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Identification
HMDB Protein ID HMDBP00151
Secondary Accession Numbers
  • 5383
  • HMDBP04881
Name Heme oxygenase 2
Synonyms
  1. HO-2
Gene Name HMOX2
Protein Type Unknown
Biological Properties
General Function Involved in heme oxygenase (decyclizing) activity
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.
Pathways
  • Mineral absorption
  • Porphyrin and chlorophyll metabolism
Reactions
Heme + AH(2) + Oxygen → Biliverdin + Fe2+ + CO + A + Water details
Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Fe3+ + FAD + Water details
GO Classification
Biological Process
small molecule metabolic process
response to oxidative stress
heme catabolic process
cellular iron ion homeostasis
heme oxidation
response to hypoxia
transmembrane transport
Cellular Component
endoplasmic reticulum membrane
plasma membrane
Function
catalytic activity
heme oxygenase (decyclizing) activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity
Molecular Function
metal ion binding
heme oxygenase (decyclizing) activity
Process
metabolic process
nitrogen compound metabolic process
heme metabolic process
heme oxidation
tetrapyrrole metabolic process
porphyrin metabolic process
oxidation reduction
Cellular Location
  1. Microsome
  2. Endoplasmic reticulum
Gene Properties
Chromosome Location 16
Locus 16p13.3
SNPs HMOX2
Gene Sequence
>951 bp
ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG
GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG
ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC
AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC
CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC
ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC
TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC
ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT
CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA
GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG
CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG
GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC
GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA
GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC
AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG
GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
Protein Properties
Number of Residues 316
Molecular Weight 36032.615
Theoretical pI 5.41
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Heme oxygenase 2
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG
NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN
WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA
GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL
AAGVALAAGLLAWYYM
GenBank ID Protein 187761307
UniProtKB/Swiss-Prot ID P30519
UniProtKB/Swiss-Prot Entry Name HMOX2_HUMAN
PDB IDs
GenBank Gene ID NM_001127204.1
GeneCard ID HMOX2
GenAtlas ID HMOX2
HGNC ID HGNC:5014
References
General References
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  3. Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J Biol Chem. 1995 Mar 17;270(11):6345-50. [PubMed:7890772 ]
  4. 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. [PubMed:1575508 ]
  5. Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr: Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. [PubMed:17965015 ]