| General information | | DisProt: | DP00303 | | Name: | Myoglobin | | Synonym(s): | MYG_PHYCA
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P02185 | | UniGene: | | | SwissProt: | MYG_PHYCA | | TrEMBL: | | | NCBI (GI): | 118595805 | | Source organism: | Physeter catodon (Sperm whale) (Physeter macrocephalus) | | Sequence length: | 153 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED - 60
LKKHGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP - 120
GDFGADAQGA MNKALELFRK DIAAKYKELG YQG
|
| Functional narrative |
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | C Helix | | Location: | 36 - 42 | | Length: | 7 | | Region sequence: |
HPETLEK | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; Mes (buffer) 20 mM; 1H2O 95 %; 2H2O 5 %)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:This region becomes disordered between a pressure change of 500 and 1200 bar.
|
| Region 2 | | Type: | Disordered | | Name: | CD loop | | Location: | 43 - 49 | | Length: | 7 | | Region sequence: |
FDRFKHL | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:This region becomes disordered between a pressure change of 500 and 1200 bar.
|
| Region 3 | | Type: | Disordered | | Name: | F Helix | | Location: | 86 - 94 | | Length: | 9 | | Region sequence: |
LKPLAQSHA | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:This region is the only disordered region for the natively folded protein when at a pressure of 30 bar.
|
| Region 4 | | Type: | Disordered | | Name: | G Helix | | Location: | 100 - 118 | | Length: | 19 | | Region sequence: |
PIKYLEFISEAIIHVLHSR | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:This region becomes disordered between a pressure change of 500 and 1200 bar.
|
| Region 5 | | Type: | Disordered | | Name: | | | Location: | 82 - 101 | | Length: | 20 | | Region sequence: |
HEAELKPLAQSHATKHKIPI | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:
|
| Region 6 | | Type: | Disordered | | Name: | H Helix (C-termini) | | Location: | 144 - 149 | | Length: | 6 | | Region sequence: |
AKYKEL | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:This region becomes disordered between a pressure change of 500 and 1200 bar.
|
| Region 7 | | Type: | Disordered | | Name: | | | Location: | 1 - 153 | | Length: | 153 | | Region sequence: |
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED
LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGYQG | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:The entire protein forms into a molten globule conformation at a pressure of 2000 bar.
|
| Region 8 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 153 | | Length: | 153 | | Region sequence: |
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED
LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGYQG | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (308 K; pH: 6; 1H2O 95 %; 2H2O 5 %; Mes (buffer) 20 mM)
| References:
- Kitahara R, Yamada H, Akasaka K, Wright PE. "High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded." J Mol Biol. 2002; 320(2): 311-9. PubMed: 12079388
- Lecomte JT, Kao YH, Cocco MJ. "The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin." Proteins. 1996; 25(3): 267-85. PubMed: 8844864
| Comments:The entire protein forms into an extended, disordered conformation at a pressure of 3000 bar.
|
| References |
- Edmundson AB. "Amino-Acid Sequence of Sperm Whale Myoglobin." Nature. 1965; 205(4974): 883-7.
- Romero-Herrera A.E., Lehmann H. "Residue 122 of sperm whale and horse myoglobin." Biochim Biophys Acta. 1974; 336: 318-323.
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
