MYG_HORSE
ID MYG_HORSE Reviewed; 154 AA.
AC P68082; P02188;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 2-154.
RC TISSUE=Heart muscle;
RX PubMed=4902609; DOI=10.1111/j.1432-1033.1969.tb00769.x;
RA Dautrevaux M., Boulanger Y., Han K., Biserte G.;
RT "Covalent structure of horse myoglobin.";
RL Eur. J. Biochem. 11:267-277(1969).
RN [2]
RP PROTEIN SEQUENCE OF 2-154.
RC TISSUE=Skeletal muscle;
RA Romero-Herrera A.E., Lehmann H.;
RT "Residue 122 of sperm whale and horse myoglobin.";
RL Biochim. Biophys. Acta 336:318-323(1974).
RN [3]
RP PROTEIN SEQUENCE OF 2-16 AND 57-71.
RX PubMed=2302197; DOI=10.1016/0006-291x(90)91922-f;
RA Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.;
RT "Internal amino acid sequencing of proteins by in situ cyanogen bromide
RT cleavage in polyacrylamide gels.";
RL Biochem. Biophys. Res. Commun. 166:139-145(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX PubMed=2359126; DOI=10.1016/s0022-2836(05)80270-0;
RA Evans S.V., Brayer G.D.;
RT "High-resolution study of the three-dimensional structure of horse heart
RT metmyoglobin.";
RL J. Mol. Biol. 213:885-897(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=3346247; DOI=10.1016/s0021-9258(18)68919-7;
RA Evans S.V., Brayer G.D.;
RT "Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure
RT determination.";
RL J. Biol. Chem. 263:4263-4268(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65.
RX PubMed=7654702; DOI=10.1021/bi00033a021;
RA Bogumil R., Maurus R., Hildebrand D.P., Brayer G.D., Mauk A.G.;
RT "Origin of the pH-dependent spectroscopic properties of pentacoordinate
RT metmyoglobin variants.";
RL Biochemistry 34:10483-10490(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX PubMed=10706294; DOI=10.1038/35002641;
RA Chu K., Vojtchovsky J., McMahon B.H., Sweet R.M., Berendzen J.,
RA Schlichting I.;
RT "Structure of a ligand-binding intermediate in wild-type carbonmonoxy
RT myoglobin.";
RL Nature 403:921-923(2000).
CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC movement of oxygen within muscles.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A91098; MYHO.
DR RefSeq; NP_001157488.1; NM_001164016.1.
DR PDB; 1AZI; X-ray; 2.00 A; A=2-154.
DR PDB; 1BJE; X-ray; 1.80 A; A=2-154.
DR PDB; 1DWR; X-ray; 1.45 A; A=2-154.
DR PDB; 1DWS; X-ray; 1.45 A; A=2-154.
DR PDB; 1DWT; X-ray; 1.40 A; A=2-154.
DR PDB; 1GJN; X-ray; 1.35 A; A=2-154.
DR PDB; 1HRM; X-ray; 1.70 A; A=2-154.
DR PDB; 1HSY; X-ray; 1.90 A; A=2-154.
DR PDB; 1NPF; X-ray; 1.90 A; A=2-154.
DR PDB; 1NPG; X-ray; 1.70 A; A=2-154.
DR PDB; 1NZ2; X-ray; 1.90 A; A=2-154.
DR PDB; 1NZ3; X-ray; 1.60 A; A=2-154.
DR PDB; 1NZ4; X-ray; 1.80 A; A=2-154.
DR PDB; 1NZ5; X-ray; 1.70 A; A=2-154.
DR PDB; 1RSE; X-ray; 1.70 A; A=2-154.
DR PDB; 1WLA; X-ray; 1.70 A; A=2-154.
DR PDB; 1XCH; X-ray; 1.70 A; A=2-154.
DR PDB; 1YMA; X-ray; 2.00 A; A=2-154.
DR PDB; 1YMB; X-ray; 1.90 A; A=2-154.
DR PDB; 1YMC; X-ray; 2.00 A; A=2-154.
DR PDB; 2FRF; X-ray; 1.20 A; A=2-154.
DR PDB; 2FRI; X-ray; 1.60 A; X=2-154.
DR PDB; 2FRJ; X-ray; 1.30 A; X=2-154.
DR PDB; 2FRK; X-ray; 1.30 A; X=2-154.
DR PDB; 2IN4; X-ray; 2.15 A; A=2-154.
DR PDB; 2NSR; X-ray; 1.90 A; A=2-154.
DR PDB; 2NSS; X-ray; 2.00 A; A=2-154.
DR PDB; 2O58; X-ray; 1.65 A; X=2-154.
