ID   MYG_MOUSE               Reviewed;         154 AA.
AC   P04247;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 183.
DE   RecName: Full=Myoglobin {ECO:0000303|PubMed:3758071};
DE   AltName: Full=Nitrite reductase MB {ECO:0000250|UniProtKB:P02144};
DE            EC=1.7.-.- {ECO:0000250|UniProtKB:P02144};
DE   AltName: Full=Pseudoperoxidase MB {ECO:0000250|UniProtKB:P02144};
DE            EC=1.11.1.- {ECO:0000250|UniProtKB:P02144};
GN   Name=Mb {ECO:0000312|MGI:MGI:96922};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3758071; DOI=10.1111/j.1432-1033.1986.tb09909.x;
RA   Blanchetot A., Price M., Jeffreys A.J.;
RT   "The mouse myoglobin gene. Characterisation and sequence comparison with
RT   other mammalian myoglobin genes.";
RL   Eur. J. Biochem. 159:469-474(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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 2-154.
RX   PubMed=4043406; DOI=10.1016/0014-5793(85)81302-8;
RA   Harris D.E., Gurnett A.M., Lehmann H., Joysey K.A.;
RT   "The myoglobin of rodents Proechimys guairae (casiragua) and Mus musculus
RT   (house mouse).";
RL   FEBS Lett. 190:288-292(1985).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9804424; DOI=10.1038/27681;
RA   Garry D.J., Ordway G.A., Lorenz J.N., Radford N.B., Chin E.R., Grange R.W.,
RA   Bassel-Duby R., Williams R.S.;
RT   "Mice without myoglobin.";
RL   Nature 395:905-908(1998).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10468637; DOI=10.1073/pnas.96.18.10495;
RA   Goedecke A., Floegel U., Zanger K., Ding Z., Hirchenhain J., Decking U.K.,
RA   Schrader J.;
RT   "Disruption of myoglobin in mice induces multiple compensatory
RT   mechanisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10495-10500(1999).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11304494; DOI=10.1161/hh0701.089753;
RA   Meeson A.P., Radford N., Shelton J.M., Mammen P.P., DiMaio J.M.,
RA   Hutcheson K., Kong Y., Elterman J., Williams R.S., Garry D.J.;
RT   "Adaptive mechanisms that preserve cardiac function in mice without
RT   myoglobin.";
RL   Circ. Res. 88:713-720(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=15132981; DOI=10.1096/fj.03-1382fje;
RA   Floegel U., Goedecke A., Klotz L.O., Schrader J.;
RT   "Role of myoglobin in the antioxidant defense of the heart.";
RL   FASEB J. 18:1156-1158(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-75 AND SER-121, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Monomeric heme protein which primary function is to store
CC       oxygen and facilitate its diffusion within muscle tissues. Reversibly
CC       binds oxygen through a pentacoordinated heme iron and enables its
CC       timely and efficient release as needed during periods of heightened
CC       demand (PubMed:10468637, PubMed:11304494). Depending on the oxidative
CC       conditions of tissues and cells, and in addition to its ability to bind
CC       oxygen, it also has a nitrite reductase activity whereby it regulates
CC       the production of bioactive nitric oxide (By similarity). Under stress
CC       conditions, like hypoxia and anoxia, it also protects cells against
CC       reactive oxygen species thanks to its pseudoperoxidase activity
CC       (PubMed:15132981). {ECO:0000250|UniProtKB:P02144,
CC       ECO:0000269|PubMed:10468637, ECO:0000269|PubMed:11304494,
CC       ECO:0000269|PubMed:15132981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(III)-heme b-[protein] + nitric oxide + H2O = Fe(II)-heme b-
CC         [protein] + nitrite + 2 H(+); Xref=Rhea:RHEA:77711, Rhea:RHEA-
CC         COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P02144};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713;
CC         Evidence={ECO:0000250|UniProtKB:P02144};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + AH2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144};
CC   -!- SUBUNIT: Monomeric. {ECO:0000250|UniProtKB:P02185}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm
CC       {ECO:0000250|UniProtKB:P02144}.
CC   -!- DISRUPTION PHENOTYPE: A majority of embryos lacking myoglobin/Mb die,
CC       apparently of congestive heart failure and vascular insufficiency,
CC       around E9.5/E10.5 (PubMed:11304494). Surviving Mb homozygous knockout
CC       mice are fertile and exhibit no obvious phenotypic abnormalities during
CC       ambient activities as well as normal exercise capacity and ventilatory
CC       response to low oxygen levels (PubMed:9804424). However, they display
CC       reprogrammed gene expression and increased myocardial vascularity,
CC       basal coronary flow, coronary flow reserve, and hematocrit indicative
CC       of compensatory mechanisms that tend to steepen the PO2 gradient from
CC       the capillary to the mitochondria (PubMed:10468637, PubMed:11304494).
