Hmox2 heme oxygenase 2 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Hmox2provided by RGD
Official Full Name: heme oxygenase 2provided by RGD
Primary source: RGD:67402
See related: Ensembl:ENSRNOG00000003773 AllianceGenome:RGD:67402
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Ho-2
Summary: Enables heme oxygenase (decyclizing) activity. Involved in response to oxidative stress. Predicted to be located in plasma membrane. Orthologous to human HMOX2 (heme oxygenase 2). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Testes (RPKM 274.1), Kidney (RPKM 164.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 10q12

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (11303512..11337640, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (10797076..10831178, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (10990034..11035493, complement)

Chromosome 10 - NC_086028.1 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: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Role of heme oxygenase in the regulation of the renal hemodynamics in a model of sex-dependent programmed hypertension by maternal diabetes.
Title: Role of heme oxygenase in the regulation of the renal hemodynamics in a model of sex-dependent programmed hypertension by maternal diabetes.
Complex Formation of Heme Oxygenase-2 with Heme Is Competitively Inhibited by the Cytosolic Domain of Caveolin-1.
Title: Complex Formation of Heme Oxygenase-2 with Heme Is Competitively Inhibited by the Cytosolic Domain of Caveolin-1.
Aorta HO-2 histological scores (HSCORE) of hypertensive rats were lower, while SBP was higher. Swimming caused enhancement of HO-2 immunostaining in aorta endothelium and adventitia of SHR. Exercise induced elevation of blood COHb index in SHR. Synchronous BP lowering effect of exercise was observed.
Title: Contribution of Heme Oxygenase 2 to Blood Pressure Regulation in Response to Swimming Exercise and Detraining in Spontaneously Hypertensive Rats.
This experiments shown here indicate that HO-2 and HO-1 are differentially regulated across sexual experience and that the two CO-producing enzymes are expressed in distinct but overlapping populations of cells in medial preoptic area.
Title: Increased expression of carbon monoxide-producing enzymes in the MPOA after sexual experience in male rats.
The increased HO activity and expression in females might play a role in the sexual dimorphism of cardiovascular ischemia susceptibility during the reproductive age.
Title: Sexual dimorphism of cardiovascular ischemia susceptibility is mediated by heme oxygenase.
The distribution of neurons expressing heme oxygenase-2 (HO-2-positive neurons) in the nuclei of various parts of the brainstem was determined.
Title: [The distribution of heme oxygenase-2 in the brainstem nuclei of rats].
HO mRNA levels display isoform-specific changes: those of HO-2 do not change appreciably, whereas those of HO-1 increase significantly in 2-h endotoxemia, with or without obstructive jaundice.
Title: Effects of Kupffer cell blockade on the hepatic expression of metallothionein and heme oxygenase genes in endotoxemic rats with obstructive jaundice.
Heme oxyenase-1 and -2 in the nephron inhibit tubuloglomerular feedback by releasing CO and biliverdin. CO's inhibitory effect is mediated by the soluble-guanylate-cyclase/cGMP signaling pathway, whereas biliverdin probably acts by reducing O2-.
Title: Heme oxygenase metabolites inhibit tubuloglomerular feedback in vivo.
Data show that siRNA blockage of BVR protein expression in cardiomyocytes inhibits HO-2 protein induction but not vice versa.
Title: The coordinated increased expression of biliverdin reductase and heme oxygenase-2 promotes cardiomyocyte survival: a reductase-based peptide counters β-adrenergic receptor ligand-mediated cardiac dysfunction.
The expression and distribution of NADPH-d and HO-2 suggest that carbon monoxide and nitric oxide are likely neurotransmitters and might function in the processing orofacial signal in the spinal trigeminal nucleus together.
Title: Distribution of heme oxygenase-2 and NADPH-diaphorase in the spinal trigeminal nucleus of the rat.

Submit: New GeneRIF Correction See all GeneRIFs (31)

General gene information

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Markers

RH133204 (e-PCR)
- UniSTS:216487

AU047167 (e-PCR)
- UniSTS:110774

D10Wox36 (e-PCR)
- UniSTS:518889

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables heme binding	IBA Inferred from Biological aspect of Ancestor more info
enables heme oxygenase (decyclizing) activity	IBA Inferred from Biological aspect of Ancestor more info
enables heme oxygenase (decyclizing) activity	IDA Inferred from Direct Assay more info	PubMed
enables heme oxygenase (decyclizing) activity	IEA Inferred from Electronic Annotation more info
enables heme oxygenase (decyclizing) activity	ISO Inferred from Sequence Orthology more info
enables heme oxygenase (decyclizing) activity	TAS Traceable Author Statement more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in heme catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in heme oxidation	IBA Inferred from Biological aspect of Ancestor more info
involved_in heme oxidation	IEA Inferred from Electronic Annotation more info
involved_in heme oxidation	TAS Traceable Author Statement more info	PubMed
involved_in response to hypoxia	IEA Inferred from Electronic Annotation more info
involved_in response to hypoxia	ISO Inferred from Sequence Orthology more info
involved_in response to oxidative stress	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: heme oxygenase 2

Names: heme oxygenase (decycling) 2

NP_001264002.1

EC 1.14.14.18

NP_077363.1

EC 1.14.14.18

XP_006245889.1

EC 1.14.14.18

XP_063125986.1

EC 1.14.14.18

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_001277073.1 → NP_001264002.1 heme oxygenase 2

See identical proteins and their annotated locations for NP_001264002.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Both variants 1 and 2 encode the same protein.

Source sequence(s)

BF283242, FM110439, FM134576, FM139649, JAXUCZ010000010

UniProtKB/Swiss-Prot

P23711

UniProtKB/TrEMBL

A0A8L2URJ2, A6K4R4

Related

ENSRNOP00000005031.2, ENSRNOT00000005031.6

Conserved Domains (2) summary

cd19165
Location:146 → 173

HemeO; kinked helix [structural motif]

pfam01126
Location:30 → 235

Heme_oxygenase; Heme oxygenase
NM_024387.2 → NP_077363.1 heme oxygenase 2

See identical proteins and their annotated locations for NP_077363.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript. Both variants 1 and 2 encode the same protein.

Source sequence(s)

JAXUCZ010000010

UniProtKB/Swiss-Prot

P23711

UniProtKB/TrEMBL

A0A8L2URJ2, A6K4R4

Conserved Domains (2) summary

cd19165
Location:146 → 173

HemeO; kinked helix [structural motif]

pfam01126
Location:30 → 235

Heme_oxygenase; Heme oxygenase

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

Reference GRCr8

Genomic

NC_086028.1 Reference GRCr8

Range

11303512..11337640 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006245827.5 → XP_006245889.1 heme oxygenase 2 isoform X1

See identical proteins and their annotated locations for XP_006245889.1

UniProtKB/Swiss-Prot

P23711

UniProtKB/TrEMBL

A0A8L2URJ2, A6K4R4

Conserved Domains (2) summary

cd19165
Location:146 → 173

HemeO; kinked helix [structural motif]

pfam01126
Location:30 → 235

Heme_oxygenase; Heme oxygenase
XM_063269916.1 → XP_063125986.1 heme oxygenase 2 isoform X1

UniProtKB/Swiss-Prot

P23711

UniProtKB/TrEMBL

A0A8L2URJ2, A6K4R4