CPESY_DROME
ID CPESY_DROME Reviewed; 392 AA.
AC O77475;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ceramide phosphoethanolamine synthase {ECO:0000303|PubMed:23449981};
DE Short=CPE synthase {ECO:0000303|PubMed:23449981};
DE EC=2.7.8.n3;
GN Name=Cpes {ECO:0000303|PubMed:23449981, ECO:0000312|FlyBase:FBgn0025335};
GN ORFNames=CG4585 {ECO:0000312|FlyBase:FBgn0025335};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:BAA32689.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10191082; DOI=10.1006/geno.1999.5746;
RA Lukacsovich T., Asztalos Z., Juni N., Awano W., Yamamoto D.;
RT "The Drosophila melanogaster 60A chromosomal division is extremely dense
RT with functional genes: their sequences, genomic organization, and
RT expression.";
RL Genomics 57:43-56(1999).
RN [2] {ECO:0000312|EMBL:AAF47081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|EMBL:AAF47081.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAL28300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28300.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=23449981; DOI=10.1074/jbc.m113.460972;
RA Vacaru A.M., van den Dikkenberg J., Ternes P., Holthuis J.C.;
RT "Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a
RT unique ethanolamine phosphotransferase in the Golgi lumen.";
RL J. Biol. Chem. 288:11520-11530(2013).
CC -!- FUNCTION: Catalyzes the biosynthesis of ceramide phosphoethanolamine
CC (CPE) through the transfer of a phosphatidyl head group from cytidine
CC 5'-diphosphate (CDP)-ethanolamine on to the primary hydroxyl of
CC ceramide. {ECO:0000269|PubMed:23449981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + CDP-ethanolamine = an N-acylsphing-
CC 4-enine 1-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:45892,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52639, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73203; EC=2.7.8.n3;
CC Evidence={ECO:0000269|PubMed:23449981};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23449981};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23449981}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:23449981}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:23449981}. Cell membrane
CC {ECO:0000269|PubMed:23449981}. Note=The majority of protein localizes
CC to the Golgi apparatus. {ECO:0000269|PubMed:23449981}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AB010261; BAA32689.1; -; Genomic_DNA.
DR EMBL; AB010264; BAA32692.1; -; mRNA.
DR EMBL; AE013599; AAF47081.1; -; Genomic_DNA.
DR EMBL; AY060752; AAL28300.1; -; mRNA.
DR RefSeq; NP_001286788.1; NM_001299859.1.
DR RefSeq; NP_001286789.1; NM_001299860.1.
DR RefSeq; NP_001286790.1; NM_001299861.1.
DR RefSeq; NP_477376.1; NM_058028.5.
DR AlphaFoldDB; O77475; -.
DR BioGRID; 63375; 2.
DR STRING; 7227.FBpp0072136; -.
DR PaxDb; O77475; -.
DR PRIDE; O77475; -.
DR DNASU; 37782; -.
DR EnsemblMetazoa; FBtr0072227; FBpp0072136; FBgn0025335.
DR EnsemblMetazoa; FBtr0343275; FBpp0309940; FBgn0025335.
DR EnsemblMetazoa; FBtr0343276; FBpp0309941; FBgn0025335.
DR EnsemblMetazoa; FBtr0343277; FBpp0309942; FBgn0025335.
DR GeneID; 37782; -.
DR KEGG; dme:Dmel_CG4585; -.
DR UCSC; CG4585-RA; d. melanogaster.
DR CTD; 37782; -.
DR FlyBase; FBgn0025335; Cpes.
DR VEuPathDB; VectorBase:FBgn0025335; -.
DR eggNOG; ENOG502S0MB; Eukaryota.
DR HOGENOM; CLU_060194_0_0_1; -.
DR InParanoid; O77475; -.
DR OMA; HTNHYLF; -.
DR OrthoDB; 911658at2759; -.
DR PhylomeDB; O77475; -.
DR BioCyc; MetaCyc:MON-18328; -.
DR BRENDA; 2.7.8.B14; 1994.
DR BioGRID-ORCS; 37782; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37782; -.
DR PRO; PR:O77475; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0025335; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; O77475; baseline and differential.
DR Genevisible; O77475; DM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; IDA:FlyBase.
DR GO; GO:1905373; P:ceramide phosphoethanolamine biosynthetic process; IDA:FlyBase.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
PE 1: Evidence at protein level;
KW Cell membrane; Golgi apparatus; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid metabolism; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..392
FT /note="Ceramide phosphoethanolamine synthase"
FT /id="PRO_0000424382"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..212
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..319
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..392
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 59..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43858 MW; FCB6E1C454AF6140 CRC64;
MIGPSSQISK ILLTLLFLLI IFYVFMDVEL YLRIHNYAIE RNYHTNVSLP ASVVGPSTSE
SGSGSIGGSS SSSSSSSSST STKLPTAGDR QPSYEDHTWI SCDINPLCHV TVKAILLDHT
NHYLFAPLAT MFDNVIGFSR STFITPNMIS FFHVGVACLA GKLVASDSLG YRRLGVLLFQ
IRTFLDDLDG HVARVRKHIR GERSEIGTSG YYVDGLCDGL GCIALLLGIF FYLKNNPPRR
GYSIIPMSDS KLPEPTMMIP KMKATTRKVA KNVISFTGQL LLSSTAWNRY IAVYQNMLER
EDVSGNQSHC QDYVFKSTWF FCVAWMWRIV NVHALLHCVL LSIFCDKLWD FLRAIRYSGY
IILLVAICLT EMHILEAQNY IFNSTACSNI SL
