CEPT1_MOUSE
ID CEPT1_MOUSE Reviewed; 416 AA.
AC Q8BGS7; Q8VC64;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1 {ECO:0000305};
DE Short=mCEPT1;
DE EC=2.7.8.1 {ECO:0000250|UniProtKB:Q9Y6K0};
DE EC=2.7.8.2 {ECO:0000250|UniProtKB:Q9Y6K0};
DE AltName: Full=1-alkenyl-2-acylglycerol choline phosphotransferase {ECO:0000305};
DE EC=2.7.8.22 {ECO:0000250|UniProtKB:Q9Y6K0};
GN Name=Cept1 {ECO:0000312|MGI:MGI:2139793};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Vagina;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000250|UniProtKB:Q9Y6K0}.
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36180;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36228;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54237;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54241;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54249;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54253;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54337;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54341;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54349;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
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:0000250|UniProtKB:Q9Y6K0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54353;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K0};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC {ECO:0000250|UniProtKB:Q9Y6K0}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC {ECO:0000250|UniProtKB:Q9Y6K0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y6K0}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9Y6K0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y6K0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGS7-2; Sequence=VSP_025988;
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AK037116; BAC29710.1; -; mRNA.
DR EMBL; BC021753; AAH21753.1; -; mRNA.
DR EMBL; BC023783; AAH23783.1; -; mRNA.
DR CCDS; CCDS17723.1; -. [Q8BGS7-1]
DR CCDS; CCDS79995.1; -. [Q8BGS7-2]
DR RefSeq; NP_001280623.1; NM_001293694.1. [Q8BGS7-2]
DR RefSeq; NP_598630.2; NM_133869.4. [Q8BGS7-1]
DR RefSeq; XP_006502534.1; XM_006502471.3. [Q8BGS7-1]
DR RefSeq; XP_006502535.1; XM_006502472.3.
DR RefSeq; XP_017175329.1; XM_017319840.1.
DR AlphaFoldDB; Q8BGS7; -.
DR BioGRID; 221308; 4.
DR STRING; 10090.ENSMUSP00000065743; -.
DR GlyGen; Q8BGS7; 1 site.
DR iPTMnet; Q8BGS7; -.
DR PhosphoSitePlus; Q8BGS7; -.
DR SwissPalm; Q8BGS7; -.
DR EPD; Q8BGS7; -.
DR jPOST; Q8BGS7; -.
DR MaxQB; Q8BGS7; -.
DR PaxDb; Q8BGS7; -.
DR PRIDE; Q8BGS7; -.
DR ProteomicsDB; 280073; -. [Q8BGS7-1]
DR ProteomicsDB; 280074; -. [Q8BGS7-2]
DR Antibodypedia; 46938; 105 antibodies from 19 providers.
DR DNASU; 99712; -.
DR Ensembl; ENSMUST00000039153; ENSMUSP00000037277; ENSMUSG00000040774. [Q8BGS7-2]
DR Ensembl; ENSMUST00000068301; ENSMUSP00000065743; ENSMUSG00000040774. [Q8BGS7-1]
DR Ensembl; ENSMUST00000121231; ENSMUSP00000112509; ENSMUSG00000040774. [Q8BGS7-1]
DR GeneID; 99712; -.
DR KEGG; mmu:99712; -.
DR UCSC; uc008qwc.2; mouse. [Q8BGS7-1]
DR UCSC; uc012cvs.2; mouse. [Q8BGS7-2]
DR CTD; 10390; -.
DR MGI; MGI:2139793; Cept1.
DR VEuPathDB; HostDB:ENSMUSG00000040774; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q8BGS7; -.
DR OMA; GMWMYST; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q8BGS7; -.
DR TreeFam; TF313270; -.
DR BRENDA; 2.7.8.1; 3474.
DR BRENDA; 2.7.8.2; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR BioGRID-ORCS; 99712; 22 hits in 80 CRISPR screens.
DR ChiTaRS; Cept1; mouse.
DR PRO; PR:Q8BGS7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BGS7; protein.
DR Bgee; ENSMUSG00000040774; Expressed in humerus cartilage element and 246 other tissues.
DR ExpressionAtlas; Q8BGS7; baseline and differential.
DR Genevisible; Q8BGS7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:MGI.
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 Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleus; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..416
FT /note="Choline/ethanolaminephosphotransferase 1"
FT /id="PRO_0000289246"
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:0000250|UniProtKB:Q9Y6K0"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K0"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 211..238
FT /note="IDVTEVQIFIIIMHLLAVIGGPPFWQSM -> FDVTESQILIILFQLLSGTV
FT GPWFWNFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025988"
SQ SEQUENCE 416 AA; 46434 MW; 74CE59CD1CC410A9 CRC64;
MSGHRSTRKR CGDSHPESPV GFGHMSTTGC VLNKLFQLPT PPLSRHQLKR LEEHRYQSAG
RSLLEPLMQG YWEWLVGRVP SWIAPNLITI IGLSINICTT ILLVFYCPTA TEQAPLWAYI
ACACGLFIYQ SLDAIDGKQA RRTNSSSPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD
WMFFCCFAGT FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSMIP
VLNIQMKLLP ALCTVAGTIF SCTNYFRVIF TGGVGKNGST IAGTSVLSPF LHIGSVITLA
VMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD
QYFNSFIDEY IVLWIALIFS FFDLIRYCVS VCNQIASHLH IHVFRIKAST AHSNHH
