ID:HMOX2_HUMAN DESCRIPTION: RecName: Full=Heme oxygenase 2; Short=HO-2; EC=1.14.99.3; FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. CATALYTIC ACTIVITY: Heme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+) + CO + 3 A + 3 H(2)O. SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum. INDUCTION: Heme oxygenase 2 activity is non-inducible. SIMILARITY: Belongs to the heme oxygenase family. SIMILARITY: Contains 2 HRM (heme regulatory motif) repeats. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/hmox2/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P30519
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.