ID   MYG_HETPO               Reviewed;         149 AA.
AC   P02206;
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   Heterodontus portusjacksoni (Port Jackson shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Heterodontoidea; Heterodontiformes;
OC   Heterodontidae; Heterodontus.
OX   NCBI_TaxID=7793;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-149, AND ACETYLATION AT THR-2.
RX   PubMed=508202; DOI=10.1071/bi9790277;
RA   Fisher W.K., Thompson E.O.P.;
RT   "Myoglobin of the shark Heterodontus portusjacksoni: isolation and amino
RT   acid sequence.";
RL   Aust. J. Biol. Sci. 32:277-294(1979).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A02527; MYRKJ.
DR   AlphaFoldDB; P02206; -.
DR   SMR; P02206; -.
DR   iPTMnet; P02206; -.
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   Acetylation; 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:508202"
FT   CHAIN           2..149
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053301"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:508202"
SQ   SEQUENCE   149 AA;  16977 MW;  756DE45FB519ABC0 CRC64;
     MTEWEHVNKV WAVVEPDIPA VGLAILLRLF KEHKETKDLF PKFKEIPVQQ LGNNEDLRKH
     GVTVLRALGN ILKQKGKHST NVKELADTHI NKHKIPPKNF VLITNIAVKV LTEMYPSDMT
     GPMQESFSKV FTVICSDLET LYKEANFQG