CHPT1_BOVIN
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 03-AUG-2022, entry version 99.
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 phosphatidylcholine biosynthesis from CDP-choline.
CC It thereby plays a central role in the formation and maintenance of
CC vesicular 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 -!- 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 STRING; 9913.ENSBTAP00000003236; -.
DR PaxDb; Q1LZE6; -.
DR PRIDE; Q1LZE6; -.
DR Ensembl; ENSBTAT00000003236; ENSBTAP00000003236; ENSBTAG00000002490.
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; 847100at2759; -.
DR TreeFam; TF313270; -.
DR UniPathway; UPA00753; UER00740.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000002490; Expressed in liver and 106 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
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
