ID   MYG_RABIT               Reviewed;         154 AA.
AC   P02170;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=952958; DOI=10.1016/0005-2795(76)90159-8;
RA   Romero-Herrera A.E., Lehmann H., Castillo O.;
RT   "The primary structure of the myoglobin of rabbit (Oryctolagus
RT   cuniculus).";
RL   Biochim. Biophys. Acta 439:51-54(1976).
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   PIR; A02492; MYRB.
DR   AlphaFoldDB; P02170; -.
DR   SMR; P02170; -.
DR   STRING; 9986.ENSOCUP00000023254; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P02170; -.
DR   Proteomes; UP000001811; Unplaced.
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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:952958"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053340"
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   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   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;  17221 MW;  7E5C5CED36F4EB56 CRC64;
     MGLSDAEWQL VLNVWGKVEA DLAGHGQEVL IRLFHTHPET LEKFDKFKHL KSEDEMKASE
     DLKKHGNTVL TALGAILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE AIIHVLHSKH
     PGDFGADAQA AMSKALELFR NDIAAQYKEL GFQG