ID   MYG_SCIVU               Reviewed;         154 AA.
AC   C0HKB7;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Myoglobin {ECO:0000303|PubMed:28216225};
GN   Name=MB;
OS   Sciurus vulgaris (Eurasian red squirrel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Sciurinae; Sciurini; Sciurus.
OX   NCBI_TaxID=55149;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-154, 3D-STRUCTURE MODELING, NMR, MASS SPECTROMETRY,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Heart muscle {ECO:0000303|PubMed:28216225}, and
RC   Skeletal muscle {ECO:0000303|PubMed:28216225};
RX   PubMed=28216225; DOI=10.1016/j.bbapap.2017.02.011;
RA   Di Giuseppe A.M., Russo L., Russo R., Ragucci S., Caso J.V., Isernia C.,
RA   Chambery A., Di Maro A.;
RT   "Molecular characterization of myoglobin from Sciurus vulgaris
RT   meridionalis: Primary structure, kinetics and spectroscopic studies.";
RL   Biochim. Biophys. Acta 1865:499-509(2017).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=16949.59; Mass_error=0.02; Method=Electrospray;
CC       Note=Apo-myoglobin.; Evidence={ECO:0000269|PubMed:28216225};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; C0HKB7; -.
DR   SMR; C0HKB7; -.
DR   Proteomes; UP000694564; Unplaced.
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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:28216225"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /evidence="ECO:0000269|PubMed:28216225"
FT                   /id="PRO_0000439883"
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:0000255|PROSITE-ProRule:PRU00238"
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:0000255|PROSITE-ProRule:PRU00238"
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;  17081 MW;  0EC70A1E70B24A74 CRC64;
     MGLSDGEWQL VLKVWGKVEA DIAGHGQEVL IRLFKDHPET LEKFDKFKNL KTEDEMKASE
     DLKKHGSTVL GALGGILKKK GQHEAEIKPL AQSHATKHKI PVKYLEFISE AIIQVLKSKH
     SGDFGADAQG AMSKALELFR NDIAAKYKEL GFQG