ID   MYG_RAT                 Reviewed;         154 AA.
AC   Q9QZ76;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Myoglobin;
GN   Name=Mb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Santos R.A., Giannocco G., Poyares L.L., Nunes M.T.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 65-78, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-32; SER-121 AND
RP   SER-133, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   EMBL; AF197916; AAF05848.1; -; mRNA.
DR   EMBL; BC070511; AAH70511.1; -; mRNA.
DR   RefSeq; NP_067599.1; NM_021588.2.
DR   AlphaFoldDB; Q9QZ76; -.
DR   SMR; Q9QZ76; -.
DR   BioGRID; 248730; 2.
DR   IntAct; Q9QZ76; 1.
DR   MINT; Q9QZ76; -.
DR   STRING; 10116.ENSRNOP00000006184; -.
DR   iPTMnet; Q9QZ76; -.
DR   PhosphoSitePlus; Q9QZ76; -.
DR   PaxDb; Q9QZ76; -.
DR   PRIDE; Q9QZ76; -.
DR   Ensembl; ENSRNOT00000006184; ENSRNOP00000006184; ENSRNOG00000004583.
DR   GeneID; 59108; -.
DR   KEGG; rno:59108; -.
DR   UCSC; RGD:620411; rat.
DR   CTD; 4151; -.
DR   RGD; 620411; Mb.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000160809; -.
DR   HOGENOM; CLU_003827_18_0_1; -.
DR   InParanoid; Q9QZ76; -.
DR   OMA; MRLFQDH; -.
DR   OrthoDB; 1405713at2759; -.
DR   PhylomeDB; Q9QZ76; -.
DR   TreeFam; TF332967; -.
DR   Reactome; R-RNO-8981607; Intracellular oxygen transport.
DR   PRO; PR:Q9QZ76; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004583; Expressed in heart and 19 other tissues.
DR   ExpressionAtlas; Q9QZ76; baseline and differential.
DR   Genevisible; Q9QZ76; RN.
DR   GO; GO:0020037; F:heme binding; NAS:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IDA:RGD.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR   GO; GO:0043353; P:enucleate erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0015671; P:oxygen transport; IDA:RGD.
DR   GO; GO:0009725; P:response to hormone; IDA:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
DR   GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR   GO; GO:0031444; P:slow-twitch skeletal muscle fiber contraction; IEP:RGD.
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   CHAIN           1..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053341"
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:0007744|PubMed:22673903"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         68
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04247"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   154 AA;  17157 MW;  98B31BE57FA020DA CRC64;
     MGLSDGEWQM VLNIWGKVEG DLAGHGQEVL ISLFKAHPET LEKFDKFKNL KSEEEMKSSE
     DLKKHGCTVL TALGTILKKK GQHAAEIQPL AQSHATKHKI PVKYLEFISE VIIQVLKKRY
     SGDFGADAQG AMSKALELFR NDIAAKYKEL GFQG