ID   MYG_DELLE               Reviewed;         154 AA.
AC   P83682;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Muscle;
RX   PubMed=15050527; DOI=10.1016/j.cbpc.2004.01.007;
RA   Stewart J.M., Blakely J.A., Karpowicz P.A., Kalanxhi E., Thatcher B.J.,
RA   Martin B.M.;
RT   "Unusually weak oxygen binding, physical properties, partial sequence,
RT   autoxidation rate and a potential phosphorylation site of beluga whale
RT   (Delphinapterus leucas) myoglobin.";
RL   Comp. Biochem. Physiol. 137B:401-412(2004).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000269|PubMed:15050527,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15050527, ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=17081; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15050527};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238, ECO:0000305}.
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DR   MINT; P83682; -.
DR   STRING; 9749.P83682; -.
DR   Proteomes; UP000248483; 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:0000269|PubMed:15050527"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053288"
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;  17178 MW;  1E15AF7A74E66A45 CRC64;
     MGLSEGEWQL VLXXXXKVEA DLAGHGQDVL IRLFKGHPET LEKFDKFKHL KTXXXMKASE
     DLKKHGNTVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLXXXXE AIIHVLHSRH
     PAEFGADAQG AMNKALELFR KDIAAKYKEL GFHG