DR PDB; 2O5B; X-ray; 2.00 A; X=2-154.
DR PDB; 2O5L; X-ray; 1.70 A; X=2-154.
DR PDB; 2O5M; X-ray; 1.65 A; X=2-154.
DR PDB; 2O5O; X-ray; 1.60 A; X=2-154.
DR PDB; 2O5Q; X-ray; 1.90 A; X=2-154.
DR PDB; 2O5S; X-ray; 1.60 A; X=2-154.
DR PDB; 2O5T; X-ray; 1.60 A; X=2-154.
DR PDB; 2V1E; X-ray; 1.30 A; A=2-154.
DR PDB; 2V1F; X-ray; 1.20 A; A=2-154.
DR PDB; 2V1G; X-ray; 1.35 A; A=2-154.
DR PDB; 2V1H; X-ray; 1.30 A; A=2-154.
DR PDB; 2V1I; X-ray; 1.20 A; A=2-154.
DR PDB; 2V1J; X-ray; 1.40 A; A=2-154.
DR PDB; 2V1K; X-ray; 1.25 A; A=2-154.
DR PDB; 2VLX; X-ray; 1.30 A; A=2-154.
DR PDB; 2VLY; X-ray; 1.60 A; A=2-154.
DR PDB; 2VLZ; X-ray; 1.50 A; A=2-154.
DR PDB; 2VM0; X-ray; 1.60 A; A=2-154.
DR PDB; 3BA2; X-ray; 1.80 A; A=2-154.
DR PDB; 3HC9; X-ray; 2.00 A; A=2-154.
DR PDB; 3HEN; X-ray; 1.90 A; A=2-154.
DR PDB; 3HEO; X-ray; 2.00 A; A=2-154.
DR PDB; 3HEP; X-ray; 1.95 A; A=2-154.
DR PDB; 3LR7; X-ray; 1.60 A; A=2-154.
DR PDB; 3LR9; X-ray; 1.55 A; A=2-154.
DR PDB; 3RJ6; X-ray; 1.23 A; A/B=2-154.
DR PDB; 3RJN; X-ray; 1.90 A; B=2-154.
DR PDB; 3V2V; X-ray; 1.65 A; A=2-154.
DR PDB; 3V2Z; X-ray; 1.65 A; A=2-154.
DR PDB; 3VAU; X-ray; 1.70 A; A=2-154.
DR PDB; 3VM9; X-ray; 1.05 A; A/B=2-154.
DR PDB; 3WFT; X-ray; 1.30 A; A=2-154.
DR PDB; 3WFU; X-ray; 1.35 A; A=2-154.
DR PDB; 3WI8; X-ray; 2.20 A; A=2-154.
DR PDB; 3WYO; X-ray; 2.00 A; A/B/C/D=2-154.
DR PDB; 4DC7; X-ray; 1.50 A; A=2-153.
DR PDB; 4DC8; X-ray; 1.50 A; A=2-153.
DR PDB; 4NS2; X-ray; 1.18 A; A=1-154.
DR PDB; 4TWU; X-ray; 1.08 A; A=1-154.
DR PDB; 4TWV; X-ray; 1.06 A; A=1-154.
DR PDB; 5AZQ; X-ray; 1.40 A; A=2-154.
DR PDB; 5AZR; X-ray; 1.20 A; A=2-154.
DR PDB; 5CMV; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN4; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN5; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN6; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN7; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN8; X-ray; 1.80 A; A=2-153.
DR PDB; 5CN9; X-ray; 1.80 A; A=2-153.
DR PDB; 5CNB; X-ray; 1.80 A; A=2-153.
DR PDB; 5CNC; X-ray; 1.80 A; A=2-153.
DR PDB; 5CND; X-ray; 1.80 A; A=2-153.
DR PDB; 5CNE; X-ray; 1.80 A; A=2-153.
DR PDB; 5CNF; X-ray; 1.80 A; A=2-153.
DR PDB; 5CNG; X-ray; 1.80 A; A=2-153.
DR PDB; 5D5R; X-ray; 1.60 A; A=2-153.
DR PDB; 5YCG; X-ray; 2.40 A; A=1-154.
DR PDB; 5YL3; X-ray; 1.50 A; A=1-154.
DR PDB; 5Z7E; X-ray; 1.80 A; A=2-154.
DR PDB; 5Z7F; X-ray; 1.90 A; A=2-154.
DR PDB; 5ZZE; X-ray; 1.42 A; A=2-153.
DR PDB; 6LS8; X-ray; 2.30 A; A/C/E/G/I/K=2-154.
DR PDB; 6LTL; X-ray; 1.25 A; A/B=2-154.
