O73688 (HMOX_TAKRU) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 62.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heme oxygenase Short name=HO EC=1.14.99.3 | ||
| Gene names |
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| Organism | Takifugu rubripes (Japanese pufferfish) (Fugu rubripes) | ||
| Taxonomic identifier | 31033 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu |
Protein attributes
| Sequence length | 277 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | Microsome By similarity. Endoplasmic reticulum By similarity. |
| Sequence similarities | Belongs to the heme oxygenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Microsome |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | heme oxidation Inferred from electronic annotation. Source: InterPro |
| 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The pufferfish SLP-1 gene, a new member of the SCL/TAL-1 family of transcription factors." Gottgens B., Gilbert J.G.R., Barton L.M., Aparicio S., Hawker K., Mistry S., Vaudin M., King A., Bentley D., Elgar G., Green A.R. Genomics 48:52-62(1998) [PubMed: 9503016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF022814 Genomic DNA. Translation: AAC41263.1. |
3D structure databases | |
| ProteinModelPortal | O73688. |
| SMR | O73688. Positions 15-224. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | fiNOG06146. |
| GeneTree | ENSGT00390000017673. |
| InParanoid | O73688. |
| OrthoDB | EOG4TF0KR. |
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. |
| SUPFAM | SSF48613. Heme_oxygenase. 1 hit. |
| PROSITE | PS00593. HEME_OXYGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMOX_TAKRU | ||||||||
| Accession | Primary (citable) accession number: O73688 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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