CHPT1_XENLA
ID CHPT1_XENLA Reviewed; 402 AA.
AC Q4KLV1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) 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; BC098988; AAH98988.1; -; mRNA.
DR RefSeq; NP_001089575.1; NM_001096106.1.
DR AlphaFoldDB; Q4KLV1; -.
DR DNASU; 734631; -.
DR GeneID; 734631; -.
DR KEGG; xla:734631; -.
DR CTD; 734631; -.
DR Xenbase; XB-GENE-6489129; chpt1.L.
DR OrthoDB; 847100at2759; -.
DR UniPathway; UPA00753; UER00740.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 734631; Expressed in egg cell and 19 other tissues.
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; IEA:UniProtKB-EC.
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 Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Manganese; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..402
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000289257"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
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 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 402 AA; 44513 MW; 787A412C501ABFFA CRC64;
MGLAEGLAAR MAPHLYIQEP LSAQQLKKLE EHKYSASGRS LVEPPMQVYW NWLVEKVPLW
LAPNTITMVG LLLNVLSTLI LVCYCPTATE GAPFWTYLLC AIGLFVYQSL DAIDGKQARR
TNSSSPLGEM FDHGCDSISI VFVNLGTIAA VRLGTLPGWM FYCCFVGMFM FYCAQWQTYV
CGTLKFGIID VTELQISVTV MFLMTAVCGP ELWDYEIPFT GLPMKTIPLL GIIGGTVYSC
SNYFRVILSG GVGKNGSTVA GTSVLSPGLH IGLVLLLALM IYKKSTTNLF LQNPCLYTLA
FGFVSAKITI KLVIAHMTKS EISLQDTAFI GPGLLFFNQY FNSFIDEYIV LWIAMVISFA
DLLRYCISVC LQIATHLRIS VFRISSNQAA EQVQTQKQKL TD
