Reviewed,
UniProtKB/Swiss-Prot P32394 (HMOX1_PIG)
Last modified
June 16, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Heme oxygenase 1 Short name=HO-1 EC=1.14.99.3 | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 288 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. |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. |
| Subcellular location | |
| Induction | Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin. |
| 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 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
| ||||||||||||||||||
References
| [1] | "Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli." Suzuki T., Sato M., Ishikawa K., Yoshida T. Biochem. Int. 28:887-893(1992) [PubMed: 1288499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| X60677 mRNA. Translation: CAA43092.1. | |
| PIR | S37687. |
| RefSeq | NP_001004027.1. |
| UniGene | Ssc.115 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NI6 based on UniProtKB P09601. |
| SMR | P32394. Positions 1-223. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 445512. |
| KEGG | ssc:445512. |
Phylogenomic databases | |
| HOVERGEN | P32394. |
Enzyme and pathway databases | |
| BRENDA | 1.14.99.3. 249. |
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 | HMOX1_PIG | ||||||||
| Accession | Primary (citable) accession number: P32394 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


