ID   MYG_BALMY               Reviewed;         154 AA.
AC   R9RZK8;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Myoglobin {ECO:0000303|PubMed:23766330};
GN   Name=MB {ECO:0000303|PubMed:23766330};
OS   Balaena mysticetus (Bowhead whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenidae; Balaena.
OX   NCBI_TaxID=27602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=23766330; DOI=10.1126/science.1234192;
RA   Mirceta S., Signore A.V., Burns J.M., Cossins A.R., Campbell K.L.,
RA   Berenbrink M.;
RT   "Evolution of mammalian diving capacity traced by myoglobin net surface
RT   charge.";
RL   Science 340:1234192-1234192(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RA   Larsen K., Thomsen B., Magalhaes J.P.;
RT   "Cloning of the myoglobin gene from bowhead.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=30442991; DOI=10.1038/s41598-018-34984-6;
RA   Isogai Y., Imamura H., Nakae S., Sumi T., Takahashi K.I., Nakagawa T.,
RA   Tsuneshige A., Shirai T.;
RT   "Tracing whale myoglobin evolution by resurrecting ancient proteins.";
RL   Sci. Rep. 8:16883-16883(2018).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; KC524747; AGM75750.1; -; mRNA.
DR   EMBL; KY471142; AUF74482.1; -; mRNA.
DR   PDB; 5YCI; X-ray; 1.97 A; A/B=1-154.
DR   PDB; 5YCJ; X-ray; 1.58 A; A/B=1-154.
DR   PDBsum; 5YCI; -.
DR   PDBsum; 5YCJ; -.
DR   AlphaFoldDB; R9RZK8; -.
DR   SMR; R9RZK8; -.
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; Heme; Iron; Metal-binding; Muscle protein; Oxygen transport;
KW   Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02185"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000450813"
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:0000269|PubMed:30442991,
FT                   ECO:0007744|PDB:5YCI"
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..18
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:5YCI"
FT   HELIX           22..36
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           53..57
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           60..78
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           103..119
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:5YCJ"
FT   HELIX           126..149
FT                   /evidence="ECO:0007829|PDB:5YCJ"
SQ   SEQUENCE   154 AA;  17207 MW;  D3155A15DEAB8EF0 CRC64;
     MVLSDGEWQL VLNIWAKVEA DVAGHGQDVL IRLFKGHPET LEKFDKFKHL KTEAEMKASE
     DLKKHGNTVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISD AIIHVLHSRH
     PGDFGADAQG AMNKALELFR KDIAAKYKEL GFQG