Hao2 hydroxyacid oxidase 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hao2provided by MGI
Official Full Name: hydroxyacid oxidase 2provided by MGI
Primary source: MGI:MGI:96012
See related: Ensembl:ENSMUSG00000027870 AllianceGenome:MGI:96012
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: Hao3; Hao-2; Haox3
Summary: Predicted to enable (S)-2-hydroxy-acid oxidase activity; FMN binding activity; and identical protein binding activity. Predicted to be involved in fatty acid alpha-oxidation and mandelate metabolic process. Located in mitochondrion. Is expressed in several structures, including adrenal gland; genitourinary system; and nervous system. Orthologous to human HAO2 (hydroxyacid oxidase 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in kidney adult (RPKM 147.3), colon adult (RPKM 32.6) and 2 other tissues See more
Orthologs: human all
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Genomic context

Location:: 3 F2.2; 3 42.9 cM

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	3	NC_000069.7 (98781835..98802692, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	3	NC_000069.6 (98874519..98895376, complement)

Chromosome 3 - NC_000069.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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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

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Variation

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Alleles

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

Endonuclease-mediated (2)
Targeted (1)

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables (S)-2-hydroxy-acid oxidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables (S)-2-hydroxy-acid oxidase activity	IEA Inferred from Electronic Annotation more info
enables (S)-2-hydroxy-acid oxidase activity	ISO Inferred from Sequence Orthology more info
enables FMN binding	IEA Inferred from Electronic Annotation more info
enables FMN binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in fatty acid oxidation	IEA Inferred from Electronic Annotation more info
involved_in fatty acid oxidation	ISO Inferred from Sequence Orthology more info
involved_in mandelate metabolic process	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in mitochondrion	HDA more info	PubMed
is_active_in peroxisomal matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisomal matrix	IEA Inferred from Electronic Annotation more info
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info
located_in peroxisome	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: 2-Hydroxyacid oxidase 2

Names: (S)-2-hydroxy-acid oxidase, peroxisomal; HAOX2; hydroxyacid oxidase (glycolate oxidase) 3; hydroxyacid oxidase 2, kidney; medium chain alpha-hydroxy acid oxidase; medium-chain 2-hydroxy acid oxidase HAOX3; medium-chain L-2-hydroxy acid oxidase

NP_062418.3

EC 1.1.3.15

XP_011238471.1

EC 1.1.3.15

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.