ID CTPT_MOUSE STANDARD; PRT; 367 AA. AC P49586; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cholinephosphate cytidylyltransferase A (EC 2.7.7.15) DE (Phosphorylcholine transferase A) (CTP:phosphocholine DE cytidylyltransferase A) (CT A) (CCT A) (CCT-alpha). GN PCYT1A OR PCYT1 OR CTPCT. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/c; TISSUE=Testis; RX MEDLINE=94140374; PubMed=8307580; RA Rutherford M.S., Rock C.O., Jenkins N.A., Gilbert D.J., RA Tessner T.G., 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 SEQUENCE FROM N.A. RX MEDLINE=95002145; PubMed=7918629; 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 SEQUENCE FROM N.A. RC STRAIN=129/J; RX MEDLINE=97294724; PubMed=9148929; 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 SEQUENCE FROM N.A. RC STRAIN=FVB/N; TISSUE=Liver; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Controls phosphatidylcholine synthesis. CC -!- CATALYTIC ACTIVITY: CTP + choline phosphate = diphosphate + CDP- CC choline. CC -!- ENZYME REGULATION: By phosphorylation (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: It can interconvert between an inactive CC cytosolic form and an active 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 -!- 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; -. DR EMBL; L28956; AAA53526.1; -. DR EMBL; U84207; AAB63446.1; -. DR EMBL; U84200; AAB63446.1; JOINED. DR EMBL; U84201; AAB63446.1; JOINED. DR EMBL; U84202; AAB63446.1; JOINED. DR EMBL; U84203; AAB63446.1; JOINED. DR EMBL; U84204; AAB63446.1; JOINED. DR EMBL; U84205; AAB63446.1; JOINED. DR EMBL; U84206; AAB63446.1; JOINED. DR EMBL; BC018313; AAH18313.1; -. DR PIR; A49366; S24935. DR HSSP; P19836; 1PEI. DR MGD; MGI:88557; Pcyt1a. DR InterPro; IPR004821; Cyt_tran_rel. DR InterPro; IPR004820; Cytidylyltransf. DR Pfam; PF01467; CTP_transf_2; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. KW Transferase; Nucleotidyltransferase; Phospholipid biosynthesis; KW Repeat; Membrane; Phosphorylation. FT DOMAIN 74 235 Catalytic (Potential). FT DOMAIN 228 287 Amphipathic (Potential). FT DOMAIN 256 288 3 X 11 AA approximate tandem repeats. FT DOMAIN 319 348 3 X repeats. FT REPEAT 319 324 1. FT REPEAT 329 333 2 (approximate). FT REPEAT 343 348 3. FT MOD_RES 362 362 PHOSPHORYLATION (BY CK2) (BY FT SIMILARITY). FT CONFLICT 360 360 D -> V (in Ref. 2). 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 //