O70252 · HMOX2_MOUSE

  • Protein
    Heme oxygenase 2
  • Gene
    Hmox2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Heme oxygenase 2

Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.

Heme oxygenase 2 soluble form

Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.

Catalytic activity

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site44Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site153heme b (UniProtKB | ChEBI)
Site159Important for catalytic activity
Binding site198heme b (UniProtKB | ChEBI)
Binding site202heme b (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentplasma membrane
Molecular Functionheme binding
Molecular Functionheme oxygenase (decyclizing) activity
Molecular Functionmetal ion binding
Biological Processheme catabolic process
Biological Processheme oxidation
Biological Processresponse to hypoxia
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Hmox2

Organism names

  • Taxonomic identifier
  • Strains
    • CD-1
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O70252
  • Secondary accessions
    • O70626

Proteomes

Organism-specific databases

Subcellular Location

Microsome membrane
; Single-pass type IV membrane protein
Endoplasmic reticulum membrane
; Single-pass type IV membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain2-294Cytoplasmic
Transmembrane295-315Helical; Anchor for type IV membrane protein

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
Modified residue2Phosphoserine
ChainPRO_00004556272-294Heme oxygenase 2 soluble form
ChainPRO_00002096922-315Heme oxygenase 2
Modified residue264S-nitrosocysteine
Modified residue281S-nitrosocysteine

Post-translational modification

A soluble form arises by proteolytic removal of the membrane anchor.
S-nitrosylated by BLVRB.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, repeat.

TypeIDPosition(s)Description
Region1-28Disordered
Compositional bias9-28Basic and acidic residues
Repeat263-268HRM 1
Repeat280-285HRM 2

Sequence similarities

Belongs to the heme oxygenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    315
  • Mass (Da)
    35,739
  • Last updated
    1998-08-01 v1
  • Checksum
    EA382EB2C7CED6D1
MSSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPSLQLILAASVALVAGLLAWYYM

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YXN4D3YXN4_MOUSEHmox293
D3YX62D3YX62_MOUSEHmox2228
D3Z4A2D3Z4A2_MOUSEHmox265

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias9-28Basic and acidic residues
Sequence conflict172-174in Ref. 2; AAC82364/AAC82363

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF029874
EMBL· GenBank· DDBJ
AAC17981.1
EMBL· GenBank· DDBJ
mRNA
AF054670
EMBL· GenBank· DDBJ
AAC82364.1
EMBL· GenBank· DDBJ
mRNA
AF054669
EMBL· GenBank· DDBJ
AAC82363.1
EMBL· GenBank· DDBJ
mRNA
BC002011
EMBL· GenBank· DDBJ
AAH02011.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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