O70252 · HMOX2_MOUSE
- ProteinHeme oxygenase 2
- GeneHmox2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids315 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe2+ + H+ + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 153 | heme b (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 159 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 198 | heme b (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 202 | heme b (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | plasma membrane | |
Molecular Function | heme binding | |
Molecular Function | heme oxygenase (decyclizing) activity | |
Molecular Function | metal ion binding | |
Biological Process | heme catabolic process | |
Biological Process | heme oxidation | |
Biological Process | response to hypoxia | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHeme oxygenase 2
- EC number
- Short namesHO-2
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO70252
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Microsome membrane ; Single-pass type IV membrane protein
Endoplasmic reticulum membrane ; Single-pass type IV membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-294 | Cytoplasmic | ||||
Sequence: SSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPS | ||||||
Transmembrane | 295-315 | Helical; Anchor for type IV membrane protein | ||||
Sequence: LQLILAASVALVAGLLAWYYM |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000455627 | 2-294 | Heme oxygenase 2 soluble form | |||
Sequence: SSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPS | ||||||
Chain | PRO_0000209692 | 2-315 | Heme oxygenase 2 | |||
Sequence: SSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPSLQLILAASVALVAGLLAWYYM | ||||||
Modified residue | 264 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 281 | S-nitrosocysteine | ||||
Sequence: C |
Post-translational modification
A soluble form arises by proteolytic removal of the membrane anchor.
S-nitrosylated by BLVRB.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MSSEVETSEGVDESEKNSMAPEKENHTK | ||||||
Compositional bias | 9-28 | Basic and acidic residues | ||||
Sequence: EGVDESEKNSMAPEKENHTK | ||||||
Repeat | 263-268 | HRM 1 | ||||
Sequence: KCPFYA | ||||||
Repeat | 280-285 | HRM 2 | ||||
Sequence: NCPFQT |
Sequence similarities
Belongs to the heme oxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)35,739
- Last updated1998-08-01 v1
- ChecksumEA382EB2C7CED6D1
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-28 | Basic and acidic residues | ||||
Sequence: EGVDESEKNSMAPEKENHTK | ||||||
Sequence conflict | 172-174 | in Ref. 2; AAC82364/AAC82363 | ||||
Sequence: RAL → SSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |