ID SMS1_MOUSE Reviewed; 419 AA. AC Q8VCQ6; Q3UIS8; Q5J3R0; Q8C464; Q8C583; Q8C652; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 02-SEP-2026, entry version 180. DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1; DE EC=2.7.8.27 {ECO:0000269|PubMed:27892528}; DE AltName: Full=Protein Mob; DE AltName: Full=Sphingomyelin synthase 1; DE AltName: Full=Transmembrane protein 23; GN Name=Sgms1; Synonyms=Tmem23; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND RP INDUCTION. RC STRAIN=BALB/cJ; RX PubMed=16226406; DOI=10.1016/j.gene.2005.07.036; RA Yang Z., Jean-Baptiste G., Khoury C., Greenwood M.T.; RT "The mouse sphingomyelin synthase 1 (SMS1) gene is alternatively spliced to RT yield multiple transcripts and proteins."; RL Gene 363:123-132(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow macrophage, Embryo, Embryonic heart, Embryonic RC spinal cord, Embryonic stem cell, Testis, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and FVB/N; RC TISSUE=Kidney {ECO:0000269|PubMed:15489334}, and Olfactory epithelium; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION. RX PubMed=14685263; DOI=10.1038/sj.emboj.7600034; RA Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.; RT "Identification of a family of animal sphingomyelin synthases."; RL EMBO J. 23:33-44(2004). RN [5] RP FUNCTION. RX PubMed=16879426; DOI=10.1111/j.1567-1364.2006.00052.x; RA Yang Z., Khoury C., Jean-Baptiste G., Greenwood M.T.; RT "Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax- RT mediated cell death in yeast."; RL FEMS Yeast Res. 6:751-762(2006). RN [6] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=22580896; DOI=10.1161/atvbaha.112.251538; RA Li Z., Fan Y., Liu J., Li Y., Huan C., Bui H.H., Kuo M.S., Park T.S., RA Cao G., Jiang X.C.; RT "Impact of sphingomyelin synthase 1 deficiency on sphingolipid metabolism RT and atherosclerosis in mice."; RL Arterioscler. Thromb. Vasc. Biol. 32:1577-1584(2012). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=22641779; DOI=10.1113/jphysiol.2012.235846; RA Lu M.H., Takemoto M., Watanabe K., Luo H., Nishimura M., Yano M., RA Tomimoto H., Okazaki T., Oike Y., Song W.J.; RT "Deficiency of sphingomyelin synthase-1 but not sphingomyelin synthase-2 RT causes hearing impairments in mice."; RL J. Physiol. (Lond.) 590:4029-4044(2012). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25605874; DOI=10.1194/jlr.m054627; RA Ding T., Kabir I., Li Y., Lou C., Yazdanyar A., Xu J., Dong J., Zhou H., RA Park T., Boutjdir M., Li Z., Jiang X.C.; RT "All members in the sphingomyelin synthase gene family have ceramide RT phosphoethanolamine synthase activity."; RL J. Lipid Res. 56:537-545(2015). RN [9] RP FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=27892528; DOI=10.1038/srep37829; RA Taniguchi M., Tasaki T., Ninomiya H., Ueda Y., Kuremoto K.I., Mitsutake S., RA Igarashi Y., Okazaki T., Takegami T.; RT "Sphingomyelin generated by sphingomyelin synthase 1 is involved in RT attachment and infection with Japanese encephalitis virus."; RL Sci. Rep. 6:37829-37829(2016). RN [10] RP STRUCTURE BY NMR OF 1-84. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SAM-domain of mouse phosphatidyl RT ceramidecholinephosphotransferase 1."; RL Submitted (JUN-2006) to the PDB data bank. CC -!- FUNCTION: Major sphingomyelin synthase at the Golgi apparatus. CC Catalyzes the reversible transfer of phosphocholine moiety in CC sphingomyelin biosynthesis: in the forward reaction transfers CC phosphocholine head group of phosphatidylcholine (PC) on to ceramide CC (CER) to form ceramide phosphocholine (sphingomyelin, SM) and CC diacylglycerol (DAG) as by-product, and in the reverse reaction CC transfers phosphocholine from SM to DAG to form PC and CER. The CC direction of the reaction depends on the levels of CER and DAG in Golgi CC membranes. Converts the newly synthesized CER, that is transported from CC the