ID CHPT1_BOVIN Reviewed; 406 AA.
AC Q1LZE6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Cholinephosphotransferase 1 {ECO:0000305};
DE EC=2.7.8.2 {ECO:0000250|UniProtKB:Q8WUD6};
DE AltName: Full=Diacylglycerol cholinephosphotransferase 1;
GN Name=CHPT1; Synonyms=CPT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the final step of de novo phosphatidylcholine (PC)
CC synthesis, i.e. the transfer of choline phosphate from CDP-choline to
CC the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby
CC plays a central role in the formation and maintenance of vesicular
CC membranes. {ECO:0000250|UniProtKB:Q8WUD6}.
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:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + CDP-choline = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54344,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:74965, ChEBI:CHEBI:75728;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54345;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
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:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
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:Q8WUD6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
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:Q4KLV1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233;
CC Evidence={ECO:0000250|UniProtKB:Q4KLV1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8WUD6};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC {ECO:0000250|UniProtKB:Q8WUD6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WUD6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8WUD6}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; BC116046; AAI16047.1; -; mRNA.
DR RefSeq; NP_001068975.1; NM_001075507.1.
DR AlphaFoldDB; Q1LZE6; -.
DR SMR; Q1LZE6; -.
DR STRING; 9913.ENSBTAP00000073107; -.
DR PaxDb; 9913-ENSBTAP00000003236; -.
DR Ensembl; ENSBTAT00000003236.5; ENSBTAP00000003236.4; ENSBTAG00000002490.5.
DR GeneID; 511291; -.
DR KEGG; bta:511291; -.
DR CTD; 56994; -.
DR VEuPathDB; HostDB:ENSBTAG00000002490; -.
DR VGNC; VGNC:27314; CHPT1.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q1LZE6; -.
DR OrthoDB; 5482983at2759; -.
DR TreeFam; TF313270; -.
DR Reactome; R-BTA-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00740.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000002490; Expressed in liver and 106 other cell types or tissues.
DR ExpressionAtlas; Q1LZE6; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006663; P:platelet activating factor 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:SF32; CHOLINEPHOSPHOTRANSFERASE 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.
PE 2: Evidence at transcript level;
KW Acetylation; Golgi apparatus; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WUD6"
FT CHAIN 2..406
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000289251"
FT TOPO_DOM 2..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 84..93
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 119..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 151..160
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 180..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 191..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 208..222
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..248
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 249..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 282..293
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..316
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 317..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 330..339
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 340..346
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 347..376
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT TOPO_DOM 377..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 64
FT /ligand="CDP-choline"
FT /ligand_id="ChEBI:CHEBI:58779"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 119
FT /ligand="CDP-choline"
FT /ligand_id="ChEBI:CHEBI:58779"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT SITE 129
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:Q4KLV1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUD6"
SQ SEQUENCE 406 AA; 45249 MW; 7EA04603AC4A27A2 CRC64;
MAAGAGARPA PRWLKALTEP LSAAQLRRLE EHRYTAAGVS LLEPPLQLYW TWLLQWIPLW
MAPNSITLLG LAINMLTTLV LISYCPTVTE EAPYWTYLLC ALGLFIYQSL DAIDGKQARR
TNSCSPLGEL FDHGCDSLST VFMAVGASIA VRLGTHPDWL FFCSFIGMFM FYCAHWQTYV
SGVLRFGKVD VTEIQIALVI VFVLSTFGGA TMWDYTIPIL EIKLKILPVL GVVGGAIFSC
SNYFHVILHG GVGKNGSTIA GTSVLSPGLH IGIIIILAIM IYKKSATNLF EKHPCLYTLM
FGCVFAKVSQ KLVIAHMTKS ELYLQDTVFI GPGLLFLDQY FNNFVDEYIV LWIAMVISSL
DMMRYFSALC LQISRHLHLS IFKTSCHQAP EQVQVLPPKS HQNNMD
//
