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

Gene ID: 11611, updated on 11-Apr-2024

Summary

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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 and serine--pyruvate aminotransferase). [provided by Alliance of Genome Resources, Apr 2022]
Expression
Restricted expression toward liver adult (RPKM 173.1) See more
Orthologs
human all
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Genomic context

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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_000067.7Genomic Context describing neighboring genes Neighboring gene kinesin family member 1A Neighboring gene STARR-seq mESC enhancer starr_01723 Neighboring gene predicted gene, 36472 Neighboring gene mab-21-like 4 Neighboring gene ciliary rootlet coiled-coil, rootletin family member 2 Neighboring gene STARR-seq mESC enhancer starr_01724 Neighboring gene STARR-seq mESC enhancer starr_01726

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • 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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Related articles in PubMed

  1. Enteric oxalate elimination is induced and oxalate is normalized in a mouse model of primary hyperoxaluria following intestinal colonization with Oxalobacter. Hatch M, et al. Am J Physiol Gastrointest Liver Physiol, 2011 Mar. PMID 21163900, Free PMC Article
  2. Differential expression of liver and kidney proteins in a mouse model for primary hyperoxaluria type I. Hernández-Fernaud JR, et al. FEBS J, 2010 Nov. PMID 20977670
  3. In vivo CRISPR-Cas9 inhibition of hepatic LDH as treatment of primary hyperoxaluria. Martinez-Turrillas R, et al. Mol Ther Methods Clin Dev, 2022 Jun 9. PMID 35402636, Free PMC Article
  4. Epigenomic and transcriptional profiling identifies impaired glyoxylate detoxification in NAFLD as a risk factor for hyperoxaluria. Gianmoena K, et al. Cell Rep, 2021 Aug 24. PMID 34433051
  5. Dysregulated oxalate metabolism is a driver and therapeutic target in atherosclerosis. Liu Y, et al. Cell Rep, 2021 Jul 27. PMID 34320345, Free PMC Article

See all (28) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. 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.
  3. 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)

Pathways from PubChem

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General gene information

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Markers

Homology

Gene Ontology Provided by MGI

Function Evidence Code Pubs
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 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 pyridoxal phosphate binding ISO
Inferred from Sequence Orthology
more info
  
enables serine-pyruvate transaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables serine-pyruvate transaminase activity ISO
Inferred from Sequence Orthology
more info
  
enables transaminase activity ISO
Inferred from Sequence Orthology
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-alanine catabolic process ISO
Inferred from Sequence Orthology
more info
  
involved_in L-cysteine catabolic process ISO
Inferred from Sequence Orthology
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 ISO
Inferred from Sequence Orthology
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
  
acts_upstream_of_or_within oxalic acid secretion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in pyruvate biosynthetic process ISO
Inferred from Sequence Orthology
more info
  
involved_in response to cAMP ISO
Inferred from Sequence Orthology
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 ISO
Inferred from Sequence Orthology
more info
  
located_in mitochondrion TAS
Traceable Author Statement
more info
 PubMed 
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 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
NP_057911.2

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)

  1. 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]

  2. 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]

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000067.7 Reference GRCm39 C57BL/6J

    Range
    93062962..93073143
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
O35423.3 GenPept UniProtKB/Swiss-Prot:O35423

Gene LinkOut

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