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Glutamate decarboxylase family member 3 pseudogene (GAD3P)

Target
GAD3P
Molecular classification
Other (Pseudogene), related to Enzyme — Glutamate decarboxylase family
01

Overview

**Glutamate decarboxylase family member 3 pseudogene (GAD3P)** is a non-coding pseudogene in the human genome, homologous to the ancient vertebrate gene *GAD3*. The non-pseudogenized ortholog, GAD3, is a third member of the glutamate decarboxylase gene family in many vertebrates, sharing ancestry with GAD1 and GAD2 (which encode enzymes responsible for synthesizing the neurotransmitter GABA from glutamate)[2]. However, *GAD3* was lost in the hominid lineage (including humans, chimpanzees, and gorillas), such that in Homo sapiens only a nonfunctional pseudogene (GAD3P) remains[2].\n\nGAD1 and GAD2 encode the well-characterized enzymes GAD67 and GAD65. If GAD3 is expressed in other vertebrates, it may have distinct tissue specificity, subcellular localization, or regulatory properties compared to its paralogs[2]. However, there is no evidence that the human pseudogene GAD3P encodes a protein, nor is it associated with diseases or considered a therapeutic target.\n\nIf your goal is to annotate **functional targets**, GAD3P should be excluded, as it is not expressed as a protein nor targeted by drugs in humans. If you meant to refer to the active glutamate decarboxylase enzymes in humans, the correct targets are GAD1 and GAD2[2][4].\n\n**Note:** \n- There are also enzymatically active glutamate decarboxylases known as GAD65 (*GAD2*, cytoplasmic/vesicular pool) and GAD67 (*GAD1*, cytoplasmic form), both established as key for GABA synthesis[4].\n- The information that GAD3 is “lost in the hominid lineage” is well supported and recent[2]. No evidence supports a functional protein or therapeutic relevance in humans.

Other names
GAD3 pseudogeneglutamate decarboxylase 3 pseudogeneputative glutamate decarboxylase 3GAD3P1
02

Biological functions

null in humans (no known function as it is a pseudogene)in functional non-hominid species, GAD3 may be involved in GABA biosynthesis
03

Disease associations

null in humans; no evidence for direct disease association due to the pseudogene status in Homo sapiens

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