ID   MYG_BISBI               Reviewed;         154 AA.
AC   P86873;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Myoglobin {ECO:0000303|PubMed:20374756};
GN   Name=MB {ECO:0000250|UniProtKB:P02192};
OS   Bison bison (American bison) (Bos bison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bison.
OX   NCBI_TaxID=9901;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-154, AND MASS SPECTROMETRY.
RC   TISSUE=Heart {ECO:0000269|PubMed:20374756};
RX   PubMed=20374756; DOI=10.1016/j.meatsci.2009.08.014;
RA   Joseph P., Suman S.P., Li S., Beach C.M., Steinke L., Fontaine M.;
RT   "Characterization of bison (Bison bison) myoglobin.";
RL   Meat Sci. 84:71-78(2010).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=16949; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20374756};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P86873; -.
DR   SMR; P86873; -.
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; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Muscle protein;
KW   Oxygen transport; Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:20374756"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000404696"
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:0000305"
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:0000305"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ76"
FT   MOD_RES         68
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04247"
SQ   SEQUENCE   154 AA;  17078 MW;  E74911B6C6851761 CRC64;
     MGLSDGEWQL VLNAWGKVEA DVAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE
     DLKKHGNTVL TALGGILKKK GHHEAEVKHL AESHANKHKI PVKYLEFISD AIIHVLHAKH
     PSDFGADAQA AMSKALELFR NDMAAQYKVL GFHG