Agxt alanine-glyoxylate aminotransferase [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Agxtprovided by MGI
Official Full Name: alanine-glyoxylate aminotransferaseprovided by MGI
Primary source: MGI:MGI:1329033
See related: Ensembl:ENSMUSG00000026272 AllianceGenome:MGI:1329033
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: AGT; SPT; Agt1; Agxt1
Summary: Enables alanine-glyoxylate transaminase activity. Acts upstream of or within Notch signaling pathway; glyoxylate metabolic process; and oxalic acid secretion. Predicted to be located in mitochondrial matrix and peroxisomal matrix. Predicted to be active in peroxisome. Is expressed in liver. Used to study primary hyperoxaluria type 1. Human ortholog(s) of this gene implicated in primary hyperoxaluria type 1. Orthologous to human AGXT (alanine--glyoxylate aminotransferase). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Restricted expression toward liver adult (RPKM 173.1) See more
Orthologs: human all
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Genomic context

Location:: 1 D; 1 47.0 cM

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (93062962..93073143)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (93135240..93145421)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

two human constructs, wild-type and engineered AGT (RHEAM), were tested in Agxt(-/-) mice. Repeat dosing in Agxt(-/-) mice resulted in a 40% reduction in urinary oxalate, suggesting therapeutic benefit.
Title: Systemic Alanine Glyoxylate Aminotransferase mRNA Improves Glyoxylate Metabolism in a Mouse Model of Primary Hyperoxaluria Type 1.
AGT-deficient mice showed decreased vascular permeability, a readout of in vivo histamine activity.
Title: In Silico Modeling of Liver Metabolism in a Human Disease Reveals a Key Enzyme for Histidine and Histamine Homeostasis.
expressed wild-type human AGT1 was predominantly localized in mouse hepatocellular peroxisomes, whereas the most common mutant form of AGT1 (G170R) was localized predominantly in the mitochondria
Title: Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer.

Submit: New GeneRIF Correction

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (4) 1 citation
Targeted (1) 1 citation

General gene information

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Markers

D17849 (e-PCR)
- UniSTS:124732

Agxt (e-PCR), detects polymorphism
- UniSTS:224090

Agxt (e-PCR), detects polymorphism
- UniSTS:305546

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables L-serine-pyruvate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables L-serine-pyruvate transaminase activity	IEA Inferred from Electronic Annotation more info
enables L-serine-pyruvate transaminase activity	ISO Inferred from Sequence Orthology more info
enables alanine-glyoxylate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables alanine-glyoxylate transaminase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables alanine-glyoxylate transaminase activity	ISO Inferred from Sequence Orthology more info
enables alanine-glyoxylate transaminase activity	ISS Inferred from Sequence or Structural Similarity more info
enables amino acid binding	IEA Inferred from Electronic Annotation more info
enables amino acid binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
enables pyridoxal phosphate binding	IEA Inferred from Electronic Annotation more info
enables pyridoxal phosphate binding	ISO Inferred from Sequence Orthology more info
enables transaminase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in L-alanine catabolic process	IEA Inferred from Electronic Annotation more info
involved_in L-alanine catabolic process	ISO Inferred from Sequence Orthology more info
involved_in L-cysteine catabolic process	IEA Inferred from Electronic Annotation more info
involved_in L-cysteine catabolic process	ISO Inferred from Sequence Orthology more info
involved_in L-serine metabolic process	IEA Inferred from Electronic Annotation more info
involved_in L-serine metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within Notch signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in glycine biosynthetic process, by transamination of glyoxylate	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	IEA Inferred from Electronic Annotation more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	ISO Inferred from Sequence Orthology more info
involved_in glyoxylate catabolic process	IEA Inferred from Electronic Annotation more info
involved_in glyoxylate catabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within glyoxylate metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in glyoxylate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glyoxylate metabolic process	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within oxalic acid secretion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in pyruvate biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in pyruvate biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in response to cAMP	IEA Inferred from Electronic Annotation more info
involved_in response to cAMP	ISO Inferred from Sequence Orthology more info
involved_in response to glucocorticoid	IEA Inferred from Electronic Annotation more info
involved_in response to glucocorticoid	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	TAS Traceable Author Statement more info	PubMed
located_in peroxisomal matrix	IEA Inferred from Electronic Annotation more info
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info
is_active_in peroxisome	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisome	ISO Inferred from Sequence Orthology more info
located_in peroxisome	ISS Inferred from Sequence or Structural Similarity more info
located_in peroxisome	TAS Traceable Author Statement more info	PubMed

General protein information

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Preferred Names: alanine--glyoxylate aminotransferase; serine--pyruvate aminotransferase, peroxisomal

Names: alanine-glyoxylate aminotransferase 1; serine--pyruvate aminotransferase, mitochondrial; serine-pyruvate aminotransferase

NP_001263639.1

EC 2.6.1.44

EC 2.6.1.51

NP_057911.2

EC 2.6.1.44

EC 2.6.1.51

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001276710.1 → NP_001263639.1 serine--pyruvate aminotransferase, peroxisomal isoform 2

See identical proteins and their annotated locations for NP_001263639.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) includes an upstream AUG start codon (uAUG) and a downstream AUG start codon (dAUG). Isoform 2 is encoded from the CDS with the dAUG start codon, and is a peroxisomal enzyme.

Source sequence(s)

AC110247, AK149432, BB868742

UniProtKB/TrEMBL

Q3UEN9

Conserved Domains (2) summary

cd06451
Location:24 → 385

AGAT_like; Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), ...

COG0075
Location:21 → 384

PucG; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]
NM_016702.3 → NP_057911.2 alanine--glyoxylate aminotransferase isoform 1 precursor

See identical proteins and their annotated locations for NP_057911.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) includes an upstream AUG start codon (uAUG) and a downstream AUG start codon (dAUG). Isoform 1 precursor is encoded from the CDS with the uAUG start codon. The mature peptide is located in mitochondrion but the sequence is identical to the peroxisomal enzyme (isoform 2).

Source sequence(s)

AC110247, AK149432, BB868742

Consensus CDS

CCDS15184.1

UniProtKB/Swiss-Prot

O35423, Q8R128

Related

ENSMUSP00000027491.6, ENSMUST00000027491.7

Conserved Domains (2) summary

cd06451
Location:46 → 407

AGAT_like; Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), ...

COG0075
Location:43 → 406

PucG; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]