ID   MYG_OTOCR               Reviewed;         154 AA.
AC   P02168;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=9463;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=4582928;
RA   Romero-Herrera A.E., Lehmann H.;
RT   "The myoglobin of primates. V. Prosimians: Galago crassicaudatus (thick-
RT   tailed galago) and Lepilemur mustelinus (sportive lemur).";
RL   Biochim. Biophys. Acta 322:10-22(1973).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles.
CC   -!- MISCELLANEOUS: Some amides were assigned by electrophoretic mobility or
CC       by homology.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A02490; MYGC.
DR   AlphaFoldDB; P02168; -.
DR   SMR; P02168; -.
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; Transport.
FT   CHAIN           1..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053296"
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;  17102 MW;  A49533B55E41577A CRC64;
     MGLSDGEWQL VLKIWGKVEA DLAGHGQDVL IRLFTAHPET LEKFDKFKNL KTADEMKASE
     DLKKHGVTVL TALGGILKKK GQHEAEIKPL AQSHATKHKI PVKYLEFISE AIIHVLQNKH
     SGDFGTDVQG AMSKALELFR NDIAAKYKEL GFQG