ID   P79846_9TELE            Unreviewed;       141 AA.
AC   P79846;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Myoglobin {ECO:0000256|ARBA:ARBA00019044, ECO:0000256|RuleBase:RU251113};
DE   Flags: Fragment;
OS   Pagetopsis macropterus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Pagetopsis.
OX   NCBI_TaxID=36194 {ECO:0000313|EMBL:AAB41673.1};
RN   [1] {ECO:0000313|EMBL:AAB41673.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart ventricle {ECO:0000313|EMBL:AAB41673.1};
RA   Vayda M.E., Yuan M.-L., Small D.J., Costello L., Sidell B.D.;
RT   "Extreme conservation of the myoglobin sequence among Antarctic
RT   notothenioid fishes.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles. {ECO:0000256|ARBA:ARBA00002755,
CC       ECO:0000256|RuleBase:RU251113}.
CC   -!- SIMILARITY: Belongs to the globin family.
CC       {ECO:0000256|ARBA:ARBA00008705, ECO:0000256|PROSITE-ProRule:PRU00238,
CC       ECO:0000256|RuleBase:RU000356}.
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DR   EMBL; U71152; AAB41673.1; -; mRNA.
DR   AlphaFoldDB; P79846; -.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 6.10.140.2100; -; 1.
DR   Gene3D; 6.10.140.2110; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR002335; Myoglobin.
DR   PANTHER; PTHR47132; MYOGLOBIN; 1.
DR   PANTHER; PTHR47132:SF1; MYOGLOBIN; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00613; MYOGLOBIN.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00238};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00238};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179,
KW   ECO:0000256|RuleBase:RU251113};
KW   Oxygen transport {ECO:0000256|ARBA:ARBA00022621, ECO:0000256|PROSITE-
KW   ProRule:PRU00238};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE-
KW   ProRule:PRU00238}.
FT   DOMAIN          1..135
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   BINDING         54
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:0000256|PROSITE-ProRule:PRU00238"
FT   BINDING         83
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:0000256|PROSITE-ProRule:PRU00238"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAB41673.1"
SQ   SEQUENCE   141 AA;  14868 MW;  8EDF8F2F32310E80 CRC64;
     VLKCWGPMEA DYATHGGLVL TRLFTEHPET LKLFPKFAGI AHGDLAGDAG VSAHGATVLN
     KLGDLLKARG AHAALLKPLS SSHATKHKIP IINFKLIAEV IGKVMEEKAG VDAGGQTGLR
     NVMAVIIADM EAAYKELGFT D
//