CC       {ECO:0000269|PubMed:10468637, ECO:0000269|PubMed:11304494,
CC       ECO:0000269|PubMed:9804424}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; BC025172; AAH25172.1; -; mRNA.
DR   EMBL; X04405; CAA27994.1; -; Genomic_DNA.
DR   EMBL; X04417; CAA27994.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS27597.1; -.
DR   PIR; A25799; MYMS.
DR   RefSeq; NP_001157519.1; NM_001164047.1.
DR   RefSeq; NP_001157520.1; NM_001164048.1.
DR   RefSeq; NP_038621.2; NM_013593.3.
DR   AlphaFoldDB; P04247; -.
DR   SMR; P04247; -.
DR   BioGRID; 201329; 2.
DR   FunCoup; P04247; 56.
DR   IntAct; P04247; 3.
DR   MINT; P04247; -.
DR   STRING; 10090.ENSMUSP00000125995; -.
DR   GlyGen; P04247; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P04247; -.
DR   MetOSite; P04247; -.
DR   PhosphoSitePlus; P04247; -.
DR   CPTAC; non-CPTAC-3847; -.
DR   jPOST; P04247; -.
DR   PaxDb; 10090-ENSMUSP00000125995; -.
DR   PeptideAtlas; P04247; -.
DR   ProteomicsDB; 252629; -.
DR   Antibodypedia; 292; 1366 antibodies from 50 providers.
DR   DNASU; 17189; -.
DR   Ensembl; ENSMUST00000019037.10; ENSMUSP00000019037.9; ENSMUSG00000018893.16.
DR   Ensembl; ENSMUST00000166179.9; ENSMUSP00000128399.2; ENSMUSG00000018893.16.
DR   Ensembl; ENSMUST00000169226.9; ENSMUSP00000125995.2; ENSMUSG00000018893.16.
DR   Ensembl; ENSMUST00000229423.2; ENSMUSP00000155115.2; ENSMUSG00000018893.16.
DR   GeneID; 17189; -.
DR   KEGG; mmu:17189; -.
DR   UCSC; uc007wmx.2; mouse.
DR   AGR; MGI:96922; -.
DR   CTD; 4151; -.
DR   MGI; MGI:96922; Mb.
DR   VEuPathDB; HostDB:ENSMUSG00000018893; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000160809; -.
DR   HOGENOM; CLU_003827_18_0_1; -.
DR   InParanoid; P04247; -.
DR   OMA; VIIRMFQ; -.
DR   OrthoDB; 6344802at2759; -.
DR   PhylomeDB; P04247; -.
DR   BRENDA; 1.11.1.16; 3474.
DR   Reactome; R-MMU-8981607; Intracellular oxygen transport.
DR   BioGRID-ORCS; 17189; 2 hits in 81 CRISPR screens.
DR   PRO; PR:P04247; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P04247; protein.
DR   Bgee; ENSMUSG00000018893; Expressed in digastric muscle group and 138 other cell types or tissues.
DR   ExpressionAtlas; P04247; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:GO_Central.
DR   GO; GO:0016528; C:sarcoplasm; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0098809; F:nitrite reductase activity; ISS:UniProtKB.
DR   GO; GO:0019825; F:oxygen binding; ISO:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; ISS:UniProtKB.
DR   GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0043353; P:enucleate erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0015671; P:oxygen transport; ISO:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR   GO; GO:0009725; P:response to hormone; ISO:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISO:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   GO; GO:0014850; P:response to muscle activity; ISO:GO_Central.
DR   GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Muscle protein; Oxidoreductase; Oxygen transport; Phosphoprotein;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4043406"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053319"
FT   DOMAIN          2..148
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         65
FT                   /ligand="nitrite"
FT                   /ligand_id="ChEBI:CHEBI:16301"
FT                   /evidence="ECO:0000250|UniProtKB:P68082"
FT   BINDING         65
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P02189,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
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:0000250|UniProtKB:P02144"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ76"
FT   MOD_RES         68
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        116
FT                   /note="L -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   154 AA;  17070 MW;  8EE1EE3FFEE36AF0 CRC64;
     MGLSDGEWQL VLNVWGKVEA DLAGHGQEVL IGLFKTHPET LDKFDKFKNL KSEEDMKGSE
     DLKKHGCTVL TALGTILKKK GQHAAEIQPL AQSHATKHKI PVKYLEFISE IIIEVLKKRH
     SGDFGADAQG AMSKALELFR NDIAAKYKEL GFQG
//