ID   MYG_CANLF               Reviewed;         154 AA.
AC   P63113; P02158;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=1252463; DOI=10.1016/0005-2795(76)90329-9;
RA   Dumur V., Dautrevaux M., Han K.;
RT   "The covalent structure of dog myoglobin.";
RL   Biochim. Biophys. Acta 420:376-386(1976).
RN   [2]
RP   ERRATUM OF PUBMED:1252463, AND SEQUENCE REVISION.
RA   Dumur V., Dautrevaux M., Han K.;
RL   Biochim. Biophys. Acta 427:759-761(1976).
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; A90606; MYDG.
DR   AlphaFoldDB; P63113; -.
DR   SMR; P63113; -.
DR   STRING; 9612.ENSCAFP00000002477; -.
DR   PaxDb; P63113; -.
DR   PRIDE; P63113; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P63113; -.
DR   Proteomes; UP000002254; 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:1252463"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053282"
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;  17337 MW;  3DE77C691A2AB0B8 CRC64;
     MGLSDGEWQI VLNIWGKVET DLAGHGQEVL IRLFKNHPET LDKFDKFKHL KTEDEMKGSE
     DLKKHGNTVL TALGGILKKK GHHEAELKPL AQSHATKHKI PVKYLEFISD AIIQVLQSKH
     SGDFHADTEA AMKKALELFR NDIAAKYKEL GFQG