DR PDB; 6LTM; X-ray; 1.65 A; A/B=2-154.
DR PDB; 7DGJ; X-ray; 1.60 A; A/B=2-154.
DR PDB; 7DGK; X-ray; 1.75 A; A/B=2-154.
DR PDB; 7DGL; X-ray; 1.91 A; A/B=2-154.
DR PDB; 7DGM; X-ray; 1.62 A; A/B=2-154.
DR PDB; 7DGN; X-ray; 2.35 A; A/B=2-154.
DR PDB; 7DGO; X-ray; 2.00 A; A/B=2-154.
DR PDBsum; 1AZI; -.
DR PDBsum; 1BJE; -.
DR PDBsum; 1DWR; -.
DR PDBsum; 1DWS; -.
DR PDBsum; 1DWT; -.
DR PDBsum; 1GJN; -.
DR PDBsum; 1HRM; -.
DR PDBsum; 1HSY; -.
DR PDBsum; 1NPF; -.
DR PDBsum; 1NPG; -.
DR PDBsum; 1NZ2; -.
DR PDBsum; 1NZ3; -.
DR PDBsum; 1NZ4; -.
DR PDBsum; 1NZ5; -.
DR PDBsum; 1RSE; -.
DR PDBsum; 1WLA; -.
DR PDBsum; 1XCH; -.
DR PDBsum; 1YMA; -.
DR PDBsum; 1YMB; -.
DR PDBsum; 1YMC; -.
DR PDBsum; 2FRF; -.
DR PDBsum; 2FRI; -.
DR PDBsum; 2FRJ; -.
DR PDBsum; 2FRK; -.
DR PDBsum; 2IN4; -.
DR PDBsum; 2NSR; -.
DR PDBsum; 2NSS; -.
DR PDBsum; 2O58; -.
DR PDBsum; 2O5B; -.
DR PDBsum; 2O5L; -.
DR PDBsum; 2O5M; -.
DR PDBsum; 2O5O; -.
DR PDBsum; 2O5Q; -.
DR PDBsum; 2O5S; -.
DR PDBsum; 2O5T; -.
DR PDBsum; 2V1E; -.
DR PDBsum; 2V1F; -.
DR PDBsum; 2V1G; -.
DR PDBsum; 2V1H; -.
DR PDBsum; 2V1I; -.
DR PDBsum; 2V1J; -.
DR PDBsum; 2V1K; -.
DR PDBsum; 2VLX; -.
DR PDBsum; 2VLY; -.
DR PDBsum; 2VLZ; -.
DR PDBsum; 2VM0; -.
DR PDBsum; 3BA2; -.
DR PDBsum; 3HC9; -.
DR PDBsum; 3HEN; -.
DR PDBsum; 3HEO; -.
DR PDBsum; 3HEP; -.
DR PDBsum; 3LR7; -.
DR PDBsum; 3LR9; -.
DR PDBsum; 3RJ6; -.
DR PDBsum; 3RJN; -.
DR PDBsum; 3V2V; -.
DR PDBsum; 3V2Z; -.
DR PDBsum; 3VAU; -.
DR PDBsum; 3VM9; -.
DR PDBsum; 3WFT; -.
DR PDBsum; 3WFU; -.
DR PDBsum; 3WI8; -.
DR PDBsum; 3WYO; -.
DR PDBsum; 4DC7; -.
DR PDBsum; 4DC8; -.
DR PDBsum; 4NS2; -.
DR PDBsum; 4TWU; -.
DR PDBsum; 4TWV; -.
DR PDBsum; 5AZQ; -.
DR PDBsum; 5AZR; -.
DR PDBsum; 5CMV; -.
DR PDBsum; 5CN4; -.
DR PDBsum; 5CN5; -.
DR PDBsum; 5CN6; -.
DR PDBsum; 5CN7; -.
DR PDBsum; 5CN8; -.
DR PDBsum; 5CN9; -.
DR PDBsum; 5CNB; -.
DR PDBsum; 5CNC; -.
DR PDBsum; 5CND; -.
DR PDBsum; 5CNE; -.
DR PDBsum; 5CNF; -.
DR PDBsum; 5CNG; -.
DR PDBsum; 5D5R; -.
DR PDBsum; 5YCG; -.
DR PDBsum; 5YL3; -.
DR PDBsum; 5Z7E; -.
DR PDBsum; 5Z7F; -.
DR PDBsum; 5ZZE; -.
DR PDBsum; 6LS8; -.
DR PDBsum; 6LTL; -.
DR PDBsum; 6LTM; -.
DR PDBsum; 7DGJ; -.
DR PDBsum; 7DGK; -.
DR PDBsum; 7DGL; -.
