COG0615; -. DR GeneTree; ENSGT00390000000269; -. DR HOGENOM; HOG000230945; -. DR HOVERGEN; HBG053531; -. DR InParanoid; P49586; -. DR KO; K00968; -. DR OMA; SKMPRCA; -. DR UniPathway; UPA00753; UER00739. DR ChiTaRS; PCYT1A; mouse. DR NextBio; 282896; -. DR PRO; PR:P49586; -. DR ArrayExpress; P49586; -. DR Bgee; P49586; -. DR Genevestigator; P49586; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0042587; C:glycogen granule; IDA:MGI. DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; ISS:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:Ensembl. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_2; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Lipid biosynthesis; KW Lipid metabolism; Membrane; Nucleotidyltransferase; KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; KW Reference proteome; Repeat; Transferase; Ubl conjugation. FT CHAIN 1 367 Choline-phosphate cytidylyltransferase A. FT /FTId=PRO_0000208454. FT REPEAT 319 324 1. FT REPEAT 329 333 2; approximate. FT REPEAT 343 348 3. FT NP_BIND 84 92 CTP (By similarity). FT NP_BIND 168 169 CTP (By similarity). FT NP_BIND 196 200 CTP (By similarity). FT REGION 228 287 Amphipathic (Potential). FT REGION 256 288 3 X 11 AA approximate tandem repeats. FT REGION 319 348 3 X repeats. FT BINDING 122 122 CTP (By similarity). FT BINDING 122 122 Substrate (By similarity). FT BINDING 151 151 Substrate (By similarity). FT BINDING 173 173 CTP (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 8 8 N6-acetyllysine (By similarity). FT MOD_RES 315 315 Phosphoserine (By similarity). FT MOD_RES 319 319 Phosphoserine (By similarity). FT MOD_RES 321 321 Phosphoserine (By similarity). FT MOD_RES 322 322 Phosphoserine (By similarity). FT MOD_RES 323 323 Phosphoserine (By similarity). FT MOD_RES 329 329 Phosphoserine (By similarity). FT MOD_RES 331 331 Phosphoserine (By similarity). FT MOD_RES 333 333 Phosphoserine (By similarity). FT MOD_RES 343 343 Phosphoserine (By similarity). FT MOD_RES 345 345 Phosphoserine (By similarity). FT MOD_RES 346 346 Phosphoserine (By similarity). FT MOD_RES 347 347 Phosphoserine. FT MOD_RES 350 350 Phosphoserine (By similarity). FT MOD_RES 352 352 Phosphoserine (By similarity). FT MOD_RES 362 362 Phosphoserine. FT CONFLICT 360 360 D -> V (in Ref. 2; AAA53526). 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 //