Myoglobin - Equus caballus (Horse)

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P68082 (MYG_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Myoglobin

Gene names

Name:

Organism

Equus caballus (Horse) [Reference proteome]

Taxonomic identifier

9796 [NCBI]

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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brown fat cell differentiation Inferred from electronic annotation. Source: Compara enucleate erythrocyte differentiation Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara
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

Removed Ref.1 Ref.2 Ref.3

Chain

2 – 154

153

Myoglobin

PRO_0000053302

Sites

Metal binding

Iron (heme distal ligand)

Metal binding

Iron (heme proximal ligand)

Experimental info

Sequence conflict

123

D → N AA sequence Ref.1

Secondary structure

154

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P68082 [UniParc].

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

FASTA

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

« Hide

References

[1]	"Covalent structure of horse myoglobin." Dautrevaux M., Boulanger Y., Han K., Biserte G. Eur. J. Biochem. 11:267-277(1969) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

MYHO. A91098.

RefSeq

NP_001157488.1. NM_001164016.1.

UniGene

Eca.16922.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZI	X-ray	2.00	A	2-153	[»]
1BJE	X-ray	1.80	A	2-153	[»]
1DWR	X-ray	1.45	A	2-154	[»]
1DWS	X-ray	1.45	A	2-154	[»]
1DWT	X-ray	1.40	A	2-154	[»]
1GJN	X-ray	1.35	A	2-154	[»]
1HRM	X-ray	1.70	A	2-153	[»]
1HSY	X-ray	1.90	A	2-154	[»]
1NPF	X-ray	1.90	A	2-153	[»]
1NPG	X-ray	1.70	A	2-153	[»]
1NZ2	X-ray	1.90	A	2-153	[»]
1NZ3	X-ray	1.60	A	2-153	[»]
1NZ4	X-ray	1.80	A	2-153	[»]
1NZ5	X-ray	1.70	A	2-153	[»]
1RSE	X-ray	1.70	A	2-153	[»]
1WLA	X-ray	1.70	A	2-153	[»]
1XCH	X-ray	1.70	A	2-153	[»]
1YMA	X-ray	2.00	A	2-153	[»]
1YMB	X-ray	1.90	A	2-154	[»]
1YMC	X-ray	2.00	A	2-153	[»]
2FRF	X-ray	1.20	A	2-153	[»]
2FRI	X-ray	1.60	X	2-153	[»]
2FRJ	X-ray	1.30	X	2-153	[»]
2FRK	X-ray	1.30	X	2-153	[»]
2IN4	X-ray	2.15	A	2-154	[»]
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	[»]
2VLX	X-ray	1.30	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	[»]
3BA2	X-ray	1.80	A	2-154	[»]
3HC9	X-ray	2.00	A	2-154	[»]
3HEN	X-ray	1.90	A	2-154	[»]
3HEO	X-ray	2.00	A	2-154	[»]
3HEP	X-ray	1.95	A	2-154	[»]
3LR7	X-ray	1.60	A	2-154	[»]
3LR9	X-ray	1.55	A	2-154	[»]
3RJ6	X-ray	1.23	A/B	2-154	[»]
3RJN	X-ray	1.90	B	2-154	[»]
3V2V	X-ray	1.65	A	2-154	[»]
3V2Z	X-ray	1.65	A	2-154	[»]
3VAU	X-ray	1.70	A	2-154	[»]
3VM9	X-ray	1.05	A/B	2-154	[»]
4DC7	X-ray	1.50	A	2-153	[»]
4DC8	X-ray	1.50	A	2-153	[»]

ProteinModelPortal

P68082.

SMR

P68082. Positions 2-154.

ModBase

Search...

Proteomic databases

PRIDE

P68082.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSECAT00000018976; ENSECAP00000015509; ENSECAG00000017982.

GeneID

100054434.

KEGG

ecb:100054434.

Organism-specific databases

CTD

4151.

Phylogenomic databases

eggNOG

NOG276460.

GeneTree

ENSGT00650000093060.

HOGENOM

HOG000070111.

HOVERGEN

HBG107340.

InParanoid

P68082.

OMA

FRNDIAA.

OrthoDB

EOG4Z8XXZ.

Enzyme and pathway databases

SABIO-RK

P68082.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002335. Myoglobin.
[Graphical view]

PANTHER

PTHR11442:SF5. PTHR11442:SF5. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00613. MYOGLOBIN.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P68082.

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:	April 3, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents