CEPT1_RAT
ID CEPT1_RAT Reviewed; 416 AA.
AC Q6AXM5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1 {ECO:0000305};
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|RGD:1359727};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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 -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; BC079471; AAH79471.1; -; mRNA.
DR RefSeq; NP_001007700.1; NM_001007699.1.
DR RefSeq; XP_006233178.1; XM_006233116.3.
DR RefSeq; XP_006233180.1; XM_006233118.3.
DR RefSeq; XP_017446413.1; XM_017590924.1.
DR AlphaFoldDB; Q6AXM5; -.
DR STRING; 10116.ENSRNOP00000032597; -.
DR GlyGen; Q6AXM5; 1 site.
DR PhosphoSitePlus; Q6AXM5; -.
DR PaxDb; Q6AXM5; -.
DR PRIDE; Q6AXM5; -.
DR Ensembl; ENSRNOT00000036551; ENSRNOP00000032597; ENSRNOG00000017723.
DR GeneID; 310773; -.
DR KEGG; rno:310773; -.
DR UCSC; RGD:1359727; rat.
DR CTD; 10390; -.
DR RGD; 1359727; Cept1.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q6AXM5; -.
DR OMA; GMWMYST; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q6AXM5; -.
DR TreeFam; TF313270; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:Q6AXM5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017723; Expressed in liver and 20 other tissues.
DR Genevisible; Q6AXM5; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
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 2: Evidence at transcript 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_0000289247"
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"
SQ SEQUENCE 416 AA; 46498 MW; 13C6E63AADC8D76B CRC64;
MSGHRSTRKR CGDSHPESPV GFGHMSTTGC ILNKLFQLPT PPLSRHQLKR LEEHRYQSAG
RSLLEPLMQG YWEWLVGRVP SWIAPNLITI IGLSINICTT ILLVFYCPTA TEQAPLWAYI
ACACGLFIYQ SLDAIDGKQA RRTNSSSPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD
WMFFCCFAGT FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSMIP
VLNIQMKLFP ALCTVAGTIF SCTNYFRVIF TGGVGKNGST IAGTSVLSPF LHIGSVITLA
VMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD
QYFNSFIDEY IVLWIALVFS FFDLIRYCVS VCNQIASHLH IHVFRIKTST AHSNHH
