ID SMS1_HUMAN Reviewed; 413 AA. AC Q86VZ5; D3DWC4; Q68U43; Q6EKK0; Q75SP1; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 24-JAN-2024, entry version 171. DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1; DE EC=2.7.8.27 {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:14976195, ECO:0000269|PubMed:17449912, ECO:0000269|PubMed:17982138, ECO:0000269|PubMed:18370930}; DE AltName: Full=Medulla oblongata-derived protein; DE Short=Protein Mob; DE AltName: Full=Sphingomyelin synthase 1; DE AltName: Full=Transmembrane protein 23; GN Name=SGMS1; Synonyms=MOB, SMS1, TMEM23; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAH42899.1}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=14976195; DOI=10.1074/jbc.m401205200; RA Yamaoka S., Miyaji M., Kitano T., Umehara H., Okazaki T.; RT "Expression cloning of a human cDNA restoring sphingomyelin synthesis and RT cell growth in sphingomyelin synthase-defective lymphoid cells."; RL J. Biol. Chem. 279:18688-18693(2004). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP37279.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RA Yuan H.F., Wang X., Wang D.M., Li H.M., Feng K., Bai C.X., Zhang R., RA Chen L., Li Y.H., Gao Y.H., Zhen M., Yue W., Xie C., Xie X.Y., Niu L.L., RA Gao W.J., Zhang J., Cao H., Pei X.T.; RT "Complete cDNA sequence of a novel gene, human mob."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305, ECO:0000312|EMBL:AAP37279.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Zhao H., Miao S.Y., Zhang X.D., Liang G., Qiao Y., Wang L.F.; RT "A new spermatogenesis-related gene."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-290 (ISOFORM 2), IDENTIFICATION (ISOFORM RP 1), AND TISSUE SPECIFICITY. RC TISSUE=Cerebellum; RX PubMed=15315829; DOI=10.1016/j.gene.2004.06.003; RA Vladychenskaya I.P., Dergunova L.V., Dmitrieva V.G., Limborska S.A.; RT "Human gene MOB: structure specification and aspects of transcriptional RT activity."; RL Gene 338:257-265(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-277 (ISOFORM 1). RA Vladychenskaya I.P., Dergunova L.V., Limborska S.A., Dmitrieva V.G.; RT "Structure and functional organization of a novel human brain-specific gene RT MOB encoding a phylogenetically conserved transmembrane protein."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP IDENTIFICATION (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11841947; DOI=10.1016/s1389-0344(01)00110-1; RA Vladychenskaya I.P., Dergunova L.V., Limborska S.A.; RT "In vitro and in silico analysis of the predicted human MOB gene encoding a RT phylogenetically conserved transmembrane protein."; RL Biomol. Eng. 18:263-268(2002). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP ACTIVITY REGULATION, AND TOPOLOGY OF C-TERMINUS. 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 [12] RP OVEREXPRESSION IN MOUSE. RX PubMed=16508036; DOI=10.1194/jlr.m600040-jlr200; RA Dong J., Liu J., Lou B., Li Z., Ye X., Wu M., Jiang X.-C.; RT "Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 RT increases the atherogenic potential in mice."; RL J. Lipid Res. 47:1307-1314(2006). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=17449912; DOI=10.1074/jbc.m702423200; RA Tafesse F.G., Huitema K., Hermansson M., van der Poel S., RA van den Dikkenberg J., Uphoff A., Somerharju P., Holthuis J.C.M.; RT "Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin RT homeostasis and growth in human HeLa cells."; RL J. Biol. Chem. 282:17537-17547(2007). RN [14] RP ACTIVE SITES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-283; HIS-285; RP HIS-328 AND ASP-332. RX PubMed=18694848; DOI=10.1016/j.bbalip.2008.07.002; RA Yeang C., Varshney S., Wang R., Zhang Y., Ye D., Jiang X.C.; RT "The domain responsible for sphingomyelin synthase (SMS) activity."; RL Biochim. Biophys. Acta 1781:610-617(2008). RN [15] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18370930; DOI=10.1042/bj20071240; RA Villani M., Subathra M., Im Y.B., Choi Y., Signorelli P., Del Poeta M., RA Luberto C.; RT "Sphingomyelin synthases regulate production of diacylglycerol at the RT Golgi."; RL Biochem. J. 414:31-41(2008). