GPD1

Protein identityUniProt · HPA

UniProt accession

P21695

Gene

GPD1

Ensembl

ENSG00000167588

Chromosome

12

Canonical length

349 aa

Protein class

Disease related genes, Enzymes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Quaternary structure

Homodimer

OverviewNCBI Gene

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. [provided by RefSeq, Mar 2012]

Canonical amino-acid sequenceUniProt

349 residues, UniProt reviewed canonical sequence.

>P21695|GPD1
     1  MASKKVCIVG SGNWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTQHEN
    61  VKYLPGHKLP PNVVAVPDVV QAAEDADILI FVVPHQFIGK ICDQLKGHLK ANATGISLIK
   121  GVDEGPNGLK LISEVIGERL GIPMSVLMGA NIASEVADEK FCETTIGCKD PAQGQLLKEL
   181  MQTPNFRITV VQEVDTVEIC GALKNVVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK
   241  LFCSGPVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE LLNGQKLQGP
   301  ETARELYSIL QHKGLVDKFP LFMAVYKVCY EGQPVGEFIH CLQNHPEHM

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against GPD1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.22

Highest tissue expression

573 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about GPD1.

Disease | AllUniProt

Conditions GPD1 is implicated in, by any mechanism.

• Hypertriglyceridemia, transient infantile (HTGTI) MIM:614480

Disease | GeneticClinVar

21 pathogenic / likely-pathogenic of 173 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Transient infantile hypertriglyceridemia and hepatosteatosis
• Inborn genetic diseases

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.83

gnomAD pLI

0.01

gnomAD missense Z

0.17

DepMap mean gene effect

-0.04

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to cAMP
• cellular response to tumor necrosis factor
• gluconeogenesis
• glycerol-3-phosphate catabolic process
• glycerol-3-phosphate metabolic process
• glycerol-3-phosphate shuttle
• positive regulation of glycolytic process

Molecular functions

• glycerol-3-phosphate dehydrogenase [NAD(P)+] activity
• NAD binding
• protein homodimerization activity
• glycerol-3-phosphate dehydrogenase (NAD+) activity

Cellular components

• cytosol
• extracellular exosome

Protein domainsUniProt · Pfam · InterPro

• Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminal
• Glycerol-3-phosphate dehydrogenase, NAD-dependent
• 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
• Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminal
• 6-phosphogluconate dehydrogenase, domain 2
• Glycerol-3-phosphate dehydrogenase, NAD-dependent, eukaryotic
• NAD(P)-binding domain superfamily
• NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus
• NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus

KeywordsUniProt

• Cytoplasm
• NAD
• Oxidoreductase
• Phosphoprotein