endoplasmic reticulum to the trans-Golgi by the Cer transport CC protein (CERT), to SM. Can form a heteromeric complex with CC glucosylceramide synthase (GCS) increasing SMS activity and reducing CC glucosylceramide synthesis, a critical mechanism that controls the CC metabolic fate of CER in the Golgi (By similarity). Does not use free CC phosphorylcholine or CDP-choline as donor. Can also transfer CC phosphoethanolamine head group of phosphatidylethanolamine (PE) on to CC CER to form ceramide phosphoethanolamine (CPE) (PubMed:25605874). CC Regulates receptor-mediated signal transduction via mitogenic DAG and CC proapoptotic CER, as well as via SM, a structural component of membrane CC rafts that serve as platforms for signal transduction and protein CC sorting (PubMed:16879426, PubMed:22580896). Plays a role in secretory CC transport via regulation of DAG pool at the Golgi apparatus and its CC downstream effects on PRKD1 (By similarity). CC {ECO:0000250|UniProtKB:Q86VZ5, ECO:0000269|PubMed:16879426, CC ECO:0000269|PubMed:22580896, ECO:0000269|PubMed:25605874}. CC -!- FUNCTION: (Microbial infection) Contributes to the brain SM production CC for Japanese encephalitis virus attachment and infection. CC {ECO:0000269|PubMed:27892528}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acylsphing-4-enine + a 1,2-diacyl-sn-glycero-3- CC phosphocholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol; CC Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815, CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27; CC Evidence={ECO:0000269|PubMed:27892528}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766; CC Evidence={ECO:0000305|PubMed:27892528}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-2-acyl-sn-3-glycerol + a sphingomyelin = a CC 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + an N- CC acylsphing-4-enine; Xref=Rhea:RHEA:43320, ChEBI:CHEBI:17636, CC ChEBI:CHEBI:52639, ChEBI:CHEBI:78421, ChEBI:CHEBI:82983; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-hexadecanoylsphinganine + a 1,2-diacyl-sn-glycero-3- CC phosphocholine = N-hexadecanoyl-sphinganine-1-phosphocholine + a 1,2- CC diacyl-sn-glycerol; Xref=Rhea:RHEA:41796, ChEBI:CHEBI:17815, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:67042, ChEBI:CHEBI:78647; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-hexadecanoyl-(4R)-hydroxysphinganine + a 1,2-diacyl-sn- CC glycero-3-phosphocholine = N-hexadecanoyl-(4R)-hydroxysphinganine- CC phosphocholine + a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:42140, CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:65107, CC ChEBI:CHEBI:78650; Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142; CC Evidence={ECO:0000250|UniProtKB:Q86VZ5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acylsphing-4-enine + a 1,2-diacyl-sn-glycero-3- CC phosphoethanolamine = an N-acylsphing-4-enine 1-phosphoethanolamine + CC a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:36079, ChEBI:CHEBI:17815, CC ChEBI:CHEBI:52639, ChEBI:CHEBI:64612, ChEBI:CHEBI:73203; CC Evidence={ECO:0000269|PubMed:25605874}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36080; CC Evidence={ECO:0000269|PubMed:25605874}; CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:27892528}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:Q86VZ5}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=SMS1-alpha; CC IsoId=Q8VCQ6-1; Sequence=Displayed; CC Name=2; Synonyms=SMS1-beta; CC IsoId=Q8VCQ6-2; Sequence=VSP_050673; CC Name=3; Synonyms=SMS1-gamma; CC IsoId=Q8VCQ6-3; Sequence=VSP_027225, VSP_027226; CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed, isoform 2 shows a CC more narrow distribution and isoform 3 is detected only in testis and CC heart. {ECO:0000269|PubMed:16226406}. CC -!- INDUCTION: [Isoform 1]: Induced by TNF. {ECO:0000269|PubMed:16226406}. CC -!- INDUCTION: [Isoform 2]: Induced by TNF. {ECO:0000269|PubMed:16226406}. CC -!