ID   MYG_ERIEU               Reviewed;         154 AA.
AC   P02156;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RC   TISSUE=Skeletal muscle;
RX   PubMed=1167790; DOI=10.1016/0005-2795(75)90003-3;
RA   Romero-Herrera A.E., Lehmann H., Fakes W.;
RT   "The primary structure of the myoglobin of the insectivore Erinaceus
RT   europaeus (common European hedgehog).";
RL   Biochim. Biophys. Acta 379:13-21(1975).
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; A02476; MYHH.
DR   AlphaFoldDB; P02156; -.
DR   SMR; P02156; -.
DR   STRING; 9365.XP_007535738.1; -.
DR   PRIDE; P02156; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   Proteomes; UP000079721; 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:1167790"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053292"
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"
SQ   SEQUENCE   154 AA;  17115 MW;  B474DEE18212225F CRC64;
     MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKDHPET LEKFDKFKHL KSEDEMKSSE
     DLKKHGTTVL TALGGILKKK GQHEAQLAPL AQSHANKHKI PVKYLEFISE AIIQVLKSKH
     AGDFGADAQG AMSKALELFR NDIAAKYKEL GFQG