Reviewed, UniProtKB/Swiss-Prot P02185 (MYG_PHYCA)

Names and origin

Protein names

Recommended name:
    Myoglobin

Gene names

Name:

MB

Organism

Physeter catodon (Sperm whale) (Physeter macrocephalus)

Taxonomic identifier

9755 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Cetacea › Odontoceti › Physeteridae › Physeter

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
Molecular function	Muscle protein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxygen transport Inferred from electronic annotation. Source: InterPro
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 154

153

Myoglobin

PRO_0000053335

Sites

Metal binding

65

1

Iron (heme distal ligand)

Metal binding

94

1

Iron (heme proximal ligand)

Natural variations

Natural variant

122

1

G → A in metmyoglobin.

Experimental info

Sequence conflict

123

1

D → N AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

154

Helix Strand Turn

Details...

Helix

5 – 18

14

Helix

19 – 21

3

Helix

22 – 36

15

Helix

38 – 41

4

Turn

45 – 49

5

Helix

53 – 57

5

Helix

60 – 78

19

Turn

79 – 81

3

Helix

84 – 96

13

Helix

102 – 119

18

Helix

121 – 123

3

Helix

126 – 150

25

Sequences

	Sequence		Length	Mass (Da)
	P02185-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: FD1D85814263E1A8	FASTA	154	17,331
	10 20 30 40 50 60 MVLSEGEWQL VLHVWAKVEA DVAGHGQDIL IRLFKSHPET LEKFDRFKHL KTEAEMKASE 70 80 90 100 110 120 DLKKHGVTVL TALGAILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISE AIIHVLHSRH 130 140 150 PGDFGADAQG AMNKALELFR KDIAAKYKEL GYQG

References

[1]	"cDNA-derived amino acid sequences of myoglobins from nine species of whales and dolphins." Iwanami K., Mita H., Yamamoto Y., Fujise Y., Yamada T., Suzuki T. Comp. Biochem. Physiol. 145B:249-256(2006) [PubMed: 16962803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Amino-acid sequence of sperm whale myoglobin." Edmundson A.B. Nature 205:883-887(1965) Cited for: PROTEIN SEQUENCE OF 2-154. Tissue: Heart muscle.
[3]	"Residue 122 of sperm whale and horse myoglobin." Romero-Herrera A.E., Lehmann H. Biochim. Biophys. Acta 336:318-323(1974) Cited for: SEQUENCE REVISION TO 123. Tissue: Skeletal muscle.
[4]	"Structure of myoglobin refined at 2.0-A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale." Takano T. J. Mol. Biol. 110:537-568(1977) [PubMed: 845959] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF METMYOGLOBIN.
[5]	"Structure of myoglobin refined at 2.0-A resolution. II. Structure of deoxymyoglobin from sperm whale." Takano T. J. Mol. Biol. 110:569-584(1977) [PubMed: 845960] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF DEOXYMYOGLOBIN.
[6]	"Structure and refinement of oxymyoglobin at 1.6-A resolution." Phillips S.E.V. J. Mol. Biol. 142:531-554(1980) [PubMed: 7463482] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF OXYMYOGLOBIN.
[7]	"X-ray crystal structure of the ferric sperm whale myoglobin: imidazole complex at 2.0-A resolution." Lionetti C., Guanziroli M.G., Frigerio F., Ascenzi P., Bolognesi M. J. Mol. Biol. 217:409-412(1991) [PubMed: 1994031] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]	"Structural dynamics of ligand diffusion in the protein matrix: a study on a new myoglobin mutant Y(B10) Q(E7) R(E10)." Brunori M., Cutruzzola F., Savino C., Travaglini-Allocatelli C., Vallone B., Gibson Q.H. Biophys. J. 76:1259-1269(1999) [PubMed: 10049310] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[9]	"The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin." Brunori M., Vallone B., Cutruzzola F., Travaglini-Allocatelli C., Berendzen J., Chu K., Sweet R.M., Schlichting I. Proc. Natl. Acad. Sci. U.S.A. 97:2058-2063(2000) [PubMed: 10681426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB271144 mRNA. Translation: BAF03579.1.

