ID   MYG_BOVIN               Reviewed;         154 AA.
AC   P02192; Q3ZC11;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2659586; DOI=10.1093/oxfordjournals.jbchem.a122679;
RA   Shimada H., Fukasawa T., Ishimura Y.;
RT   "Expression of bovine myoglobin cDNA as a functionally active holoprotein
RT   in Saccharomyces cerevisiae.";
RL   J. Biochem. 105:417-422(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-154.
RC   TISSUE=Heart;
RX   PubMed=5477290; DOI=10.1111/j.1432-1033.1970.tb01103.x;
RA   Han K., Dautrevaux M., Chaila X., Biserte G.;
RT   "The covalent structure of beef heart myoglobin.";
RL   Eur. J. Biochem. 16:465-471(1970).
RN   [4]
RP   MASS SPECTROMETRY.
RX   PubMed=20374756; DOI=10.1016/j.meatsci.2009.08.014;
RA   Joseph P., Suman S.P., Li S., Beach C.M., Steinke L., Fontaine M.;
RT   "Characterization of bison (Bison bison) myoglobin.";
RL   Meat Sci. 84:71-78(2010).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles.
CC   -!- MASS SPECTROMETRY: Mass=16949; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20374756};
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   EMBL; D00409; BAA00311.1; -; mRNA.
DR   EMBL; BC102986; AAI02987.1; -; mRNA.
DR   PIR; JX0068; MYBO.
DR   RefSeq; NP_776306.1; NM_173881.2.
DR   AlphaFoldDB; P02192; -.
DR   SMR; P02192; -.
DR   STRING; 9913.ENSBTAP00000007014; -.
DR   Allergome; 1305; Bos d Myoglobin.
DR   CarbonylDB; P02192; -.
DR   PaxDb; P02192; -.
DR   PRIDE; P02192; -.
DR   Ensembl; ENSBTAT00000007014; ENSBTAP00000007014; ENSBTAG00000005333.
DR   Ensembl; ENSBTAT00000084629; ENSBTAP00000065000; ENSBTAG00000005333.
DR   GeneID; 280695; -.
DR   KEGG; bta:280695; -.
DR   CTD; 4151; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005333; -.
DR   VGNC; VGNC:31270; MB.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000160809; -.
DR   HOGENOM; CLU_003827_18_0_1; -.
DR   InParanoid; P02192; -.
DR   OMA; MRLFQDH; -.
DR   OrthoDB; 1405713at2759; -.
DR   TreeFam; TF332967; -.
DR   Reactome; R-BTA-8981607; Intracellular oxygen transport.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000005333; Expressed in tongue muscle and 95 other tissues.
DR   ExpressionAtlas; P02192; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0015671; P:oxygen transport; IBA:GO_Central.
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:5477290"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053280"
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"
FT   CONFLICT        6
FT                   /note="G -> W (in Ref. 2; AAI02987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="L -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100..102
FT                   /note="IPV -> VIP (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123..125
FT                   /note="DFG -> NFA (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143..146
FT                   /note="MAAQ -> AAEK (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  17078 MW;  E74911B6C6851761 CRC64;
     MGLSDGEWQL VLNAWGKVEA DVAGHGQEVL IRLFTGHPET LEKFDKFKHL KTEAEMKASE
     DLKKHGNTVL TALGGILKKK GHHEAEVKHL AESHANKHKI PVKYLEFISD AIIHVLHAKH
     PSDFGADAQA AMSKALELFR NDMAAQYKVL GFHG