CEPT1_HUMAN
ID CEPT1_HUMAN Reviewed; 416 AA.
AC Q9Y6K0; Q69YJ9; Q9P0Y8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1 {ECO:0000305};
DE Short=hCEPT1;
DE EC=2.7.8.1 {ECO:0000269|PubMed:10191259};
DE EC=2.7.8.2 {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425};
DE AltName: Full=1-alkenyl-2-acylglycerol choline phosphotransferase {ECO:0000305|PubMed:10893425};
DE EC=2.7.8.22 {ECO:0000269|PubMed:10893425};
GN Name=CEPT1 {ECO:0000312|HGNC:HGNC:24289}; ORFNames=PRO1101;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=10191259; DOI=10.1042/bj3390291;
RA Henneberry A.L., McMaster C.R.;
RT "Cloning and expression of a human choline/ethanolaminephosphotransferase:
RT synthesis of phosphatidylcholine and phosphatidylethanolamine.";
RL Biochem. J. 339:291-298(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y., Feng F.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 5 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-162.
RC TISSUE=Bone marrow;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10893425; DOI=10.1074/jbc.m005786200;
RA Henneberry A.L., Wistow G., McMaster C.R.;
RT "Cloning, genomic organization, and characterization of a human
RT cholinephosphotransferase.";
RL J. Biol. Chem. 275:29808-29815(2000).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=12216837; DOI=10.1007/s11745-002-0947-6;
RA Wright M.M., McMaster C.R.;
RT "PC and PE synthesis: mixed micellar analysis of the
RT cholinephosphotransferase and ethanolaminephosphotransferase activities of
RT human choline/ethanolamine phosphotransferase 1 (CEPT1).";
RL Lipids 37:663-672(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-144; SER-146; GLY-156;
RP THR-214; GLU-215; VAL-216; ILE-221; LEU-226 AND VAL-228.
RX PubMed=12221122; DOI=10.1091/mbc.01-11-0540;
RA Henneberry A.L., Wright M.M., McMaster C.R.;
RT "The major sites of cellular phospholipid synthesis and molecular
RT determinants of fatty acid and lipid head group specificity.";
RL Mol. Biol. Cell 13:3148-3161(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes both phosphatidylcholine and
CC phosphatidylethanolamine biosynthesis from CDP-choline and CDP-
CC ethanolamine, respectively. Involved in protein-dependent process of
CC phospholipid transport to distribute phosphatidyl choline to the
CC lumenal surface. Has a higher cholinephosphotransferase activity than
CC ethanolaminephosphotransferase activity. {ECO:0000269|PubMed:10191259,
CC ECO:0000269|PubMed:10893425, ECO:0000269|PubMed:12216837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:32943,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:64612; EC=2.7.8.1;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + CDP-choline = 1-O-alkyl-2-acyl-
CC sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:36179,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36702, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36180;
CC Evidence={ECO:0000305|PubMed:10893425};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-2-acyl-sn-glycerol + CDP-choline = 1-O-(1Z-
CC alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:36227, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:77286, ChEBI:CHEBI:77296; EC=2.7.8.22;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36228;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycerol + CDP-choline = 1,2-dioctanoyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54232,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:76979, ChEBI:CHEBI:78228;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + CDP-choline = 1,2-didecanoyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54236,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78226;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54237;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54240, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54241;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-choline =
CC 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP
CC + H(+); Xref=Rhea:RHEA:54244, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73001, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:54248, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54249;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-
CC ethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:54252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:73007, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54253;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + CDP-choline = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54332, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:74963, ChEBI:CHEBI:82949;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-
CC (9Z-hexadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54336, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:83717, ChEBI:CHEBI:84417;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54337;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-
CC di-(9Z-hexadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:54340, ChEBI:CHEBI:15378, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:84417, ChEBI:CHEBI:138145;
CC Evidence={ECO:0000269|PubMed:10191259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54341;
CC Evidence={ECO:0000305|PubMed:10191259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + CDP-choline = 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54348, ChEBI:CHEBI:15378, ChEBI:CHEBI:44811,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:75936;
CC Evidence={ECO:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54349;
CC Evidence={ECO:0000305|PubMed:10893425};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC CDP-choline = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:55430, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:77184;
CC Evidence={ECO:0000269|PubMed:10893425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54353;
CC Evidence={ECO:0000305|PubMed:10893425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10191259};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10191259};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for CDP-choline {ECO:0000269|PubMed:10191259,
CC ECO:0000269|PubMed:12216837};
CC KM=101 uM for CDP-ethanolamine {ECO:0000269|PubMed:10191259,
CC ECO:0000269|PubMed:12216837};
CC Vmax=10.5 nmol/min/mg enzyme with CDP-choline as substrate
CC {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:12216837};
CC Vmax=4.35 nmol/min/mg enzyme with CDP-ethanolamine as substrate
CC {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:12216837};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425}.
CC -!- INTERACTION:
CC Q9Y6K0; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1237183, EBI-742688;
CC Q9Y6K0; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1237183, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12221122}. Nucleus membrane
CC {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12221122}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10191259}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61194.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF068302; AAD25170.1; -; mRNA.
DR EMBL; AF138862; AAF61194.1; ALT_FRAME; mRNA.
DR EMBL; AL355816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032610; AAH32610.1; -; mRNA.
DR EMBL; BC049196; AAH49196.1; -; mRNA.
DR EMBL; AL833102; CAH10403.1; -; mRNA.
DR CCDS; CCDS830.1; -.
DR RefSeq; NP_001007795.1; NM_001007794.2.
DR RefSeq; NP_001317672.1; NM_001330743.1.
