Myoglobin - Equus caballus (Horse)

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Reviewed, UniProtKB/Swiss-Prot P68082 (MYG_HORSE)

Last modified November 25, 2008. Version 35. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Myoglobin

Gene names

Name:

MB

Organism

Equus caballus (Horse)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

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

Removed

Chain

153

Myoglobin

PRO_0000053302

Sites

Metal binding

1

Iron (heme distal ligand)

Metal binding

1

Iron (heme proximal ligand)

Experimental info

Sequence conflict

1

D → N AA sequence Ref.1

Secondary structure

1

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154

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P68082-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 20EABC4A66ACE975
Show »

154

17,083

        10         20         30         40         50         60 
MGLSDGEWQQ VLNVWGKVEA DIAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE 

        70         80         90        100        110        120 
DLKKHGTVVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISD AIIHVLHSKH 

       130        140        150 
PGDFGADAQG AMTKALELFR NDIAAKYKEL GFQG

References

[1]	"Covalent structure of horse myoglobin." Dautrevaux M., Boulanger Y., Han K., Biserte G. Eur. J. Biochem. 11:267-277(1969) [PubMed: 4902609] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-154. Tissue: Heart muscle.
[2]	"Residue 122 of sperm whale and horse myoglobin." Romero-Herrera A.E., Lehmann H. Biochim. Biophys. Acta 336:318-323(1974) Cited for: PROTEIN SEQUENCE OF 2-154. Tissue: Skeletal muscle.
[3]	"Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels." Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J. Biochem. Biophys. Res. Commun. 166:139-145(1990) [PubMed: 2302197] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16 AND 57-71.
[4]	"High-resolution study of the three-dimensional structure of horse heart metmyoglobin." Evans S.V., Brayer G.D. J. Mol. Biol. 213:885-897(1990) [PubMed: 2359126] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[5]	"Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure determination." Evans S.V., Brayer G.D. J. Biol. Chem. 263:4263-4268(1988) [PubMed: 3346247] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]	"Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants." Bogumil R., Maurus R., Hildebrand D.P., Brayer G.D., Mauk A.G. Biochemistry 34:10483-10490(1995) [PubMed: 7654702] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65.
[7]	"Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin." Chu K., Vojtchovsky J., McMahon B.H., Sweet R.M., Berendzen J., Schlichting I. Nature 403:921-923(2000) [PubMed: 10706294] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

MYHO. A91098.

RefSeq

XP_001500028.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZI	X-ray	2.00	A	1-154	[»]
1BJE	X-ray	1.80	A	1-154	[»]
1DWR	X-ray	1.45	A	1-154	[»]
1DWS	X-ray	1.45	A	1-154	[»]
1DWT	X-ray	1.40	A	1-154	[»]
1GJN	X-ray	1.35	A	1-154	[»]
1HRM	X-ray	1.70	A	1-154	[»]
1HSY	X-ray	1.90	A	1-154	[»]
1NPF	X-ray	1.90	A	1-154	[»]
1NPG	X-ray	1.70	A	1-154	[»]
1NZ2	X-ray	1.90	A	1-154	[»]
1NZ3	X-ray	1.60	A	1-154	[»]
1NZ4	X-ray	1.80	A	1-154	[»]
1NZ5	X-ray	1.70	A	1-154	[»]
1RSE	X-ray	1.70	A	1-154	[»]
1WLA	X-ray	1.70	A	1-154	[»]
1XCH	X-ray	1.70	A	1-154	[»]
1YMA	X-ray	2.00	A	1-154	[»]
1YMB	X-ray	1.90	A	1-154	[»]
1YMC	X-ray	2.00	A	1-154	[»]
2FRF	X-ray	1.20	A	2-154	[»]
2FRI	X-ray	1.60	X	2-154	[»]
2FRJ	X-ray	1.30	X	2-154	[»]
2FRK	X-ray	1.30	X	2-154	[»]
2IN4	X-ray	2.15	A	1-154	[»]
2NSR	X-ray	1.90	A	2-154	[»]
2NSS	X-ray	2.00	A	2-154	[»]
2O58	X-ray	1.65	X	2-154	[»]
2O5B	X-ray	2.00	X	2-154	[»]
2O5L	X-ray	1.70	X	2-154	[»]
2O5M	X-ray	1.65	X	2-154	[»]
2O5O	X-ray	1.60	X	2-154	[»]
2O5Q	X-ray	1.90	X	2-154	[»]
2O5S	X-ray	1.60	X	2-154	[»]
2O5T	X-ray	1.60	X	2-154	[»]
2V1E	X-ray	1.30	A	2-154	[»]
2V1F	X-ray	1.20	A	2-154	[»]
2V1G	X-ray	1.35	A	2-154	[»]
2V1H	X-ray	1.30	A	2-154	[»]
2V1I	X-ray	1.20	A	2-154	[»]
2V1J	X-ray	1.40	A	2-154	[»]
2V1K	X-ray	1.25	A	2-154	[»]
2VLY	X-ray	1.60	A	2-154	[»]
2VLZ	X-ray	1.50	A	2-154	[»]
2VM0	X-ray	1.60	A	2-154	[»]

ModBase

Genome annotation databases

GeneID

Phylogenomic databases

HOVERGEN

Family and domain databases

InterPro

IPR012292. Globin.
IPR000971. Globin_subset.
IPR002335. Myoglobin.
[Graphical view]

Gene3D

G3DSA:1.10.490.10. Globin_related. 1 hit.

PANTHER

PTHR11442:SF5. Myoglobin. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00613. MYOGLOBIN.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Other Resources

LinkHub

Entry information

Entry name

MYG_HORSE

Accession

Primary (citable) accession number: P68082
Secondary accession number(s): P02188

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 35 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents