ID   MYG_CAPHI               Reviewed;         154 AA.
AC   B7U9B5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 3.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Myoglobin {ECO:0000312|EMBL:ACJ68031.1};
GN   Name=MB {ECO:0000250|UniProtKB:P02190};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-154.
RC   TISSUE=Heart muscle {ECO:0000269|PubMed:20416681};
RX   PubMed=20416681; DOI=10.1016/j.meatsci.2009.02.017;
RA   Suman S.P., Joseph P., Li S., Steinke L., Fontaine M.;
RT   "Primary structure of goat myoglobin.";
RL   Meat Sci. 82:456-460(2009).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:ACJ68031.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-154.
RC   TISSUE=Muscle {ECO:0000312|EMBL:ACJ68031.1};
RA   Jia J.J., Ge C.R., Wang Z.C., Gu F.Y.;
RL   Submitted (NOV-2008) 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:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; FJ457764; ACJ68031.1; -; mRNA.
DR   AlphaFoldDB; B7U9B5; -.
DR   SMR; B7U9B5; -.
DR   STRING; 9925.ENSCHIP00000004261; -.
DR   CarbonylDB; B7U9B5; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
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:20416681"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000404697"
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                   /evidence="ECO:0000305"
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                   /evidence="ECO:0000305"
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"
FT   CONFLICT        53
FT                   /note="G -> E (in Ref. 2; ACJ68031)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  16955 MW;  63E289F55A364204 CRC64;
     MGLSDGEWTL VLNAWGKVEA DVAGHGQEVL IRLFTGHPET LEKFDKFKHL KTGAEMKASE
     DLKKHGNTVL TALGGILKKK GHHEAEVKHL AESHANKHKI PVKYLEFISD AIIHVLHAKH
     PSDFGADAQG AMSKALELFR NDMAAQYKVL GFQG