Heme oxygenase 2
Details
- Name
- Heme oxygenase 2
- Synonyms
- 1.14.14.18
- HO-2
- HO2
- Gene Name
- HMOX2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0001171|Heme oxygenase 2 MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL AAGVALAAGLLAWYYM
- Number of residues
- 316
- Molecular Weight
- 36032.615
- Theoretical pI
- 5.09
- GO Classification
- Functionsheme oxygenase (decyclizing) activity / metal ion bindingProcessescellular iron ion homeostasis / heme catabolic process / heme oxidation / porphyrin-containing compound metabolic process / response to hypoxia / small molecule metabolic process / transmembrane transportComponentsendoplasmic reticulum membrane / membrane / plasma membrane
- General Function
- Metal ion binding
- Specific 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.
- Pfam Domain Function
- Heme_oxygenase (PF01126)
- Transmembrane Regions
- Not Available
- Cellular Location
- Microsome
- Gene sequence
>lcl|BSEQ0010410|Heme oxygenase 2 (HMOX2) ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
- Chromosome Location
- 16
- Locus
- 16p13.3
- External Identifiers
Resource Link UniProtKB ID P30519 UniProtKB Entry Name HMOX2_HUMAN GenBank Protein ID 443771 GenBank Gene ID D21243 GenAtlas ID HMOX2 HGNC ID HGNC:5014 - General References
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- McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. 1992 May 15;295(1):13-20. [Article]
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