DR RefSeq; NP_006081.1; NM_006090.4.
DR AlphaFoldDB; Q9Y6K0; -.
DR BioGRID; 115662; 68.
DR IntAct; Q9Y6K0; 42.
DR MINT; Q9Y6K0; -.
DR STRING; 9606.ENSP00000441980; -.
DR BindingDB; Q9Y6K0; -.
DR ChEMBL; CHEMBL4105740; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR SwissLipids; SLP:000000137; -.
DR TCDB; 4.F.1.1.1; the choline/ethanolaminephosphotransferase 1 (cept1) family.
DR GlyGen; Q9Y6K0; 1 site.
DR iPTMnet; Q9Y6K0; -.
DR PhosphoSitePlus; Q9Y6K0; -.
DR SwissPalm; Q9Y6K0; -.
DR BioMuta; CEPT1; -.
DR DMDM; 74753524; -.
DR EPD; Q9Y6K0; -.
DR jPOST; Q9Y6K0; -.
DR MassIVE; Q9Y6K0; -.
DR MaxQB; Q9Y6K0; -.
DR PaxDb; Q9Y6K0; -.
DR PeptideAtlas; Q9Y6K0; -.
DR PRIDE; Q9Y6K0; -.
DR ProteomicsDB; 86708; -.
DR Antibodypedia; 46938; 105 antibodies from 19 providers.
DR DNASU; 10390; -.
DR Ensembl; ENST00000357172.9; ENSP00000349696.4; ENSG00000134255.15.
DR Ensembl; ENST00000545121.5; ENSP00000441980.1; ENSG00000134255.15.
DR GeneID; 10390; -.
DR KEGG; hsa:10390; -.
DR MANE-Select; ENST00000357172.9; ENSP00000349696.4; NM_006090.5; NP_006081.1.
DR UCSC; uc001eah.1; human.
DR CTD; 10390; -.
DR DisGeNET; 10390; -.
DR GeneCards; CEPT1; -.
DR HGNC; HGNC:24289; CEPT1.
DR HPA; ENSG00000134255; Low tissue specificity.
DR MIM; 616751; gene.
DR neXtProt; NX_Q9Y6K0; -.
DR OpenTargets; ENSG00000134255; -.
DR PharmGKB; PA134892657; -.
DR VEuPathDB; HostDB:ENSG00000134255; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q9Y6K0; -.
DR OMA; GHMSRSE; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q9Y6K0; -.
DR TreeFam; TF313270; -.
DR BioCyc; MetaCyc:HS05844-MON; -.
DR BRENDA; 2.7.8.1; 2681.
DR BRENDA; 2.7.8.2; 2681.
DR PathwayCommons; Q9Y6K0; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SABIO-RK; Q9Y6K0; -.
DR SignaLink; Q9Y6K0; -.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR BioGRID-ORCS; 10390; 106 hits in 1080 CRISPR screens.
DR ChiTaRS; CEPT1; human.
DR GenomeRNAi; 10390; -.
DR Pharos; Q9Y6K0; Tchem.
DR PRO; PR:Q9Y6K0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y6K0; protein.
DR Bgee; ENSG00000134255; Expressed in buccal mucosa cell and 198 other tissues.
DR ExpressionAtlas; Q9Y6K0; baseline and differential.
DR Genevisible; Q9Y6K0; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047359; F:1-alkenyl-2-acylglycerol choline phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0004307; F:ethanolaminephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; PTHR10414; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..416
FT /note="Choline/ethanolaminephosphotransferase 1"
FT /id="PRO_0000289245"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 138
FT /note="K->M: Induces a reduction in both
FT cholinephosphotransferase and
FT ethanolaminephosphotransferase activities."
FT MUTAGEN 144
FT /note="N->G: No effect."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 146
FT /note="S->Q,C: No effect."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 156
FT /note="G->C,S,A: Induces a reduction in
FT cholinephosphotransferase activity and abolishes
FT ethanolaminephosphotransferase activity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 214
FT /note="T->A: Alters the profile of diacylglycerol
FT utilization and results in modest reduction in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 215
FT /note="E->A,D: Induces a strong reduction in enzyme
FT activity without altering diacylglycerol specificity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 215
FT /note="E->Q: Induces a strong reduction in enzyme activity
FT and alters diacylglycerol specificity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 216
FT /note="V->A: Alters the profile of diacylglycerol
FT utilization and results in modest reduction in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 221
FT /note="I->A: Alters the profile of diacylglycerol
FT utilization and results in modest reduction in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 226
FT /note="L->A: Does not affect either the enzyme activity or
FT the diacylglycerol specificity."
FT /evidence="ECO:0000269|PubMed:12221122"
FT MUTAGEN 228
FT /note="V->A: Does not affect either the enzyme activity or
FT the diacylglycerol specificity."
FT /evidence="ECO:0000269|PubMed:12221122"
SQ SEQUENCE 416 AA; 46554 MW; A25FED1193342FD9 CRC64;
MSGHRSTRKR CGDSHPESPV GFGHMSTTGC VLNKLFQLPT PPLSRHQLKR LEEHRYQSAG
RSLLEPLMQG YWEWLVRRVP SWIAPNLITI IGLSINICTT ILLVFYCPTA TEQAPLWAYI
ACACGLFIYQ SLDAIDGKQA RRTNSSSPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD
WMFFCCFAGT FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSMIP
VLNIQMKIFP ALCTVAGTIF SCTNYFRVIF TGGVGKNGST IAGTSVLSPF LHIGSVITLA
AMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD
QYFNSFIDEY IVLWIALVFS FFDLIRYCVS VCNQIASHLH IHVFRIKVST AHSNHH