- DISRUPTION PHENOTYPE: Null mice have hearing impairments with stria CC vascularis (SV) in these mice exhibiting atrophy and disorganized CC marginal cells resulting in significantly smaller endocochlear CC potentials (EPs). These decreased EPs, together with abnormal KCNQ1 CC expression patterns, increase with age. There is a decrease in plasma, CC liver, and macrophage sphingomyelin (59%, 45%, and 54%, respectively) CC and a dramatic increase in glycosphingolipids. No change in ceramide, CC total cholesterol, phospholipids nor triglycerides levels. Diminished CC macrophage MAP kinase and NFKB1 activation is observed. Atherosclerosis CC in SMS1(-/-)/LDLR(-/-) mice is significantly decreased. CC {ECO:0000269|PubMed:22580896, ECO:0000269|PubMed:22641779}. CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY509044; AAS90514.1; -; mRNA. DR EMBL; AK076554; BAC36390.1; -; mRNA. DR EMBL; AK079254; BAC37590.1; -; mRNA. DR EMBL; AK082974; BAC38717.1; -; mRNA. DR EMBL; AK133967; BAE21960.1; -; mRNA. DR EMBL; AK146782; BAE27428.1; -; mRNA. DR EMBL; AK150272; BAE29428.1; -; mRNA. DR EMBL; AK151170; BAE30173.1; -; mRNA. DR EMBL; AK152312; BAE31117.1; -; mRNA. DR EMBL; AK153406; BAE31966.1; -; mRNA. DR EMBL; AK160539; BAE35856.1; -; mRNA. DR EMBL; BC019443; AAH19443.2; -; mRNA. DR EMBL; BC085298; AAH85298.1; -; mRNA. DR CCDS; CCDS29750.1; -. [Q8VCQ6-1] DR RefSeq; NP_001161997.1; NM_001168525.1. [Q8VCQ6-1] DR RefSeq; NP_001161998.1; NM_001168526.1. [Q8VCQ6-1] DR RefSeq; NP_001349352.1; NM_001362423.1. [Q8VCQ6-1] DR RefSeq; NP_659041.3; NM_144792.5. [Q8VCQ6-1] DR RefSeq; XP_006526881.1; XM_006526818.5. [Q8VCQ6-1] DR RefSeq; XP_006526882.1; XM_006526819.3. [Q8VCQ6-1] DR RefSeq; XP_006526883.1; XM_006526820.5. [Q8VCQ6-1] DR RefSeq; XP_011245504.1; XM_011247202.3. [Q8VCQ6-1] DR RefSeq; XP_011245505.1; XM_011247203.3. [Q8VCQ6-1] DR RefSeq; XP_017173594.1; XM_017318105.3. [Q8VCQ6-3] DR RefSeq; XP_030106691.1; XM_030250831.2. [Q8VCQ6-1] DR RefSeq; XP_030106692.1; XM_030250832.1. [Q8VCQ6-1] DR RefSeq; XP_030106693.1; XM_030250833.2. [Q8VCQ6-1] DR RefSeq; XP_030106695.1; XM_030250835.1. [Q8VCQ6-1] DR RefSeq; XP_030106696.1; XM_030250836.2. [Q8VCQ6-1] DR RefSeq; XP_030106697.1; XM_030250837.1. [Q8VCQ6-1] DR PDB; 2D8C; NMR; -; A=1-84. DR AlphaFoldDB; Q8VCQ6; -. DR SMR; Q8VCQ6; -. DR BioGRID; 228984; 2. DR FunCoup; Q8VCQ6; 2509. DR STRING; 10090.ENSMUSP00000117336; -. DR BindingDB; Q8VCQ6; -. DR ChEMBL; CHEMBL4523408; -. DR PhosphoSitePlus; Q8VCQ6; -. DR PaxDb; 10090-ENSMUSP00000117336; -. DR ProteomicsDB; 261459; -. [Q8VCQ6-1] DR ProteomicsDB; 261460; -. [Q8VCQ6-2] DR ProteomicsDB; 261461; -. [Q8VCQ6-3] DR Antibodypedia; 27870; 205 antibodies from 26 providers. DR DNASU; 208449; -. DR Ensembl; ENSMUST00000099514.10; ENSMUSP00000097114.4; ENSMUSG00000040451.19. [Q8VCQ6-1] DR Ensembl; ENSMUST00000142618.8; ENSMUSP00000117336.2; ENSMUSG00000040451.19. [Q8VCQ6-1] DR Ensembl; ENSMUST00000151289.9; ENSMUSP00000123395.2; ENSMUSG00000040451.19. [Q8VCQ6-1] DR Ensembl; ENSMUST00000152340.8; ENSMUSP00000119869.2; ENSMUSG00000040451.19. [Q8VCQ6-3] DR GeneID; 208449; -. DR KEGG; mmu:208449; -. DR UCSC; uc008hfc.2; mouse. [Q8VCQ6-1] DR UCSC; uc008hfh.1; mouse. [Q8VCQ6-2] DR AGR; MGI:2444110; -. DR CTD; 259230; -. DR MGI; MGI:2444110; Sgms1. DR VEuPathDB; HostDB:ENSMUSG00000040451; -. DR eggNOG; KOG3058; Eukaryota. DR GeneTree; ENSGT00940000158306; -. DR HOGENOM; CLU_027104_1_0_1; -. DR InParanoid; Q8VCQ6; -. DR OMA; HWPLRCP; -. DR OrthoDB; 422827at2759; -. DR PhylomeDB; Q8VCQ6; -. DR BRENDA; 2.7.8.27; 3474. DR BRENDA; 2.7.8.48; 3474. DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis. DR BioGRID-ORCS; 208449; 10 hits in 80 CRISPR screens. DR EvolutionaryTrace; Q8VCQ6; -. DR PRO; PR:Q8VCQ6; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q8VCQ6; protein. DR Bgee; ENSMUSG00000040451; Expressed in spermatid and 257 other cell types or tissues. DR ExpressionAtlas; Q8VCQ6; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:HGNC-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI. DR GO; GO:1990676; C:Golgi trans cisterna membrane; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; TAS:HGNC-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISS:UniProtKB. DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; IMP:MGI. DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:MGI. DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IMP:MGI. