ID CHPT1_RAT Reviewed; 398 AA.
AC Q66H21;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 120.
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 {ECO:0000312|RGD:1359283}; Synonyms=Cpt1;
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=Testis;
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 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; BC082074; AAH82074.1; -; mRNA.
DR RefSeq; NP_001007751.1; NM_001007750.1.
DR AlphaFoldDB; Q66H21; -.
DR SMR; Q66H21; -.
DR STRING; 10116.ENSRNOP00000072444; -.
DR PhosphoSitePlus; Q66H21; -.
DR PaxDb; 10116-ENSRNOP00000007305; -.
DR Ensembl; ENSRNOT00000080939.2; ENSRNOP00000072444.1; ENSRNOG00000058271.2.
DR KEGG; rno:362866; -.
DR UCSC; RGD:1359283; rat.
DR AGR; RGD:1359283; -.
DR CTD; 56994; -.
DR RGD; 1359283; Chpt1.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_1_0_1; -.
DR InParanoid; Q66H21; -.
DR OrthoDB; 5482983at2759; -.
DR PhylomeDB; Q66H21; -.
DR TreeFam; TF313270; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:Q66H21; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000058271; Expressed in adult mammalian kidney and 18 other cell types or tissues.
DR Genevisible; Q66H21; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; ISO:RGD.
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:0006663; P:platelet activating factor biosynthetic process; ISO:RGD.
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..398
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000289254"
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..398
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 398 AA; 44601 MW; 9A6A12BD69E107D9 CRC64;
MAAGAGARPA PRWVKALGEP LSAAQLRRLE DHRYSAAGES LFEPPLQLFW TWLLQWIPLW
IAPNTITLFG LAINLFTTLV LIFYCPTVTE EAPYWTYLLC ALGLFIYQSL DAIDGKQARR
TNSCSPLGEL FDHGCDSLST VFMAIGASIA VRLGTHPDWL FFCSFVGMFM FYCAHWQTYV
SGVLRFGRVD VTEIQVALVI VFLLSTFGGA MMWDYTIPIL EIKLKILPVL GVVGGLIFSC
SNYFHVILHG GVGKNGSTIA GTSVLSPGLH IGLIIILAIM IYKKSATNVF EKHPCLYTLM
FGCVFAKVAQ KLVIAHMTKS ELYLQDTVFI GPGLLFLDQY FNNFIDEYVV LWIAMVITSF
DMMIYFSSLC LQISRHLHLS IFKTSYQQAP EQVHKHID
//
