SGMS1

Phosphatidylcholine:ceramide cholinephosphotransferase 1 is an enzyme that in humans is encoded by the SGMS1 gene.[5][6][7]

SGMS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2D8C
Identifiers
Aliases	SGMS1, MOB, MOB1, SMS1, TMEM23, hmob33, sphingomyelin synthase 1
External IDs	OMIM: 611573 MGI: 2444110 HomoloGene: 27040 GeneCards: SGMS1
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q11.23 Start 50,305,586 bp[1] End 50,625,163 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19|19 C1 Start 32,122,727 bp[2] End 32,389,714 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • kinase activity • transferase activity • ceramide cholinephosphotransferase activity • sphingomyelin synthase activity • ceramide phosphoethanolamine synthase activity Cellular component • integral component of membrane • integral component of Golgi membrane • Golgi trans cisterna • Golgi membrane • cell membrane • Golgi apparatus • endoplasmic reticulum • cell nucleus • membrane • integral component of plasma membrane • integral component of endoplasmic reticulum membrane Biological process • lipid metabolism • sphingomyelin biosynthetic process • sphingolipid biosynthetic process • phosphorylation • apoptotic process • sphingolipid metabolic process • ceramide biosynthetic process • regulation of intrinsic apoptotic signaling pathway • inflammatory response • positive regulation of gene expression • cellular response to lipopolysaccharide • cellular response to tumor necrosis factor Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	259230	208449
Ensembl	ENSG00000198964	ENSMUSG00000040451
UniProt	Q86VZ5	Q8VCQ6
RefSeq (mRNA)	NM_147156	NM_001168525 NM_001168526 NM_144792 NM_001362423
RefSeq (protein)	NP_671512	NP_001161997 NP_001161998 NP_659041 NP_001349352
Location (UCSC)	Chr 10: 50.31 – 50.63 Mb	Chr 19: 32.12 – 32.39 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is predicted to be a five-pass transmembrane protein. This gene may be predominately expressed in brain.[7]

Model organisms

Model organisms have been used in the study of SGMS1 function. A conditional knockout mouse line called Sgms1^{tm1a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: - In-depth immunological phenotyping[14]

Sgms1 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[9][14]	Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Abnormal
Heart weight	Normal
Salmonella infection	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Trichuris Challenge	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000198964 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040451 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Vladychenskaya IP, Dergunova LV, Limborska SA (Feb 2002). "In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein". Biomolecular Engineering. 18 (6): 263–8. doi:10.1016/S1389-0344(01)00110-1. PMID 11841947.
6. Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T (Apr 2004). "Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells". The Journal of Biological Chemistry. 279 (18): 18688–93. doi:10.1074/jbc.M401205200. PMID 14976195.
7. "Entrez Gene: TMEM23 transmembrane protein 23".
8. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
9. "International Mouse Phenotyping Consortium".
10. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
11. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
12. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
13. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
14. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Albi E, Magni MV (Oct 1999). "Sphingomyelin synthase in rat liver nuclear membrane and chromatin". FEBS Letters. 460 (2): 369–72. doi:10.1016/S0014-5793(99)01378-2. PMID 10544266. S2CID 3025859.
• Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC (Jan 2004). "Identification of a family of animal sphingomyelin synthases". The EMBO Journal. 23 (1): 33–44. doi:10.1038/sj.emboj.7600034. PMC 1271672. PMID 14685263.
• Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA (Sep 2004). "Human gene MOB: structure specification and aspects of transcriptional activity". Gene. 338 (2): 257–65. doi:10.1016/j.gene.2004.06.003. PMID 15315829.
• Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC (Jun 2006). "Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice". Journal of Lipid Research. 47 (6): 1307–14. doi:10.1194/jlr.M600040-JLR200. PMID 16508036.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
• Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC (Jun 2007). "Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells". The Journal of Biological Chemistry. 282 (24): 17537–47. doi:10.1074/jbc.M702423200. PMID 17449912.
• Separovic D, Hanada K, Maitah MY, Nagy B, Hang I, Tainsky MA, Kraniak JM, Bielawski J (Jun 2007). "Sphingomyelin synthase 1 suppresses ceramide production and apoptosis post-photodamage". Biochemical and Biophysical Research Communications. 358 (1): 196–202. doi:10.1016/j.bbrc.2007.04.095. PMC 2701614. PMID 17467659.
• Li Z, Hailemariam TK, Zhou H, Li Y, Duckworth DC, Peake DA, Zhang Y, Kuo MS, Cao G, Jiang XC (Sep 2007). "Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1771 (9): 1186–94. doi:10.1016/j.bbalip.2007.05.007. PMC 2712822. PMID 17616479.