ID   MYG_APTFO               Reviewed;         153 AA.
AC   P02199;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-71.
RX   PubMed=4763336; DOI=10.1016/0014-5793(73)80481-8;
RA   Peiffer S., Deconinck M., Paul C., Depreter J., Schnek A.G., Leonis J.;
RT   "Penguin (Aptenodytes forsteri) myoglobin. A 70 residue N-terminal
RT   sequence.";
RL   FEBS Lett. 37:295-297(1973).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-153.
RA   Castillo O., Lehmann H., Joysey K.A., Friday A.E.;
RL   (In) Schnek A.G., Vandecasserie C. (eds.);
RL   Myoglobin, pp.130-141, Editions de l'Universite de Bruxelles, Brussels
RL   (1977).
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; A94423; MYPN.
DR   AlphaFoldDB; P02199; -.
DR   SMR; P02199; -.
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; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4763336, ECO:0000269|Ref.2"
FT   CHAIN           2..153
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053354"
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         93
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"
SQ   SEQUENCE   153 AA;  17436 MW;  7042118B684BF64E CRC64;
     MGLNDQEWQQ VLTMWGKVES DLAGHGHAVL MRLFKSHPET MDRFDKFRGL KTPDEMRGSE
     DMKKHGVTVL TLGQILKKKG HHEAELKPLS QTHATKHKVP VKYLEFISEA IMKVIAQKHA
     SNFGADAQEA MKKALELFRN DMASKYKEFG FQG