Q5E9F2 (HMOX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 49.
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 1 Short name=HO-1 EC=1.14.99.3 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 289 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein 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 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 |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| 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 |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 289 | 289 | Heme oxygenase 1 | PRO_0000209686 | |||||
Sites | |||||||||
| Metal binding | 26 | 1 | Iron (heme axial ligand) By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 40 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 28 | 1 | Q → E AA sequence Ref.3 | ||||||
| Sequence conflict | 100 | 1 | P → PH AA sequence Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
| [3] | "Structural studies on bovine spleen heme oxygenase. Immunological and structural diversity among mammalian heme oxygenase enzymes." Schacter B.A., Cripps V., Troxler R.F., Offner G.D. Arch. Biochem. Biophys. 282:404-412(1990) [PubMed: 1700666] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND 200-205. Tissue: Spleen. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT020968 mRNA. Translation: AAX08985.1. BC102105 mRNA. Translation: AAI02106.4. |
| IPI | IPI00690186. |
| PIR | S13265. |
| RefSeq | NP_001014912.1. NM_001014912.1. |
| UniGene | Bt.4001. |
3D structure databases | |
| ProteinModelPortal | Q5E9F2. |
| SMR | Q5E9F2. Positions 1-224. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5E9F2. |
Proteomic databases | |
| PRIDE | Q5E9F2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582. |
| GeneID | 513221. |
| KEGG | bta:513221. |
Organism-specific databases | |
| CTD | 3162. |
Phylogenomic databases | |
| eggNOG | maNOG09761. |
| GeneTree | ENSGT00390000017673. |
| HOVERGEN | HBG005982. |
| InParanoid | Q5E9F2. |
| 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. |
| KO | K00510. |
| 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 | HMOX1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q5E9F2 Secondary accession number(s): Q3ZCK7, Q7M338 | ||||||||
| 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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