ID   MYG_THUAL               Reviewed;         147 AA.
AC   P02205; Q9DGI7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Myoglobin;
GN   Name=mb;
OS   Thunnus albacares (Yellowfin tuna) (Neothunnus macropterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=11247835; DOI=10.1152/ajpregu.2001.280.4.r1123;
RA   Marcinek D.J., Bonaventura J., Wittenberg J.B., Block B.A.;
RT   "Oxygen affinity and amino acid sequence of myoglobins from endothermic and
RT   ectothermic fish.";
RL   Am. J. Physiol. 280:R1123-R1133(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147, AND ACETYLATION AT ALA-2.
RX   PubMed=7430163; DOI=10.1016/s0021-9258(19)70394-9;
RA   Watts D.A., Rice R.H., Brown W.D.;
RT   "The primary structure of myoglobin from yellowfin tuna (Thunnus
RT   albacares).";
RL   J. Biol. Chem. 255:10916-10924(1980).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS).
RX   PubMed=15299440; DOI=10.1107/s0907444993014271;
RA   Birnbaum G.I., Evans S.V., Przybylska M., Rose D.R.;
RT   "1.70-A resolution structure of myoglobin from yellowfin tuna. An example
RT   of a myoglobin lacking the D helix.";
RL   Acta Crystallogr. D 50:283-289(1994).
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   EMBL; AF291838; AAG02112.1; -; mRNA.
DR   PIR; A02526; MYTUY.
DR   PDB; 1MYT; X-ray; 1.74 A; A=2-147.
DR   PDBsum; 1MYT; -.
DR   AlphaFoldDB; P02205; -.
DR   SMR; P02205; -.
DR   iPTMnet; P02205; -.
DR   EvolutionaryTrace; P02205; -.
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; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Muscle protein; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7430163"
FT   CHAIN           2..147
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053375"
FT   BINDING         60
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         89
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7430163"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           12..15
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           18..32
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           34..39
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   TURN            41..45
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           55..73
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           79..91
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           98..114
FT                   /evidence="ECO:0007829|PDB:1MYT"
FT   HELIX           119..143
FT                   /evidence="ECO:0007829|PDB:1MYT"
SQ   SEQUENCE   147 AA;  15660 MW;  3D13814403B48D44 CRC64;
     MADFDAVLKC WGPVEADYTT MGGLVLTRLF KEHPETQKLF PKFAGIAQAD IAGNAAISAH
     GATVLKKLGE LLKAKGSHAA ILKPLANSHA TKHKIPINNF KLISEVLVKV MHEKAGLDAG
     GQTALRNVMG IIIADLEANY KELGFSG