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 24-NOV-2009, entry version 44. DE RecName: Full=Myoglobin; GN Name=MB; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE OF 2-154. RC TISSUE=Heart muscle; RX MEDLINE=70064092; PubMed=4902609; RX 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 MEDLINE=90147691; 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 RT bromide cleavage in polyacrylamide gels."; RL Biochem. Biophys. Res. Commun. 166:139-145(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=90294302; 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 RT heart metmyoglobin."; RL J. Mol. Biol. 213:885-897(1990). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=88153746; PubMed=3346247; RA Evans S.V., Brayer G.D.; RT "Horse heart metmyoglobin. A 2.8-A resolution three-dimensional RT structure determination."; RL J. Biol. Chem. 263:4263-4268(1988). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-65. RX MEDLINE=95383313; 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 RT pentacoordinate metmyoglobin variants."; RL Biochemistry 34:10483-10490(1995). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX MEDLINE=20168811; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A91098; MYHO. DR RefSeq; NP_001157488.1; -. DR PDB; 1AZI; X-ray; 2.00 A; A=2-153. DR PDB; 1BJE; X-ray; 1.80 A; A=2-153. 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=2-153. DR PDB; 1HSY; X-ray; 1.90 A; A=2-154. DR PDB; 1NPF; X-ray; 1.90 A; A=2-153. DR PDB; 1NPG; X-ray; 1.70 A; A=2-153. DR PDB; 1NZ2; X-ray; 1.90 A; A=2-153. DR PDB; 1NZ3; X-ray; 1.60 A; A=2-153. DR PDB; 1NZ4; X-ray; 1.80 A; A=2-153. DR PDB; 1NZ5; X-ray; 1.70 A; A=2-153. DR PDB; 1RSE; X-ray; 1.70 A; A=2-153. DR PDB; 1WLA; X-ray; 1.70 A; A=2-153. DR PDB; 1XCH; X-ray; 1.70 A; A=2-153. DR PDB; 1YMA; X-ray; 2.00 A; A=2-153. DR PDB; 1YMB; X-ray; 1.90 A; A=2-154. DR PDB; 1YMC; X-ray; 2.00 A; A=2-153. DR PDB; 2FRF; X-ray; 1.20 A; A=2-153. DR PDB; 2FRI; X-ray; 1.60 A; X=2-153. DR PDB; 2FRJ; X-ray; 1.30 A; X=2-153. DR PDB; 2FRK; X-ray; 1.30 A; X=2-153. 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 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 Ensembl; ENSECAT00000018976; ENSECAP00000015509; ENSECAG00000017982; Equus caballus. DR GeneID; 100054434; -. DR KEGG; ecb:100054434; -. DR CTD; 100054434; -. DR HOVERGEN; P68082; -. DR OMA; FRNDIAA; -. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. DR GO; GO:0015671; P:oxygen transport; IEA:UniProtKB-KW. DR InterPro; IPR012292; Globin. DR InterPro; IPR009050; Globin-like. DR InterPro; IPR000971; Globin_subset. DR InterPro; IPR002335; Myoglobin. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR PANTHER; PTHR11442:SF5; Myoglobin; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00613; MYOGLOBIN. 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; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 154 Myoglobin. FT /FTId=PRO_0000053302. FT METAL 65 65 Iron (heme distal ligand). FT METAL 94 94 Iron (heme proximal ligand). FT CONFLICT 123 123 D -> N (in Ref. 1; AA sequence). FT HELIX 5 20 FT HELIX 22 36 FT HELIX 38 41 FT TURN 45 49 FT HELIX 53 57 FT HELIX 60 77 FT TURN 78 81 FT HELIX 84 96 FT HELIX 102 119 FT HELIX 126 150 SQ SEQUENCE 154 AA; 17083 MW; 20EABC4A66ACE975 CRC64; MGLSDGEWQQ VLNVWGKVEA DIAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE DLKKHGTVVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISD AIIHVLHSKH PGDFGADAQG AMTKALELFR NDIAAKYKEL GFQG //