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MB myoglobin [ Physeter catodon (sperm whale) ]

Gene ID: 102975021, updated on 5-Aug-2022

Summary

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Gene symbol
MB
Gene description
myoglobin
See related
Ensembl:ENSPCTG00005011582
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Physeter catodon
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; Physeteridae; Physeter
Orthologs
human mouse all
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Genomic context

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Location:
chromosome: Un
Exon count:
3
Annotation release Status Assembly Chr Location
102 current ASM283717v2 (GCF_002837175.2) Unplaced Scaffold NW_021145510.1 (28809..39467, complement)
101 previous assembly ASM283717v1 (GCF_002837175.1) Unplaced Scaffold NW_019873573.1 (21120174..21130832, complement)

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

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin. Tse W, et al. Biochem J, 2021 Feb 26. PMID 33543749, Free PMC Article
  2. sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability. Katina NS, et al. Biophys J, 2017 Sep 5. PMID 28877500, Free PMC Article
  3. Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram? Balobanov VA, et al. Biochemistry (Mosc), 2017 May. PMID 28601072
  4. Benchmarking Rapid TLES Simulations of Gas Diffusion in Proteins: Mapping O2 Migration and Escape in Myoglobin as a Case Study. Shadrina MS, et al. J Chem Theory Comput, 2016 Apr 12. PMID 26938707
  5. Structures of K42N and K42Y sperm whale myoglobins point to an inhibitory role of distal water in peroxidase activity. Wang C, et al. Acta Crystallogr D Biol Crystallogr, 2014 Nov. PMID 25372675

See all (16) 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.
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General gene information

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Homology

General protein information

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Preferred Names
myoglobin

NCBI Reference Sequences (RefSeq)

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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: Physeter catodon Annotation Release 102 details...Open this link in a new tab

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

Reference ASM283717v2 Primary Assembly

Genomic

  1. NW_021145510.1 Reference ASM283717v2 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

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.