CEPT1_CHICK
ID CEPT1_CHICK Reviewed; 416 AA.
AC Q5ZKD1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
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; ORFNames=RCJMB04_11l7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG31812.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ720153; CAG31812.1; ALT_INIT; mRNA.
DR RefSeq; NP_001006392.1; NM_001006392.2.
DR AlphaFoldDB; Q5ZKD1; -.
DR STRING; 9031.ENSGALP00000000194; -.
DR PaxDb; Q5ZKD1; -.
DR GeneID; 421152; -.
DR KEGG; gga:421152; -.
DR CTD; 10390; -.
DR VEuPathDB; HostDB:geneid_421152; -.
DR eggNOG; KOG2877; Eukaryota.
DR InParanoid; Q5ZKD1; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q5ZKD1; -.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:Q5ZKD1; -.
DR Proteomes; UP000000539; Unplaced.
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; 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: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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..416
FT /note="Choline/ethanolaminephosphotransferase 1"
FT /id="PRO_0000289248"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
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 CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 416 AA; 46097 MW; A3FB4A5692A756D8 CRC64;
MSGHRNLKRR CGESHLESPA GCAHGPAAAC VLSKLVQLPT PPLSKHQLKR LEEHKYQSAG
RSLLEPLMQG YWEWLVGKVP AWIAPNLITI IGLLINIFTT LLLVYYCPTA TEQAPPWAYI
ACACGLFIYQ SLDTIDGKQA RRTNSSTPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD
WMFFCCFAGT FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSLIP
ILNIQVKIFP ALCTVAGTIF SCTNYFGVIF TGGVGKNGST IAGTSVLSPF LHIGSVIALA
AMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD
QYFNSFIDEY IVLWIALIFS LFDLLRYCVS VCNQIAAHLH IHVFRIKSSS THSNHH