DR PDBsum; 7DGM; -.
DR PDBsum; 7DGN; -.
DR PDBsum; 7DGO; -.
DR AlphaFoldDB; P68082; -.
DR BMRB; P68082; -.
DR PCDDB; P68082; -.
DR SASBDB; P68082; -.
DR SMR; P68082; -.
DR STRING; 9796.ENSECAP00000015509; -.
DR Allergome; 10877; Equ c Myoglobin.
DR CarbonylDB; P68082; -.
DR CPTAC; CPTAC-1474; -.
DR PaxDb; P68082; -.
DR PRIDE; P68082; -.
DR ABCD; P68082; 1 sequenced antibody.
DR Ensembl; ENSECAT00000036478; ENSECAP00000026577; ENSECAG00000017982.
DR GeneID; 100054434; -.
DR KEGG; ecb:100054434; -.
DR CTD; 4151; -.
DR VGNC; VGNC:20004; MB.
DR GeneTree; ENSGT00940000160809; -.
DR HOGENOM; CLU_003827_18_0_1; -.
DR InParanoid; P68082; -.
DR OMA; MRLFQDH; -.
DR OrthoDB; 1405713at2759; -.
DR TreeFam; TF332967; -.
DR SABIO-RK; P68082; -.
DR EvolutionaryTrace; P68082; -.
DR Proteomes; UP000002281; Chromosome 28.
DR Bgee; ENSECAG00000017982; Expressed in gluteus medius and 12 other tissues.
DR ExpressionAtlas; P68082; baseline.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0015671; P:oxygen transport; IBA:GO_Central.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR002335; Myoglobin.
DR PANTHER; PTHR47132; PTHR47132; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00613; MYOGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Muscle protein; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2302197,
FT ECO:0000269|PubMed:4902609, ECO:0000269|Ref.2"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /id="PRO_0000053302"
FT BINDING 65
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000269|PubMed:7654702"
FT BINDING 94
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:10706294,
FT ECO:0000269|PubMed:2359126, ECO:0000269|PubMed:7654702,
FT ECO:0007744|PDB:1AZI, ECO:0007744|PDB:1BJE,
FT ECO:0007744|PDB:1DWR, ECO:0007744|PDB:1DWS,
FT ECO:0007744|PDB:1DWT, ECO:0007744|PDB:1GJN,
FT ECO:0007744|PDB:1HSY, ECO:0007744|PDB:1NPF,
FT ECO:0007744|PDB:1NPG, ECO:0007744|PDB:1NZ2,
FT ECO:0007744|PDB:1NZ3, ECO:0007744|PDB:1NZ4,
FT ECO:0007744|PDB:1NZ5, ECO:0007744|PDB:1RSE,
FT ECO:0007744|PDB:1WLA, ECO:0007744|PDB:1XCH,
FT ECO:0007744|PDB:1YMA, ECO:0007744|PDB:1YMB,
FT ECO:0007744|PDB:2FRF, ECO:0007744|PDB:2FRI,
FT ECO:0007744|PDB:2FRJ, ECO:0007744|PDB:2FRK,
FT ECO:0007744|PDB:2NSR, ECO:0007744|PDB:2NSS,
FT ECO:0007744|PDB:2V1E, ECO:0007744|PDB:2V1F,
FT ECO:0007744|PDB:2V1G, ECO:0007744|PDB:2V1H,
FT ECO:0007744|PDB:2V1I, ECO:0007744|PDB:2V1J,
FT ECO:0007744|PDB:2V1K, ECO:0007744|PDB:2VLX,
FT ECO:0007744|PDB:2VLY, ECO:0007744|PDB:2VLZ,
FT ECO:0007744|PDB:2VM0, ECO:0007744|PDB:3HC9,
FT ECO:0007744|PDB:3HEN, ECO:0007744|PDB:3HEO,
FT ECO:0007744|PDB:3HEP, ECO:0007744|PDB:3LR7,
FT ECO:0007744|PDB:3LR9, ECO:0007744|PDB:3RJ6,
FT ECO:0007744|PDB:3VM9, ECO:0007744|PDB:3WYO,
FT ECO:0007744|PDB:4DC7, ECO:0007744|PDB:4DC8,
FT ECO:0007744|PDB:4NS2"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ76"
FT CONFLICT 123
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 60..96
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3VM9"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3VM9"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:3VM9"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:5AZQ"
SQ SEQUENCE 154 AA; 17083 MW; 20EABC4A66ACE975 CRC64;
MGLSDGEWQQ VLNVWGKVEA DIAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE
DLKKHGTVVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISD AIIHVLHSKH
PGDFGADAQG AMTKALELFR NDIAAKYKEL GFQG
