3-dehydrosphinganine reductase

3-dehydrosphinganine reductase
Identifiers
EC number	1.1.1.102
CAS number	37250-36-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

3-ketodihydrosphingosine reductase
Identifiers
Symbols	KDSR ; DHSR; FVT1; SDR35C1
External IDs	OMIM: 136440 MGI: 1918000 HomoloGene: 1539 GeneCards: KDSR Gene
EC number	1.1.1.102
Gene ontology Molecular function • 3-dehydrosphinganine reductase activity Cellular component • extracellular space • endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral component of membrane Biological process • sphingolipid metabolic process • 3-keto-sphinganine metabolic process • sphingolipid biosynthetic process • small molecule metabolic process • oxidation-reduction process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2531	70750
Ensembl	ENSG00000119537	ENSMUSG00000009905
UniProt	Q06136	Q6GV12
RefSeq (mRNA)	NM_002035	NM_027534
RefSeq (protein)	NP_002026	NP_081810
Location (UCSC)	Chr 18: 63.33 – 63.37 Mb	Chr 1: 106.72 – 106.76 Mb
PubMed search

3-dehydrosphinganine reductase (EC 1.1.1.102) also known as 3-ketodihydrosphingosine reductase (KDSR) or follicular variant translocation protein 1 (FVT1) is an enzyme that in humans is encoded by the KDSR gene.^{[1][2][3][4][5]}

Function

3-dehydrosphinganine reductase catalyzes the chemical reaction:

sphinganine + NADP⁺ $\rightleftharpoons$ 3-dehydrosphinganine + NADPH + H⁺

Thus, the two substrates of this enzyme are sphinganine and NADP⁺, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. This enzyme participates in sphingolipid metabolism.

Tissue distribution

Follicular lymphoma variant translocation 1 is a secreted protein which is weakly expressed in hematopoietic tissue.

Clinical significance

FVT1 shows a high rate of transcription in some T cell malignancies and in phytohemagglutinin-stimulated lymphocytes. The proximity of FVT1 to BCL2 suggests that it may participate in the tumoral process.^[5]

References

1. Rimokh R, Gadoux M, Bertheas MF, Berger F, Garoscio M, Deleage G, Germain D, Magaud JP (Feb 1993). "FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma". Blood 81 (1): 136–42. PMID 8417785.
2. Kihara A, Igarashi Y (Nov 2004). "FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane". J. Biol. Chem. 279 (47): 49243–50. doi:10.1074/jbc.M405915200. PMID 15328338.
3. Krebs S, Medugorac I, Rother S, Strasser K, Forster M (Apr 2007). "A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy". Proc. Natl. Acad. Sci. U.S.A. 104 (16): 6746–51. doi:10.1073/pnas.0607721104. PMC 1868895. PMID 17420465.
4. Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (Short-Chain Dehydrogenase/Reductase and Related Enzymes) Nomenclature Initiative". Chem. Biol. Interact. 178 (1–3): 94–8. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
5. "Entrez Gene: FVT1 follicular lymphoma variant translocation 1".

Further reading

• Quintero-Ramos A, Valdez-Vélázquez LL, Hernández G, et al. (2006). "[Assessment of five thrombophilic genetic polymorphisms among couples with habitual abortion]". Gaceta médica de México 142 (2): 95–8. PMID 16711541.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Wang J, Blakey GL, Zhang L, et al. (2004). "Uterine tumor resembling ovarian sex cord tumor: report of a case with t(X;6)(p22.3;q23.1) and t(4;18)(q21.1;q21.3)". Diagn. Mol. Pathol. 12 (3): 174–80. PMID 12960700.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Nacheva E, Dyer MJ, Metivier C, et al. (1994). "B-cell non-Hodgkin's lymphoma cell line (Karpas 1106) with complex translocation involving 18q21.3 but lacking BCL2 rearrangement and expression". Blood 84 (10): 3422–8. PMID 7949096.
• Stoffel W, LeKim D, Sticht G (1968). "Biosynthesis of dihydrosphingosine in vitro". Hoppe. Seylers. Z. Physiol. Chem. 349 (5): 664–70. doi:10.1515/bchm2.1968.349.1.664. PMID 4386961.
• Stoffel W, LeKim D, Sticht G (1968). "Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one)". Hoppe. Seylers. Z. Physiol. Chem. 349 (12): 1637–44. doi:10.1515/bchm2.1968.349.2.1637. PMID 4387676.