MYG_THUOR
ID MYG_THUOR Reviewed; 147 AA.
AC P68190; Q9DD47;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Myoglobin;
GN Name=mb;
OS Thunnus orientalis (North Pacific bluefin tuna) (Thunnus thynnus
OS orientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX NCBI_TaxID=8238;
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).
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; AF291836; AAG02110.1; -; mRNA.
DR PDB; 2NRL; X-ray; 0.91 A; A=2-147.
DR PDB; 2NX0; X-ray; 0.95 A; A=2-147.
DR PDBsum; 2NRL; -.
DR PDBsum; 2NX0; -.
DR AlphaFoldDB; P68190; -.
DR SMR; P68190; -.
DR EvolutionaryTrace; P68190; -.
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 Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..147
FT /note="Myoglobin"
FT /id="PRO_0000053378"
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 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 HELIX 3..8
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2NRL"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2NRL"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:2NRL"
FT HELIX 119..142
FT /evidence="ECO:0007829|PDB:2NRL"
SQ SEQUENCE 147 AA; 15628 MW; B0439FAB1B85609A CRC64;
MADFDAVLKC WGPVEADYTT IGGLVLTRLF KEHPETQKLF PKFAGIAQAD IAGNAAVSAH
GATVLKKLGE LLKAKGSHAA ILKPLANSHA TKHKIPINNF KLISEVLVKV MHEKAGLDAG
GQTALRNVMG IIIADLEANY KELGFSG
