Glycerol-3-phosphate dehydrogenase 1

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) Band 12q13.12 Start 50,103,982 bp End 50,111,313 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 F1|15 56.13 cM Start 99,615,396 bp End 99,622,886 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in subcutaneous adipose tissue gastrocnemius muscle abdominal fat triceps brachii muscle vastus lateralis muscle right lobe of liver kidney thoracic diaphragm kidney tubule jejunal mucosa Top expressed in brown adipose tissue vastus lateralis muscle triceps brachii muscle intercostal muscle subcutaneous adipose tissue sternocleidomastoid muscle ankle joint white adipose tissue temporal muscle duodenum More reference expression data BioGPS n/a
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 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 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: 99.62 – 99.62 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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.

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. S2CID 30120853.
• 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. doi:10.1023/a:1027332523114. PMID 14674682. S2CID 25108711.
• 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. doi:10.1134/s0026893309020186. PMID 19425502. S2CID 30196165.
• 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. S2CID 207194967.
• 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.