Reviewed,
UniProtKB/Swiss-Prot O70453 (HMOX3_RAT)
Last modified
June 16, 2009.
Version 56.
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 3 Short name=HO-3 EC=1.14.99.3 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 290 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. Heme oxygenase 3 could be implicated in some heme-dependent regulatory role in the cell. |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | |
| Tissue specificity | Found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis. |
| 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] | "Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3." McCoubrey W.K. Jr., Huang T.J., Maines M.D. Eur. J. Biochem. 247:725-732(1997) [PubMed: 9266719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
Cross-references
Sequence databases | |
|---|---|
| AF058787 mRNA. Translation: AAC14142.1. | |
| IPI | IPI00198589. |
| RefSeq | NP_001070904.1. |
| UniGene | Rn.133155 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IVJ based on UniProtKB P06762. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 365909. |
| KEGG | rno:365909. |
Organism-specific databases | |
| RGD | 1565339. LOC365909. |
Phylogenomic databases | |
| HOVERGEN | O70453. |
Enzyme and pathway databases | |
| BRENDA | 1.14.99.3. 248. |
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. |
| PROSITE | PS00593. HEME_OXYGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 688338. |
Entry information
| Entry name | HMOX3_RAT | ||||||||
| Accession | Primary (citable) accession number: O70453 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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