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

    Gene ID: 79239, updated on 9-Dec-2024

    Summary

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    Official Symbol
    Hmox2provided by RGD
    Official Full Name
    heme oxygenase 2provided by RGD
    Primary source
    RGD:67402
    See related
    EnsemblRapid: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, Dec 2024]
    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

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    See Hmox2 in Genome Data Viewer
    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_086028.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC134480753 Neighboring gene cell death-inducing p53 target 1 Neighboring gene high mobility group nucleosomal binding domain 4, pseudogene 3 Neighboring gene NmrA like redox sensor 1 Neighboring gene DnaJ heat shock protein family (Hsp40) member A3

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Depletion of endogenous serotonin synthesis with p-CPA attenuates upregulation of constitutive isoform of heme oxygenase-2 expression, edema formation and cell injury following a focal trauma to the rat spinal cord. Sharma HS, et al. Acta Neurochir Suppl, 2003. PMID 14753474
    2. Contribution of Heme Oxygenase 2 to Blood Pressure Regulation in Response to Swimming Exercise and Detraining in Spontaneously Hypertensive Rats. Kilic-Toprak E, et al. Med Sci Monit, 2018 Aug 22. PMID 30132448, Free PMC Article
    3. Heme oxygenase is necessary for the excitatory response of cultured neonatal rat rostral ventrolateral medulla neurons to hypoxia. D'Agostino D, et al. Am J Physiol Regul Integr Comp Physiol, 2009 Jan. PMID 18971354, Free PMC Article
    4. [The distribution of heme oxygenase-2 in the brainstem nuclei of rats]. Kotsiuba AY, et al. Morfologiia, 2012. PMID 23659033
    5. Role of heme oxygenases in sepsis-induced diaphragmatic contractile dysfunction and oxidative stress. Barreiro E, et al. Am J Physiol Lung Cell Mol Physiol, 2002 Aug. PMID 12114211

    See all (42) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. 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.
    3. 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.
    4. 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.
    5. 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.
    6. 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].
    7. 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.
    8. 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.
    9. 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.
    10. 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

    Homology

    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
    NP_077363.1
    XP_006245889.1
    XP_063125986.1

    NCBI Reference Sequences (RefSeq)

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    NEW Try the new Transcript table

    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_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
      ENSRNOP00000084166.1, ENSRNOT00000114400.2
      Conserved Domains (2) summary
      cd19165
      Location:146 → 173
      HemeO; kinked helix [structural motif]
      pfam01126
      Location:30 → 235
      Heme_oxygenase; Heme oxygenase

    2. 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
      Related
      ENSRNOP00000075102.3, ENSRNOT00000077164.3
      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

    1. NC_086028.1 Reference GRCr8

      Range
      11303512..11337640 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. 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

    2. XM_063269916.1 → XP_063125986.1  heme oxygenase 2 isoform X1

      UniProtKB/Swiss-Prot
      P23711
      UniProtKB/TrEMBL
      A0A8L2URJ2, A6K4R4
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P23711.1 GenPept UniProtKB/Swiss-Prot:P23711

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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