ID   MYG_KOGSI               Reviewed;         154 AA.
AC   P02184;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Kogia sima (Dwarf sperm whale) (Physeter simus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Kogia.
OX   NCBI_TaxID=9752;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=843520; DOI=10.1021/bi00624a010;
RA   Dwulet F.E., Jones B.N., Lehman L.D., Gurd F.R.N.;
RT   "The complete amino acid sequence of the major component myoglobin of dwarf
RT   sperm whale (Kogia simus).";
RL   Biochemistry 16:873-877(1977).
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. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A90407; MYWHW.
DR   PDB; 6BMG; X-ray; 1.88 A; A/B=1-154.
DR   PDBsum; 6BMG; -.
DR   AlphaFoldDB; P02184; -.
DR   BMRB; P02184; -.
DR   SMR; P02184; -.
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   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Muscle protein; Oxygen transport; Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:843520"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053307"
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   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   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"
FT   HELIX           5..20
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           22..36
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           38..43
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           60..78
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:6BMG"
FT   HELIX           126..149
FT                   /evidence="ECO:0007829|PDB:6BMG"
SQ   SEQUENCE   154 AA;  17368 MW;  FE5119EFE32E265D CRC64;
     MVLSEGEWQL VLHVWAKVEA DIAGHGQDIL IRLFKHHPET LEKFDRFKHL KSEAEMKASE
     DLKKHGVTVL TALGAILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISE AIIHVLHSRH
     PADFGADAQG AMSKALELFR KDIAAKYKEL GYQG