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=17982138; DOI=10.1194/jlr.m700401-jlr200; RA Ding T., Li Z., Hailemariam T., Mukherjee S., Maxfield F.R., Wu M.P., RA Jiang X.C.; RT "SMS overexpression and knockdown: impact on cellular sphingomyelin and RT diacylglycerol metabolism, and cell apoptosis."; RL J. Lipid Res. 49:376-385(2008). RN [17] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19454763; DOI=10.1194/jlr.m900230-jlr200; RA Ternes P., Brouwers J.F., van den Dikkenberg J., Holthuis J.C.; RT "Sphingomyelin synthase SMS2 displays dual activity as ceramide RT phosphoethanolamine synthase."; RL J. Lipid Res. 50:2270-2277(2009). RN [18] RP FUNCTION. RX PubMed=21980337; DOI=10.1371/journal.pone.0023644; RA Subathra M., Qureshi A., Luberto C.; RT "Sphingomyelin synthases regulate protein trafficking and secretion."; RL PLoS ONE 6:e23644-e23644(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Major sphingomyelin synthase at the Golgi apparatus CC (PubMed:17449912, PubMed:14685263). Catalyzes the reversible transfer CC of phosphocholine moiety in sphingomyelin biosynthesis: in the forward CC reaction transfers phosphocholine head group of phosphatidylcholine CC (PC) on to ceramide (CER) to form ceramide phosphocholine CC (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the CC reverse reaction transfers phosphocholine from SM to DAG to form PC and CC CER. The direction of the reaction depends on the levels of CER and DAG CC in Golgi membranes (PubMed:14685263, PubMed:17449912, PubMed:14976195, CC PubMed:17982138, PubMed:19454763). Does not use free phosphorylcholine CC or CDP-choline as donor (PubMed:14976195, PubMed:14685263). Regulates CC 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:14976195, PubMed:17449912, PubMed:17982138). Plays a CC role in secretory transport via regulation of DAG pool at the Golgi CC apparatus and its downstream effects on PRKD1 (PubMed:18370930, CC PubMed:21980337). {ECO:0000269|PubMed:14685263, CC ECO:0000269|PubMed:14976195, ECO:0000269|PubMed:17449912, CC ECO:0000269|PubMed:17982138, ECO:0000269|PubMed:18370930, CC ECO:0000269|PubMed:19454763, ECO:0000269|PubMed:21980337}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4- CC enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin; 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:14685263, ECO:0000269|PubMed:14976195, CC ECO:0000269|PubMed:17449912, ECO:0000269|PubMed:17982138, CC ECO:0000269|PubMed:18370930}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766; CC Evidence={ECO:0000305|PubMed:14685263, ECO:0000305|PubMed:14976195, CC ECO:0000305|PubMed:17449912, ECO:0000305|PubMed:17982138, CC ECO:0000305|PubMed:18370930}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767; CC Evidence={ECO:0000305|PubMed:14685263}; 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:0000269|PubMed:14685263}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321; CC Evidence={ECO:0000305|PubMed:14685263}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322; CC Evidence={ECO:0000305|PubMed:14685263}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N- CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl- CC sphinganine-1-phosphocholine; Xref=Rhea:RHEA:41796, CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:67042, CC ChEBI:CHEBI:78647; Evidence={ECO:0000269|PubMed:19454763}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797; CC