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   16-OCT-2013, entry version 121.
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-315; SER-319 AND
RP   SER-347, AND MASS 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-347, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
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   [9]
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.
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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   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   OrthoDB; EOG4DR9CX; -.
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.
FT   MOD_RES     319    319       Phosphoserine.
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
//