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Database: UniProt
Entry: F6PYU3_ORNAN
LinkDB: F6PYU3_ORNAN
Original site: F6PYU3_ORNAN 
ID   F6PYU3_ORNAN            Unreviewed;       409 AA.
AC   F6PYU3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Cholinephosphotransferase 1 {ECO:0000256|ARBA:ARBA00040330};
DE            EC=2.7.8.2 {ECO:0000256|ARBA:ARBA00038987};
DE   AltName: Full=Diacylglycerol cholinephosphotransferase 1 {ECO:0000256|ARBA:ARBA00041597};
GN   Name=CHPT1 {ECO:0000313|Ensembl:ENSOANP00000008863.3};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000008863.3, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000008863.3, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000008863.3,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000008863.3}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000008863.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036651};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54233;
CC         Evidence={ECO:0000256|ARBA:ARBA00036651};
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:0000256|ARBA:ARBA00036100};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54333;
CC         Evidence={ECO:0000256|ARBA:ARBA00036100};
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:0000256|ARBA:ARBA00036890};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54245;
CC         Evidence={ECO:0000256|ARBA:ARBA00036890};
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:0000256|ARBA:ARBA00035763};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54345;
CC         Evidence={ECO:0000256|ARBA:ARBA00035763};
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:0000256|ARBA:ARBA00035868};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC         Evidence={ECO:0000256|ARBA:ARBA00035868};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC       phosphatidylcholine from phosphocholine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00037890}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR   AlphaFoldDB; F6PYU3; -.
DR   STRING; 9258.ENSOANP00000008863; -.
DR   Ensembl; ENSOANT00000008865.3; ENSOANP00000008863.3; ENSOANG00000005575.3.
DR   eggNOG; KOG2877; Eukaryota.
DR   GeneTree; ENSGT00950000183117; -.
DR   HOGENOM; CLU_035066_1_0_1; -.
DR   InParanoid; F6PYU3; -.
DR   OMA; MTRSELY; -.
DR   OrthoDB; 5482983at2759; -.
DR   TreeFam; TF313270; -.
DR   Proteomes; UP000002279; Chromosome 14.
DR   Bgee; ENSOANG00000005575; Expressed in testis and 8 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        69..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   409 AA;  44893 MW;  1293EE7AB44E2F07 CRC64;
     MAAGAGAGAG AGAGWAWWAP AEPLSPAQLK RLEEHRYNAA GRSLLEPPLQ RFWGWLVERV
     PPWLAPNTIT LTGLLLNLLT TLVLVAYCPT ATEQAPFWTF LLCALGLFIY QSLDAIDGKQ
     ARRTNSSSPL GELFDHGCDS VSTVFVAIGA CISIRLGTNP DWLFFCCFIG MFMFYCAHWQ
     TYVSGMLRFG KVDVTEVQIA IIIIFLLSAI GGTTMWDYTI PMIELKLKVF PILGIVAGAL
     FSCSNYFHVI LNGGVGKNGS TIAGTSVLSP GLHIGLIIAL AIMIYKKSAS QLFEKHPCLY
     VLTFGCVSAK VTQKLVIAHM TKSELYLQDT AFIGPGLLFL NQYFNSFIDE YIILWIAMCI
     SVFDLLRYST AVCLQIAAHL KICVFRIASH PAPEQVQVLS SKSHQNNMD
//
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