ID   MYG_DRONO               Reviewed;         154 AA.
AC   P86874;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Myoglobin {ECO:0000303|PubMed:20621424};
GN   Name=MB {ECO:0000250|UniProtKB:P85077};
OS   Dromaius novaehollandiae (Emu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX   NCBI_TaxID=8790;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-154, AND MASS SPECTROMETRY.
RC   TISSUE=Muscle {ECO:0000269|PubMed:20621424};
RX   PubMed=20621424; DOI=10.1016/j.meatsci.2010.04.041;
RA   Suman S.P., Joseph P., Li S., Beach C.M., Fontaine M., Steinke L.;
RT   "Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae)
RT   skeletal muscle.";
RL   Meat Sci. 86:623-628(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=17380; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20621424};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P86874; -.
DR   SMR; P86874; -.
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; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:20621424"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000404698"
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"
SQ   SEQUENCE   154 AA;  17507 MW;  EBBFB7166C4497E3 CRC64;
     MGLSDQEWQH VLTIWGKVES DLAGHGHEIL MRLFHDLPET LDRFERFKGL TTPDQMKASE
     ELKKHGVTVL TQLGKILKLK GKHEAELKPL AQTHATKHKI PVKYLEFISE VIIKVIAEKH
     SADFGADSQA AMKKALELFR NDMASKYKEF GFQG