ID   MYG_CARCR               Reviewed;         154 AA.
AC   P56208;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Caretta caretta (Loggerhead sea turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Caretta.
OX   NCBI_TaxID=8467;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=8260943;
RA   Petruzzelli R., Aureli G., Casale E., Nardini M., Rizzi M., Ascenzi P.,
RA   Coletta M., de Sanctis G., Desideri A., Galtieri A., Bolognesi M.;
RT   "Structural studies on the loggerhead sea turtle (Caretta caretta)
RT   myoglobin.";
RL   Biochem. Mol. Biol. Int. 31:19-24(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX   PubMed=7714901; DOI=10.1006/jmbi.1994.0153;
RA   Nardini M., Tarricone C., Rizzi M., Lania A., Desideri A., de Sanctis G.,
RA   Coletta M., Petruzzelli R., Ascenzi P., Coda A., Bolognesi M.;
RT   "Reptile heme protein structure: X-ray crystallographic study of the aquo-
RT   met and cyano-met derivatives of the loggerhead sea turtle (Caretta
RT   caretta) myoglobin at 2.0-A resolution.";
RL   J. Mol. Biol. 247:459-465(1995).
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   PDB; 1LHS; X-ray; 2.00 A; A=2-154.
DR   PDB; 1LHT; X-ray; 2.00 A; A=2-154.
DR   PDBsum; 1LHS; -.
DR   PDBsum; 1LHT; -.
DR   AlphaFoldDB; P56208; -.
DR   SMR; P56208; -.
DR   EvolutionaryTrace; P56208; -.
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; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Muscle protein; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8260943"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053380"
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:0000269|PubMed:7714901"
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:7714901,
FT                   ECO:0007744|PDB:1LHS, ECO:0007744|PDB:1LHT"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           22..36
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           53..57
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           60..77
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   TURN            78..81
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   HELIX           126..148
FT                   /evidence="ECO:0007829|PDB:1LHS"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:1LHS"
SQ   SEQUENCE   154 AA;  17522 MW;  3D67EBD5FE1075E9 CRC64;
     MGLSDDEWNH VLGIWAKVEP DLSAHGQEVI IRLFQLHPET QERFAKFKNL TTIDALKSSE
     EVKKHGTTVL TALGRILKQK NNHEQELKPL AESHATKHKI PVKYLEFICE IIVKVIAEKH
     PSDFGADSQA AMKKALELFR NDMASKYKEF GFQG