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MB myoglobin [ Physeter macrocephalus (sperm whale) ]

Gene ID: 102975021, updated on 18-Jan-2025
Gene symbol
MB
Gene description
myoglobin
See related
Ensembl:ENSPCTG00005011582
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Physeter macrocephalus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; Physeteridae; Physeter
Orthologs
human mouse all
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Location:
chromosome: Un
Exon count:
3
Annotation release Status Assembly Chr Location
RS_2025_01 current ASM283717v5 (GCF_002837175.3) Unplaced Scaffold NW_021145510.1 (28809..39467, complement)
102 previous assembly ASM283717v2 (GCF_002837175.2) Unplaced Scaffold NW_021145510.1 (28809..39467, complement)

NW_021145510.1Genomic Context describing neighboring genes Neighboring gene apolipoprotein L6-like

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Probing the non-native H helix translocation in apomyoglobin folding intermediates. Aoto PC, et al. Biochemistry, 2014 Jun 17. PMID 24857522, Free PMC Article
  2. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. Takano T. J Mol Biol, 1977 Mar 5. PMID 845960
  3. X-ray crystal structure of the ferric sperm whale myoglobin: imidazole complex at 2.0 A resolution. Lionetti C, et al. J Mol Biol, 1991 Feb 5. PMID 1994031
  4. Structure and refinement of oxymyoglobin at 1.6 A resolution. Phillips SE. J Mol Biol, 1980 Oct 5. PMID 7463482
  5. Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10). Brunori M, et al. Biophys J, 1999 Mar. PMID 10049310, Free PMC Article

See all (18) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin.
    Title: Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin.
  2. Study investigated the effect of amino acid substitutions on propensity of the completely helical protein sperm whale apomyoglobin (sw ApoMb) for amyloid formation from its structured state in the absence of denaturing agents; demonstrated that stability of the protein native state determines both protein aggregation propensity and structural peculiarities of formed aggregates.
    Title: sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.
  3. The current report presents spectral properties of sperm whale apomyoglobin studied over a wide range of conditions with the use of circular dichroism and fluorescence techniques.
    Title: Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?
  4. A temperature-controlled locally enhanced sampling (TLES) simulation examines multiple diffusion trajectories per simulation by accommodating multiple noninteracting copies of a gas molecule that diffuse independently, while the protein and water molecules experience an average interaction from all copies. Using TLES this study presents mapping O2 migration and escape in Myoglobin.
    Title: Benchmarking Rapid TLES Simulations of Gas Diffusion in Proteins: Mapping O2 Migration and Escape in Myoglobin as a Case Study.
  5. Data suggest that adding hydrophilicity (such as in I107E mutation) to distal pocket is at origin of increase in nitric oxide reductase (NOR) activity in sperm whale myoglobin; proton transfer appears important in biocatalysis by P. aeruginosa NOR.
    Title: Effect of Outer-Sphere Side Chain Substitutions on the Fate of the trans Iron-Nitrosyl Dimer in Heme/Nonheme Engineered Myoglobins (Fe(B)Mbs): Insights into the Mechanism of Denitrifying NO Reductases.
  6. The crystal structures of the K42Y and K42N mutants revealed that the substitutions at position 42 elongate the distances between the distal His55 and the heme iron and also the hydrogen-bonding distances between His55 and the Fe-coordinated water.
    Title: Structures of K42N and K42Y sperm whale myoglobins point to an inhibitory role of distal water in peroxidase activity.
  7. Nitrite binds to oxy myoglobin to generate an undetectable ferrous-peroxynitrate intermediate, whose decay leads to nitrate and ferryl. The ferryl is then reduced to met by the excess nitrite.
    Title: Involvement of ferryl in the reaction between nitrite and the oxy forms of globins.
  8. Data from studies on recombinant/mutant proteins suggest apomyoglobin folding exhibits several energetic bottlenecks that frustrate folding; relief of any one of major identified bottlenecks is insufficient to speed progression to transition state.
    Title: Probing the non-native H helix translocation in apomyoglobin folding intermediates.
Submit: New GeneRIF Correction

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables heme binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables oxygen binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in oxygen transport IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in extracellular exosome IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
myoglobin
Names
nitrite reductase MB
pseudoperoxidase MB
NP_001277651.1

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001290722.1 → NP_001277651.1  myoglobin

    See identical proteins and their annotated locations for NP_001277651.1

    Status: PROVISIONAL

    Source sequence(s)
    AB271144
    UniProtKB/Swiss-Prot
    P02185, Q0KIY8
    Related
    ENSPCTP00005016290.1, ENSPCTT00005017972.1
    Conserved Domains (1) summary
    cl21461
    Location:6 → 154
    Globin-like; Globin-like protein superfamily

RefSeqs of Annotated Genomes: GCF_002837175.3-RS_2025_01

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ASM283717v5 Primary Assembly

Genomic

  1. NW_021145510.1 Reference ASM283717v5 Primary Assembly

    Range
    28809..39467 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P02185.2 GenPept UniProtKB/Swiss-Prot:P02185

Gene LinkOut

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Molecular Biology Databases