PIR

MYWHP. A90591.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
101M	X-ray	2.07	A	1-154	[»]
102M	X-ray	1.84	A	1-154	[»]
103M	X-ray	2.07	A	1-154	[»]
104M	X-ray	1.71	A	1-154	[»]
105M	X-ray	2.02	A	1-154	[»]
106M	X-ray	1.99	A	1-154	[»]
107M	X-ray	2.09	A	1-154	[»]
108M	X-ray	2.67	A	1-154	[»]
109M	X-ray	1.83	A	1-154	[»]
110M	X-ray	1.77	A	1-154	[»]
111M	X-ray	1.88	A	1-154	[»]
112M	X-ray	2.34	A	1-154	[»]
1A6G	X-ray	1.15	A	1-152	[»]
1A6K	X-ray	1.10	A	1-152	[»]
1A6M	X-ray	1.00	A	1-152	[»]
1A6N	X-ray	1.15	A	1-152	[»]
1ABS	X-ray	1.50	A	1-154	[»]
1AJG	X-ray	1.69	A	1-154	[»]
1AJH	X-ray	1.69	A	1-154	[»]
1BVC	X-ray	1.50	A	1-154	[»]
1BVD	X-ray	1.40	A	1-154	[»]
1BZ6	X-ray	1.20	A	1-154	[»]
1BZP	X-ray	1.15	A	1-154	[»]
1BZR	X-ray	1.15	A	1-154	[»]
1CH1	X-ray	1.90	A	1-154	[»]
1CH2	X-ray	1.80	A	1-154	[»]
1CH3	X-ray	2.00	A	1-154	[»]
1CH5	X-ray	2.10	A	1-154	[»]
1CH7	X-ray	1.90	A	1-154	[»]
1CH9	X-ray	1.80	A	1-154	[»]
1CIK	X-ray	1.70	A	1-154	[»]
1CIO	X-ray	1.60	A	1-154	[»]
1CO8	X-ray	1.80	A	1-154	[»]
1CO9	X-ray	1.60	A	1-154	[»]
1CP0	X-ray	2.00	A	1-154	[»]
1CP5	X-ray	2.10	A	1-154	[»]
1CPW	X-ray	2.20	A	1-154	[»]
1CQ2	neutron diffraction	2.00	A	1-154	[»]
1DO1	X-ray	1.50	A	1-154	[»]
1DO3	X-ray	1.55	A	1-154	[»]
1DO4	X-ray	1.70	A	1-154	[»]
1DO7	X-ray	1.85	A	1-154	[»]
1DTI	X-ray	1.70	A	1-154	[»]
1DTM	X-ray	2.13	A	1-154	[»]
1DUK	X-ray	2.13	A	1-154	[»]
1DUO	X-ray	2.00	A	1-154	[»]
1DXC	X-ray	1.40	A	1-154	[»]
1DXD	X-ray	1.40	A	1-154	[»]
1EBC	X-ray	1.80	A	1-154	[»]
1F63	X-ray	1.80	A	1-154	[»]
1F65	X-ray	1.70	A	1-154	[»]
1F6H	X-ray	3.31	A	1-154	[»]
1FCS	X-ray	1.60	A	1-154	[»]
1H1X	X-ray	1.40	A	1-154	[»]
1HJT	X-ray	1.70	A	1-154	[»]
1IOP	X-ray	1.90	A	1-154	[»]
1IRC	X-ray	2.17	A	1-154	[»]
1J3F	X-ray	1.45	A	1-154	[»]
1J52	X-ray	1.90	A	1-154	[»]
1JDO	X-ray	1.90	A	1-154	[»]
1JP6	X-ray	2.30	A	1-154	[»]
1JP8	X-ray	2.30	A	1-154	[»]
1JP9	X-ray	1.70	A	1-154	[»]
1JPB	X-ray	1.70	A	1-154	[»]
1JW8	X-ray	1.30	A	1-154	[»]
1L2K	neutron diffraction	1.50	A	1-154	[»]
1LTW	X-ray	1.70	A	1-154	[»]
1LUE	X-ray	1.70	A	1-154	[»]
