SMS1_HUMAN
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 03-AUG-2022, entry version 163.
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}.
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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; 2.
DR STRING; 9606.ENSP00000354829; -.
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; Q86VZ5; -.
DR PeptideAtlas; Q86VZ5; -.
DR PRIDE; Q86VZ5; -.
DR ProteomicsDB; 12771; -.
DR ProteomicsDB; 70096; -. [Q86VZ5-1]
DR ProteomicsDB; 70097; -. [Q86VZ5-2]
DR Antibodypedia; 27870; 206 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 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; 599210at2759; -.
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; 30 hits in 1078 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 202 other tissues.
DR ExpressionAtlas; Q86VZ5; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:HGNC-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Gene3D; 1.10.150.50; -; 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; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
DR SUPFAM; SSF47769; SSF47769; 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
