ID B8JLM0_DANRE Unreviewed; 426 AA.
AC B8JLM0; A0A8M1NPR8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1 {ECO:0000256|ARBA:ARBA00039228};
DE EC=2.7.8.1 {ECO:0000256|ARBA:ARBA00038986};
DE EC=2.7.8.2 {ECO:0000256|ARBA:ARBA00038987};
DE EC=2.7.8.22 {ECO:0000256|ARBA:ARBA00038994};
DE AltName: Full=1-alkenyl-2-acylglycerol choline phosphotransferase {ECO:0000256|ARBA:ARBA00042366};
GN Name=cept1a {ECO:0000313|Ensembl:ENSDARP00000076042,
GN ECO:0000313|RefSeq:NP_001138264.1,
GN ECO:0000313|ZFIN:ZDB-GENE-081105-47};
GN Synonyms=si:dkey-208b23.1 {ECO:0000313|RefSeq:NP_001138264.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000076042};
RN [1] {ECO:0000313|RefSeq:NP_001138264.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001138264.1};
RX PubMed=22479358;
RA Mariotti M., Ridge P.G., Zhang Y., Lobanov A.V., Pringle T.H., Guigo R.,
RA Hatfield D.L., Gladyshev V.N.;
RT "Composition and evolution of the vertebrate and mammalian
RT selenoproteomes.";
RL PLoS ONE 7:E33066-E33066(2012).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000076042, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000076042};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000076042}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000076042};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:NP_001138264.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001138264.1};
RX PubMed=25601102;
RA Haug M.F., Gesemann M., Lazovic V., Neuhauss S.C.;
RT "Eumetazoan cryptochrome phylogeny and evolution.";
RL Genome Biol. Evol. 7:601-619(2015).
RN [5] {ECO:0000313|RefSeq:NP_001138264.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001138264.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [6] {ECO:0000313|RefSeq:NP_001138264.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001138264.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [7] {ECO:0000313|RefSeq:NP_001138264.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001138264.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes both phosphatidylcholine and
CC phosphatidylethanolamine biosynthesis from CDP-choline and CDP-
CC ethanolamine, respectively. Involved in protein-dependent process of
CC phospholipid transport to distribute phosphatidyl choline to the
CC lumenal surface. Has a higher cholinephosphotransferase activity than
CC ethanolaminephosphotransferase activity.
CC {ECO:0000256|ARBA:ARBA00037663}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-
CC (9Z-hexadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54336, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:83717, ChEBI:CHEBI:84417;
CC Evidence={ECO:0000256|ARBA:ARBA00035878};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54337;
CC Evidence={ECO:0000256|ARBA:ARBA00035878};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-
CC di-(9Z-hexadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:54340, ChEBI:CHEBI:15378, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:84417, ChEBI:CHEBI:138145;
CC Evidence={ECO:0000256|ARBA:ARBA00036341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54341;
CC Evidence={ECO:0000256|ARBA:ARBA00036341};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54240, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000256|ARBA:ARBA00036096};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54241;
CC Evidence={ECO:0000256|ARBA:ARBA00036096};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + CDP-ethanolamine = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:54248, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000256|ARBA:ARBA00036523};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54249;
CC Evidence={ECO:0000256|ARBA:ARBA00036523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + CDP-choline = 1,2-didecanoyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54236,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78226;
CC Evidence={ECO:0000256|ARBA:ARBA00036329};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54237;
CC Evidence={ECO:0000256|ARBA:ARBA00036329};
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-O-(1Z-alkenyl)-2-acyl-sn-glycerol + CDP-choline = 1-O-(1Z-
CC alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:36227, ChEBI:CHEBI:15378, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:77286, ChEBI:CHEBI:77296; EC=2.7.8.22;
CC Evidence={ECO:0000256|ARBA:ARBA00036576};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36228;
CC Evidence={ECO:0000256|ARBA:ARBA00036576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-2-acyl-sn-glycerol + CDP-choline = 1-O-alkyl-2-acyl-
CC sn-glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:36179,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36702, ChEBI:CHEBI:52595,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000256|ARBA:ARBA00035779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36180;
CC Evidence={ECO:0000256|ARBA:ARBA00035779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol +
CC CDP-choline = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:54352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:55430, ChEBI:CHEBI:58779,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:77184;
CC Evidence={ECO:0000256|ARBA:ARBA00036748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54353;
CC Evidence={ECO:0000256|ARBA:ARBA00036748};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + CDP-choline = 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:54348, ChEBI:CHEBI:15378, ChEBI:CHEBI:44811,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:75936;
CC Evidence={ECO:0000256|ARBA:ARBA00036059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54349;
CC Evidence={ECO:0000256|ARBA:ARBA00036059};
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-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-
CC ethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:54252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57876, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:73007, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000256|ARBA:ARBA00035972};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54253;
CC Evidence={ECO:0000256|ARBA:ARBA00035972};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:32943,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:64612; EC=2.7.8.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32944;
CC Evidence={ECO:0000256|ARBA:ARBA00036031};
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC {ECO:0000256|ARBA:ARBA00037891}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004232}.
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 EMBL; CU463105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU469314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001138264.1; NM_001144792.3.
DR STRING; 7955.ENSDARP00000076042; -.
DR PaxDb; 7955-ENSDARP00000076042; -.
DR Ensembl; ENSDART00000081601; ENSDARP00000076042; ENSDARG00000058716.
DR Ensembl; ENSDART00000081601.5; ENSDARP00000076042.3; ENSDARG00000058716.5.
DR GeneID; 560225; -.
DR KEGG; dre:560225; -.
DR AGR; ZFIN:ZDB-GENE-081105-47; -.
DR CTD; 560225; -.
DR ZFIN; ZDB-GENE-081105-47; cept1a.
DR eggNOG; KOG2877; Eukaryota.
DR HOGENOM; CLU_035066_1_0_1; -.
DR OMA; WVWSIVG; -.
DR OrthoDB; 5482983at2759; -.
DR PhylomeDB; B8JLM0; -.
DR TreeFam; TF313270; -.
DR Proteomes; UP000000437; Chromosome 8.
DR Bgee; ENSDARG00000058716; Expressed in early embryo and 13 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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0004307; F:ethanolaminephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
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:SF27; CHOLINE_ETHANOLAMINEPHOSPHOTRANSFERASE 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 1: Evidence at protein level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B8JLM0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47538 MW; 808DCA55A32F5B95 CRC64;
MSSHKRPVRA RSDSDSSSSA PRDPIVAATE EGPSLLTRLM ELPVARLSRQ QLKRLEEHRY
SSEGRSLLEP FMQGFWCWLV SKVPLWMAPN LITIVGLATN IVSTLILVYY CPTATEQAPT
WAYLACALGL FIYQSLDAID GKQARRTNSS TPLGELFDHG CDSLSTVFVV LGTCIAVQLG
TYPDWMFFCC FVGIFMFYCA HWQTYVSGTL RFGIIDVTEV QIFIISMYLL AAIGGTAFWQ
SMIPVLNIQV KIIPALFTLL GAVFSCTNYF RVIFTGGMGK NGSTIAGTSV LSPSFHIGVV
ITLALMIYKK SSVQLFEKHP CLYVLAFGFV SAKLTNRLVV AHMTKSEMHR YDLAFTGPAL
LFLNQYFNSF INEYCLLWVA LVLSAFDLVR YCVSVCNQIA THLNIRVFSI QPPSPSRVQT
DGRNHH
//
