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   01-OCT-2004 (Rel. 45, Last annotation update)
DE   Choline-phosphate cytidylyltransferase A (EC 2.7.7.15)
DE   (Phosphorylcholine transferase A) (CTP:phosphocholine
DE   cytidylyltransferase A) (CT A) (CCT A) (CCT-alpha).
GN   Name=Pcyt1a; Synonyms=Pcyt1, 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., 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   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; DOI=10.1073/pnas.242603899;
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 human
RT   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; disulfide-linked (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.
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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   GO; GO:0006656; P:phosphatidylcholine biosynthesis; IDA.
DR   GO; GO:0009628; P:response to abiotic stimulus; IDA.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR004821; Cyt_trans_rel.
DR   InterPro; IPR001800; Lipoprotein_6.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
KW   Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW   Phosphorylation; Repeat; Transferase.
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   DISULFID     37     37       Interchain (By similarity).
FT   MOD_RES     362    362       Phosphoserine (by CK2) (By 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
//