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central. DR GO; GO:0046317; P:regulation of glucosylceramide biosynthetic process; ISO:GO_Central. DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:UniProtKB. DR CDD; cd01610; PAP2_like; 1. DR CDD; cd09514; SAM_SGMS1; 1. DR FunFam; 1.10.150.50:FF:000040; Phosphatidylcholine:ceramide cholinephosphotransferase 1; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR045221; Sphingomyelin_synth-like. DR InterPro; IPR025749; Sphingomyelin_synth-like_dom. DR PANTHER; PTHR21290:SF28; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 1; 1. DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1. DR Pfam; PF14360; PAP2_C; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PDBsum; 2D8C; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Golgi apparatus; Kinase; KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..419 FT /note="Phosphatidylcholine:ceramide FT cholinephosphotransferase 1" FT /id="PRO_0000221069" FT TOPO_DOM 1..141 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 142..162 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 163..189 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 190..210 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 211..220 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 242..281 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 282..302 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 303..309 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 331..335 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT TRANSMEM 336..353 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 354..419 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT DOMAIN 13..76 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184, FT ECO:0000305" FT ACT_SITE 291 FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT ACT_SITE 334 FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT ACT_SITE 338 FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q86VZ5" FT VAR_SEQ 215..419 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16226406" FT /id="VSP_050673" FT VAR_SEQ 215..217 FT /note="SII -> LSP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16226406" FT /id="VSP_027225" FT VAR_SEQ 218..419 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:16226406" FT /id="VSP_027226" FT CONFLICT 132 FT /note="S -> Y (in Ref. 2; BAC37590)" FT /evidence="ECO:0000305" FT CONFLICT 406 FT /note="L -> I (in Ref. 2; BAE27428)" FT /evidence="ECO:0000305" FT HELIX 17..24 FT /evidence="ECO:0007829|PDB:2D8C" FT TURN 28..36 FT /evidence="ECO:0007829|PDB:2D8C" FT HELIX 39..43 FT /evidence="ECO:0007829|PDB:2D8C" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:2D8C" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:2D8C" FT TURN 60..63 FT /evidence="ECO:0007829|PDB:2D8C" FT HELIX 64..76 FT /evidence="ECO:0007829|PDB:2D8C" SQ SEQUENCE 419 AA; 49317 MW; 554CC26609F5F345 CRC64; MLSARTMKEV VYWSPKKVAD WLLENAMPEY CEPLEHFTGQ DLINLTQEDF KKPPLYRVSS DNGQRLLDMI ETLKMEHHME AHKNGHANGH LSIGVDIPNP DGSFSIKTKP NGMPNGFRKE MIKIPMPEPE RSQYPMEWGK TFLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYKSIISRR FFCIVGTLYL YRCITMYVTT LPVPGMHFNC SPKLFGDWEA QVRRIMKLIA GGGLSITGSH NMCGDYLYSG HTVMLTLTYL FIKEYSPRRL WWYHWICWLL SVVGIFCILL AHDHYTVDVV VAYYITTRLF WWYHTMANQQ VLKEASQMNL LARVWWYRPF QYFEKNVQGI VPRSYHWPFP WPVVHLSRQV KYSRLVNDT //