ID   MYG_RANTA               Reviewed;         154 AA.
AC   C0HJR0;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Myoglobin {ECO:0000303|Ref.1};
GN   Name=MB {ECO:0000250|UniProtKB:P02144};
OS   Rangifer tarandus (Reindeer) (Cervus tarandus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Odocoileinae; Rangifer.
OX   NCBI_TaxID=9870;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154, SUBUNIT, STRUCTURE BY NMR OF 2-154, MASS
RP   SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Muscle {ECO:0000303|Ref.1};
RX   DOI=10.1039/C5RA01316J;
RA   Di Guiseppe A.M.A., Caso J.V., Severino V., Ragucci S., Chambery A.,
RA   Russo R., Fattorusso R., Ferreras J.M., Russo L., Di Maro A.;
RT   "Insight into the structural and functional features of myoglobin from
RT   Hystrix cristata L. and Rangifer tarandus L.";
RL   RSC Adv. 5:26388-26401(2015).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=16923.46; Mass_error=0.08; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; C0HJR0; -.
DR   SMR; C0HJR0; -.
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; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|Ref.1"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000438693"
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;  17055 MW;  E13E47B6C6851761 CRC64;
     MGLSDGEWQL VLNAWGKVEA DVAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE
     DLKKHGNTVL TALGGILKKK GHHEAEVKHL AESHANKHKI PVKYLEFISD AIIHVLHAKH
     PSDFGADAQG AMSKALELFR NDMAAQYKVL GFQG