P02173 · MYG_ORCOR
- ProteinMyoglobin
- GeneMB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids154 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity.
Catalytic activity
- Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H+ + nitriteThis reaction proceeds in the backward direction.
- AH2 + H2O2 = A + 2 H2O
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | sarcoplasm | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | nitrite reductase activity | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Molecular Function | peroxidase activity | |
Biological Process | removal of superoxide radicals |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMyoglobin
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Whippomorpha > Cetacea > Odontoceti > Delphinidae > Orcinus
Accessions
- Primary accessionP02173
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000053324 | 2-154 | Myoglobin | |||
Sequence: GLSDGEWQLVLNVWGKVEADLAGHGQDILIRLFKGHPETLEKFDKFKHLKTEADMKASEDLKKHGNTVLTALGAILKKKGHHDAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPAEFGADAQGAMNKALELFRKDIAAKYKELGFHG | ||||||
Modified residue | 4 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 68 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Interaction
Subunit
Monomeric.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-148 | Globin | ||||
Sequence: GLSDGEWQLVLNVWGKVEADLAGHGQDILIRLFKGHPETLEKFDKFKHLKTEADMKASEDLKKHGNTVLTALGAILKKKGHHDAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPAEFGADAQGAMNKALELFRKDIAAKYK |
Sequence similarities
Belongs to the globin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length154
- Mass (Da)17,202
- Last updated2007-01-23 v2
- Checksum0D287946EF253C05
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 123 | in Ref. 2; AA sequence | ||||
Sequence: E → Q |
Keywords
- Technical term