Evidence={ECO:0000305|PubMed:19454763}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798; CC Evidence={ECO:0000305|PubMed:14685263}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-hexadecanoyl- CC (4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl- CC (4R)-hydroxysphinganine-phosphocholine; Xref=Rhea:RHEA:42140, CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:65107, CC ChEBI:CHEBI:78650; Evidence={ECO:0000269|PubMed:19454763}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141; CC Evidence={ECO:0000305|PubMed:19454763}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142; CC Evidence={ECO:0000305|PubMed:14685263}; CC -!- ACTIVITY REGULATION: Inhibited by bacterial PC-phospholipase C CC inhibitor D609. {ECO:0000269|PubMed:14685263}. CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:17982138}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:17449912, CC ECO:0000269|PubMed:18694848}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q86VZ5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86VZ5-2; Sequence=VSP_027223, VSP_027224; CC -!- TISSUE SPECIFICITY: Brain, heart, kidney, liver, muscle and stomach. CC {ECO:0000269|PubMed:11841947, ECO:0000269|PubMed:14685263, CC ECO:0000269|PubMed:15315829}. CC -!- MISCELLANEOUS: Overexpression of the human protein in mouse causes CC increased non-HDL-sphingomyelin and non-HDL cholesterol levels, CC decreased HDL-sphingomyelin and HDL-cholesterol levels and increases CC the atherogenic potential of non-HDL lipoprotein particles. 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; AB154421; BAD16809.1; -; mRNA. DR EMBL; AY280959; AAP37279.1; -; mRNA. DR EMBL; AY312431; AAQ82051.1; -; mRNA. DR EMBL; AK026683; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH471142; EAW80430.1; -; Genomic_DNA. DR EMBL; CH471142; EAW80429.1; -; Genomic_DNA. DR EMBL; CH471142; EAW80431.1; -; Genomic_DNA. DR EMBL; CH471142; EAW80432.1; -; Genomic_DNA. DR EMBL; AC069547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117341; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL596137; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC042899; AAH42899.1; -; mRNA. DR EMBL; AY364088; AAR13294.1; -; mRNA. DR EMBL; AY332650; AAQ22363.1; -; mRNA. DR EMBL; BN000143; CAD79708.1; -; mRNA. DR CCDS; CCDS7240.1; -. [Q86VZ5-1] DR RefSeq; NP_671512.1; NM_147156.3. [Q86VZ5-1] DR RefSeq; XP_005269732.1; XM_005269675.1. [Q86VZ5-1] DR RefSeq; XP_011537884.1; XM_011539582.2. DR RefSeq; XP_011537885.1; XM_011539583.2. [Q86VZ5-1] DR AlphaFoldDB; Q86VZ5; -. DR SMR; Q86VZ5; -. DR BioGRID; 129227; 16. DR IntAct; Q86VZ5; 1. DR STRING; 9606.ENSP00000354829; -. DR BindingDB; Q86VZ5; -. DR ChEMBL; CHEMBL3611965; -. DR GuidetoPHARMACOLOGY; 2520; -. DR SwissLipids; SLP:000000171; -. DR iPTMnet; Q86VZ5; -. DR PhosphoSitePlus; Q86VZ5; -. DR BioMuta; SGMS1; -. DR DMDM; 44888473; -. DR EPD; Q86VZ5; -. DR jPOST; Q86VZ5; -. DR MassIVE; Q86VZ5; -. DR MaxQB; Q86VZ5; -. DR PaxDb; 9606-ENSP00000354829; -. DR PeptideAtlas; Q86VZ5; -. DR ProteomicsDB; 12771; -. DR ProteomicsDB; 70096; -. [Q86VZ5-1] DR ProteomicsDB; 70097; -. [Q86VZ5-2] DR Pumba; Q86VZ5; -. DR Antibodypedia; 27870; 223 antibodies from 25 providers. DR DNASU; 259230; -. DR Ensembl; ENST00000361781.7; ENSP00000354829.2; ENSG00000198964.14. [Q86VZ5-1] DR GeneID; 259230; -. DR KEGG; hsa:259230; -. DR MANE-Select; ENST00000361781.7; ENSP00000354829.2; NM_147156.4; NP_671512.1. DR UCSC; uc001jje.4; human. DR AGR; HGNC:29799; -. DR CTD; 259230; -. DR DisGeNET; 259230; -. DR GeneCards; SGMS1; -. DR HGNC; HGNC:29799; SGMS1. DR HPA; ENSG00000198964; Low tissue specificity. DR MIM; 611573; gene. DR neXtProt; NX_Q86VZ5; -. DR OpenTargets; ENSG00000198964; -. DR PharmGKB; PA162403042; -. DR VEuPathDB; HostDB:ENSG00000198964; -. DR eggNOG; KOG3058; Eukaryota. DR GeneTree; ENSGT00940000158306; -. DR InParanoid; Q86VZ5; -. DR OMA; WICWTLS; -. DR OrthoDB; 1343173at2759; -. DR PhylomeDB; Q86VZ5; -. DR TreeFam; TF314547; -. DR BRENDA; 2.7.8.27; 2681. DR PathwayCommons; Q86VZ5; -. DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis. DR SignaLink; Q86VZ5; -. DR BioGRID-ORCS; 259230; 34 hits in 1158 CRISPR screens. DR ChiTaRS; SGMS1; human. DR GeneWiki; SGMS1; -. DR GenomeRNAi; 259230; -. DR Pharos; Q86VZ5; Tchem. DR PRO; PR:Q86VZ5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q86VZ5; Protein. DR Bgee; ENSG00000198964; Expressed in adrenal tissue and 204 other cell types or tissues. DR ExpressionAtlas; Q86VZ5; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:HGNC-UCL. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0000138; C:Golgi trans cisterna; IDA:MGI. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; TAS:HGNC-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:HGNC-UCL. DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IDA:UniProtKB. DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; IDA:MGI. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; TAS:HGNC-UCL. DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome. DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IDA:UniProtKB. DR CDD; cd01610; PAP2_like; 1. DR CDD; cd09514; SAM_SGMS1; 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. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Golgi apparatus; Kinase; Lipid metabolism; KW Membrane; Phosphoprotein; Reference proteome; Sphingolipid metabolism; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..413 FT /note="Phosphatidylcholine:ceramide FT cholinephosphotransferase 1" FT /id="PRO_0000221068" FT TRANSMEM 136..156 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 215..235 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 276..296 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 325..413 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 7..70 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184, FT ECO:0000305" FT ACT_SITE 285 FT /evidence="ECO:0000269|PubMed:18694848" FT ACT_SITE 328 FT /evidence="ECO:0000269|PubMed:18694848" FT ACT_SITE 332 FT /evidence="ECO:0000269|PubMed:18694848" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..199 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15315829" FT /id="VSP_027223" FT VAR_SEQ 200..208 FT /note="IQWLLLKYK -> MTRMFLNNP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15315829" FT /id="VSP_027224" FT MUTAGEN 283 FT /note="S->A: Completely abolishes enzyme activity. No FT change in subcellular location." FT /evidence="ECO:0000269|PubMed:18694848" FT MUTAGEN 285 FT /note="H->A: Completely abolishes enzyme activity. No FT change in subcellular location." FT /evidence="ECO:0000269|PubMed:18694848" FT MUTAGEN 328 FT /note="H->A: Completely abolishes enzyme activity. No FT change in subcellular location." FT /evidence="ECO:0000269|PubMed:18694848" FT MUTAGEN 332 FT /note="D->A: Completely abolishes enzyme activity. No FT change in subcellular location." FT /evidence="ECO:0000269|PubMed:18694848" FT CONFLICT 162 FT /note="P -> L (in Ref. 3; AAQ82051)" FT /evidence="ECO:0000305" SQ SEQUENCE 413 AA; 48617 MW; 6E79AED84F4BFD21 CRC64; MKEVVYWSPK KVADWLLENA MPEYCEPLEH FTGQDLINLT QEDFKKPPLC RVSSDNGQRL LDMIETLKME HHLEAHKNGH ANGHLNIGVD IPTPDGSFSI KIKPNGMPNG YRKEMIKIPM PELERSQYPM EWGKTFLAFL YALSCFVLTT VMISVVHERV PPKEVQPPLP DTFFDHFNRV QWAFSICEIN GMILVGLWLI QWLLLKYKSI ISRRFFCIVG TLYLYRCITM YVTTLPVPGM HFNCSPKLFG DWEAQLRRIM KLIAGGGLSI TGSHNMCGDY LYSGHTVMLT LTYLFIKEYS PRRLWWYHWI CWLLSVVGIF CILLAHDHYT VDVVVAYYIT TRLFWWYHTM ANQQVLKEAS QMNLLARVWW YRPFQYFEKN VQGIVPRSYH WPFPWPVVHL SRQVKYSRLV NDT //