Glycerol-3-phosphate dehydrogenase 1

Glycerol-3-phosphate dehydrogenase 1 is a protein that in humans is encoded by the GPD1 gene.[5]

GPD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WPQ, 1X0V, 1X0X
Identifiers
Aliases	GPD1, GPD-C, GPDH-C, HTGTI, glycerol-3-phosphate dehydrogenase 1
External IDs	OMIM: 138420 MGI: 95679 HomoloGene: 5593 GeneCards: GPD1
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.12 Start 50,103,982 bp[1] End 50,111,313 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 F1|15 56.13 cM Start 99,717,515 bp[2] End 99,725,005 bp[2]
Gene ontology Molecular function • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor • protein homodimerization activity • NAD binding • glycerol-3-phosphate dehydrogenase [NAD+ activity] • oxidoreductase activity • glycerol-3-phosphate dehydrogenase (quinone) activity • GO:0036439 glycerol-3-phosphate dehydrogenase [NAD(P)+ activity] Cellular component • cytoplasm • cytosol • glycerol-3-phosphate dehydrogenase complex • mitochondrion • extracellular exosome Biological process • phosphatidic acid biosynthetic process • glycerolipid metabolic process • gluconeogenesis • glycerol-3-phosphate catabolic process • cellular response to tumor necrosis factor • glycerol-3-phosphate metabolic process • NADH metabolic process • NADH oxidation • oxidation-reduction process • glycerophosphate shuttle • positive regulation of glycolytic process • cellular response to cAMP • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2819	14555
Ensembl	ENSG00000167588	ENSMUSG00000023019
UniProt	P21695	P13707
RefSeq (mRNA)	NM_005276 NM_001257199	NM_010271
RefSeq (protein)	NP_001244128 NP_005267	NP_034401
Location (UCSC)	Chr 12: 50.1 – 50.11 Mb	Chr 15: 99.72 – 99.73 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. The encoded protein plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of dihydroxyacetone phosphate (DHAP) and reduced nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+.

The encoded cytosolic protein and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria.

Mutations in this gene are a cause of transient infantile hypertriglyceridemia. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.

References

1. GRCh38: Ensembl release 89: ENSG00000167588 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023019 - 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. "Entrez Gene: Glycerol-3-phosphate dehydrogenase 1". Retrieved 2017-03-23.

Further reading

• Gudayol M, Vidal J, Usac EF, Morales A, Fabregat ME, Fernández-Checa JC, Novials A, Gomis R (2001). "Identification and functional analysis of mutations in FAD-binding domain of mitochondrial glycerophosphate dehydrogenase in caucasian patients with type 2 diabetes mellitus". Endocrine. 16 (1): 39–42. doi:10.1385/ENDO:16:1:39. PMID 11822825.
• Swierczynski J, Zabrocka L, Goyke E, Raczynska S, Adamonis W, Sledzinski Z (2003). "Enhanced glycerol 3-phosphate dehydrogenase activity in adipose tissue of obese humans". Mol. Cell. Biochem. 254 (1–2): 55–9. PMID 14674682.
• Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z (2006). "Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)". J. Mol. Biol. 357 (3): 858–69. doi:10.1016/j.jmb.2005.12.074. PMID 16460752.
• Park JJ, Berggren JR, Hulver MW, Houmard JA, Hoffman EP (2006). "GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle". Physiol. Genomics. 27 (2): 114–21. doi:10.1152/physiolgenomics.00045.2006. PMID 16849634.
• MacDonald MJ, Longacre MJ, Langberg EC, Tibell A, Kendrick MA, Fukao T, Ostenson CG (2009). "Decreased levels of metabolic enzymes in pancreatic islets of patients with type 2 diabetes". Diabetologia. 52 (6): 1087–91. doi:10.1007/s00125-009-1319-6. PMC 2903059. PMID 19296078.
• Krasnov GS, Oparina NIu, Khankin SL, Mashkova TD, Ershov AN, Zatsepina OG, Karpov VL, Beresten' SF (2009). "[Colorectal cancer 2D-proteomics: identification of altered protein expression]". Mol. Biol. (Mosk.) (in Russian). 43 (2): 348–56. PMID 19425502.
• Guindalini C, Lee KS, Andersen ML, Santos-Silva R, Bittencourt LR, Tufik S (2010). "The influence of obstructive sleep apnea on the expression of glycerol-3-phosphate dehydrogenase 1 gene". Exp. Biol. Med. (Maywood). 235 (1): 52–6. doi:10.1258/ebm.2009.009150. PMID 20404019.
• Basel-Vanagaite L, Zevit N, Har Zahav A, Guo L, Parathath S, Pasmanik-Chor M, McIntyre AD, Wang J, Albin-Kaplanski A, Hartman C, Marom D, Zeharia A, Badir A, Shoerman O, Simon AJ, Rechavi G, Shohat M, Hegele RA, Fisher EA, Shamir R (2012). "Transient infantile hypertriglyceridemia, fatty liver, and hepatic fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate dehydrogenase 1". Am. J. Hum. Genet. 90 (1): 49–60. doi:10.1016/j.ajhg.2011.11.028. PMC 3257852. PMID 22226083.
• Joshi M, Eagan J, Desai NK, Newton SA, Towne MC, Marinakis NS, Esteves KM, De Ferranti S, Bennett MJ, McIntyre A, Beggs AH, Berry GT, Agrawal PB (2014). "A compound heterozygous mutation in GPD1 causes hepatomegaly, steatohepatitis, and hypertriglyceridemia". Eur. J. Hum. Genet. 22 (10): 1229–32. doi:10.1038/ejhg.2014.8. PMC 4169545. PMID 24549054.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.