1MBC	X-ray	1.50	A	1-154	[»]
1MBD	X-ray	1.40	A	1-154	[»]
1MBI	X-ray	2.00	A	1-154	[»]
1MBN	X-ray	2.00	A	1-154	[»]
1MBO	X-ray	1.60	A	1-154	[»]
1MCY	X-ray	1.70	A	1-154	[»]
1MGN	X-ray	1.90	A	1-154	[»]
1MLF	X-ray	2.00	A	1-154	[»]
1MLG	X-ray	2.00	A	1-154	[»]
1MLH	X-ray	2.00	A	1-154	[»]
1MLJ	X-ray	2.00	A	1-154	[»]
1MLK	X-ray	1.80	A	1-154	[»]
1MLL	X-ray	1.70	A	1-154	[»]
1MLM	X-ray	1.80	A	1-154	[»]
1MLN	X-ray	2.00	A	1-154	[»]
1MLO	X-ray	1.80	A	1-154	[»]
1MLQ	X-ray	2.00	A	1-154	[»]
1MLR	X-ray	2.00	A	1-154	[»]
1MLS	X-ray	1.70	A	1-154	[»]
1MLU	X-ray	1.90	A	1-154	[»]
1MOA	X-ray	1.90	A	1-154	[»]
1MOB	X-ray	2.20	A	1-154	[»]
1MOC	X-ray	2.00	A	1-154	[»]
1MOD	X-ray	2.00	A	1-154	[»]
1MTI	X-ray	1.90	A	1-154	[»]
1MTJ	X-ray	1.70	A	1-154	[»]
1MTK	X-ray	1.80	A	1-154	[»]
1MYF	NMR	-	A	1-154	[»]
1MYM	X-ray	1.70	A	1-154	[»]
1MYZ	X-ray	1.60	A	1-154	[»]
1MZ0	X-ray	1.60	A	1-154	[»]
1N9F	X-ray	1.80	A	1-154	[»]
1N9H	X-ray	1.80	A	1-154	[»]
1N9I	X-ray	1.60	A	1-154	[»]
1N9X	X-ray	1.60	A	1-154	[»]
1NAZ	X-ray	1.04	A	1-154	[»]
1O16	X-ray	1.95	A	1-154	[»]
1OBM	X-ray	1.85	A	1-154	[»]
1OFJ	X-ray	1.80	A	1-154	[»]
1OFK	X-ray	1.80	A	1-154	[»]
1SPE	X-ray	2.00	A	1-154	[»]
1SWM	X-ray	1.80	A	1-154	[»]
1TES	X-ray	1.70	A	1-154	[»]
1U7R	X-ray	1.15	A	1-154	[»]
1U7S	X-ray	1.40	A	1-154	[»]
1UFJ	X-ray	1.60	A	1-154	[»]
1UFP	X-ray	2.10	A	1-154	[»]
1V9Q	X-ray	1.45	A	1-154	[»]
1VXA	X-ray	2.00	A	1-154	[»]
1VXB	X-ray	2.00	A	1-154	[»]
1VXC	X-ray	1.70	A	1-154	[»]
1VXD	X-ray	1.70	A	1-154	[»]
1VXE	X-ray	1.70	A	1-154	[»]
1VXF	X-ray	1.70	A	1-154	[»]
1VXG	X-ray	1.70	A	1-154	[»]
1VXH	X-ray	1.70	A	1-154	[»]
1WVP	X-ray	1.53	A	2-154	[»]
1YOG	X-ray	1.65	A	1-154	[»]
1YOH	X-ray	1.65	A	1-154	[»]
1YOI	X-ray	1.65	A	1-154	[»]
2BLH	X-ray	1.77	A	1-154	[»]
2BLI	X-ray	1.70	A	1-154	[»]
2BLJ	X-ray	1.80	M	1-154	[»]
2BW9	X-ray	1.68	M	1-154	[»]
2BWH	X-ray	1.90	A	1-154	[»]
2CMM	X-ray	1.80	A	1-154	[»]
2D6C	X-ray	2.26	A/B	1-154	[»]
2E2Y	X-ray	1.60	A	1-154	[»]
2EB8	X-ray	1.65	A	1-154	[»]
2EB9	X-ray	1.80	A	1-154	[»]
2EF2	X-ray	1.80	A	1-154	[»]
2EKT	X-ray	1.10	A	2-154	[»]