Q0KIY2 · MYG_BALED

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site65nitrite (UniProtKB | ChEBI)
Binding site65O2 (UniProtKB | ChEBI)
Binding site94Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue

GO annotations

AspectTerm
Cellular Componentextracellular exosome
Cellular Componentsarcoplasm
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionnitrite reductase activity
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Molecular Functionperoxidase activity
Biological Processremoval of superoxide radicals

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Myoglobin
  • Alternative names
    • Nitrite reductase MB
      (EC:1.7.-.-
      ) . EC:1.7.-.- (UniProtKB | ENZYME | Rhea)
    • Pseudoperoxidase MB
      (EC:1.11.1.-
      ) . EC:1.11.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      MB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Whippomorpha > Cetacea > Mysticeti > Balaenopteridae > Balaenoptera

Accessions

  • Primary accession
    Q0KIY2

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002615781-154Myoglobin
Modified residue4Phosphoserine
Modified residue68Phosphothreonine

Keywords

Interaction

Subunit

Monomeric.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-148Globin

Sequence similarities

Belongs to the globin family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    154
  • Mass (Da)
    17,249
  • Last updated
    2007-01-23 v3
  • Checksum
    E3753A672A1D5C34
MVLSDAEWQLVLNIWAKVEADVAGHGQDILIRLFKGHPETLEKFDKFKHLKTEAEMKASEDLKKHGNTVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSRHPGDFGADAQAAMNKALELFRKDIAAKYKELGFQG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB271150
EMBL· GenBank· DDBJ
BAF03585.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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