Reviewed,
UniProtKB/Swiss-Prot P43242 (HMOX2_RABIT)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heme oxygenase 2 Short name=HO-2 EC=1.14.99.3 | ||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 312 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| 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 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | |
| Sequence similarities | Belongs to the heme oxygenase family. Contains 2 HRM (heme regulatory motif) repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Microsome |
| Domain | Repeat |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | heme oxidation Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Characterization of a cDNA-encoding rabbit brain heme oxygenase-2 and identification of a conserved domain among mammalian heme oxygenase isozymes: possible heme-binding site?" Rotenberg M.O., Maines M.D. Arch. Biochem. Biophys. 290:336-344(1991) [PubMed: 1929402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
Cross-references
Sequence databases | |
|---|---|
| S61699 mRNA. Translation: AAB20093.1. | |
| PIR | S18387. |
| RefSeq | NP_001076216.1. |
| UniGene | Ocu.3307 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IVJ based on UniProtKB P06762. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSOCUG00000006018. Oryctolagus cuniculus. [Contig view] |
| GeneID | 100009523. |
Phylogenomic databases | |
| HOVERGEN | P43242. |
Enzyme and pathway databases | |
| BRENDA | 1.14.99.3. 255. |
Family and domain databases | |
| InterPro | IPR002051. Haem_Oase. IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR018207. Haem_oxygenase_CS. [Graphical view] |
| Gene3D | G3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit. |
| PANTHER | PTHR10720. Haem_Oase. 1 hit. |
| Pfam | PF01126. Heme_oxygenase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000343. Haem_Oase. 1 hit. |
| PRINTS | PR00088. HAEMOXYGNASE. |
| PROSITE | PS00593. HEME_OXYGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMOX2_RABIT | ||||||||
| Accession | Primary (citable) accession number: P43242 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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