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Database: UniProt
Entry: G7NW49_MACFA
LinkDB: G7NW49_MACFA
Original site: G7NW49_MACFA 
ID   G7NW49_MACFA            Unreviewed;       444 AA.
AC   G7NW49;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Choline/ethanolaminephosphotransferase 1 {ECO:0000256|ARBA:ARBA00039228};
DE            EC=2.7.8.1 {ECO:0000256|ARBA:ARBA00038986};
DE            EC=2.7.8.2 {ECO:0000256|ARBA:ARBA00038987};
DE            EC=2.7.8.22 {ECO:0000256|ARBA:ARBA00038994};
DE   AltName: Full=1-alkenyl-2-acylglycerol choline phosphotransferase {ECO:0000256|ARBA:ARBA00042366};
GN   Name=CEPT1 {ECO:0000313|Ensembl:ENSMFAP00000025434.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000025434.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000025434.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000025434.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037663}.
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:0000256|ARBA:ARBA00035878};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54337;
CC         Evidence={ECO:0000256|ARBA:ARBA00035878};
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:0000256|ARBA:ARBA00036341};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54341;
CC         Evidence={ECO:0000256|ARBA:ARBA00036341};
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:0000256|ARBA:ARBA00036096};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54241;
CC         Evidence={ECO:0000256|ARBA:ARBA00036096};
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:0000256|ARBA:ARBA00036523};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54249;
CC         Evidence={ECO:0000256|ARBA:ARBA00036523};
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:0000256|ARBA:ARBA00036329};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54237;
CC         Evidence={ECO:0000256|ARBA:ARBA00036329};
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:0000256|ARBA:ARBA00036651};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233;
CC         Evidence={ECO:0000256|ARBA:ARBA00036651};
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:0000256|ARBA:ARBA00036576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36228;
CC         Evidence={ECO:0000256|ARBA:ARBA00036576};
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:0000256|ARBA:ARBA00035779};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36180;
CC         Evidence={ECO:0000256|ARBA:ARBA00035779};
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:0000256|ARBA:ARBA00036748};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54353;
CC         Evidence={ECO:0000256|ARBA:ARBA00036748};
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:0000256|ARBA:ARBA00036059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54349;
CC         Evidence={ECO:0000256|ARBA:ARBA00036059};
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:0000256|ARBA:ARBA00036100};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC         Evidence={ECO:0000256|ARBA:ARBA00036100};
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:0000256|ARBA:ARBA00036890};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC         Evidence={ECO:0000256|ARBA:ARBA00036890};
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:0000256|ARBA:ARBA00035972};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54253;
CC         Evidence={ECO:0000256|ARBA:ARBA00035972};
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:0000256|ARBA:ARBA00035868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC         Evidence={ECO:0000256|ARBA:ARBA00035868};
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:0000256|ARBA:ARBA00036031};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944;
CC         Evidence={ECO:0000256|ARBA:ARBA00036031};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC       phosphatidylcholine from phosphocholine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00037890}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00037891}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC       {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004232}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR   AlphaFoldDB; G7NW49; -.
DR   Ensembl; ENSMFAT00000033583.2; ENSMFAP00000025434.2; ENSMFAG00000044191.2.
DR   VEuPathDB; HostDB:ENSMFAG00000044191; -.
DR   eggNOG; KOG2877; Eukaryota.
DR   GeneTree; ENSGT00950000183117; -.
DR   OrthoDB; 5482983at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000044191; Expressed in spleen and 13 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:Ensembl.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   InterPro; IPR014472; CHOPT.
DR   PANTHER; PTHR10414:SF27; CHOLINE_ETHANOLAMINEPHOSPHOTRANSFERASE 1; 1.
DR   PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF015665; CHOPT; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        87..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
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"
SQ   SEQUENCE   444 AA;  49549 MW;  B5719225C328FB6D 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
     AMIYKKSTVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD
     QYFNSFIDEY IVLWIALVFS FFDLIRYCVS VCNQIASHLH IHVFRIKGKN VSAEIPSSLA
     KELNCAAQNK DQLEVGCPRL KVKD
//
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