MYG_PIG
ID MYG_PIG Reviewed; 154 AA.
AC P02189;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3005120; DOI=10.1016/0378-1119(85)90033-2;
RA Akaboshi E.;
RT "Cloning and sequence analysis of porcine myoglobin cDNA.";
RL Gene 40:137-140(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-154.
RX PubMed=952959; DOI=10.1016/0005-2795(76)90160-4;
RA Rousseaux J., Dautrevaux M., Han K.;
RT "Comparison of the amino acid sequence of pig heart myoglobin with other
RT ungulate myoglobins.";
RL Biochim. Biophys. Acta 439:55-62(1976).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX PubMed=2383370; DOI=10.1107/s0108768189012450;
RA Smerdon S.J., Oldfield T.J., Dodson E.J., Dodson G.G., Hubbard R.E.,
RA Wilkinson A.J.;
RT "Determination of the crystal structure of recombinant pig myoglobin by
RT molecular replacement and its refinement.";
RL Acta Crystallogr. B 46:370-377(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX PubMed=9843395; DOI=10.1021/bi9812470;
RA Krzywda S., Murshudov G.N., Brzozowski A.M., Jaskolski M., Scott E.E.,
RA Klizas S.A., Gibson Q.H., Olson J.S., Wilkinson A.J.;
RT "Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine
RT substitution.";
RL Biochemistry 37:15896-15907(1998).
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; M14433; AAA31073.1; -; mRNA.
DR PIR; A23988; MYPG.
DR RefSeq; NP_999401.1; NM_214236.1.
DR PDB; 1M6C; X-ray; 1.90 A; A/B=2-154.
DR PDB; 1M6M; X-ray; 1.80 A; A/B=2-154.
DR PDB; 1MDN; X-ray; 1.98 A; A/B=2-154.
DR PDB; 1MNH; X-ray; 2.30 A; A=2-154.
DR PDB; 1MNI; X-ray; 2.07 A; A/B=2-154.
DR PDB; 1MNJ; X-ray; 2.20 A; A/B=2-154.
DR PDB; 1MNK; X-ray; 2.20 A; A/B=2-154.
DR PDB; 1MNO; X-ray; 1.95 A; A/B=2-154.
DR PDB; 1MWC; X-ray; 1.70 A; A/B=2-154.
DR PDB; 1MWD; X-ray; 1.80 A; A/B=2-154.
DR PDB; 1MYG; X-ray; 1.75 A; A/B=2-154.
DR PDB; 1MYH; X-ray; 1.90 A; A/B=2-154.
DR PDB; 1MYI; X-ray; 2.00 A; A/B=2-154.
DR PDB; 1MYJ; X-ray; 1.90 A; A/B=2-154.
DR PDB; 1PMB; X-ray; 2.50 A; A/B=2-154.
DR PDB; 1YCA; X-ray; 2.90 A; A/B=2-154.
DR PDB; 1YCB; X-ray; 2.10 A; A/B=2-154.
DR PDBsum; 1M6C; -.
DR PDBsum; 1M6M; -.
DR PDBsum; 1MDN; -.
DR PDBsum; 1MNH; -.
DR PDBsum; 1MNI; -.
DR PDBsum; 1MNJ; -.
DR PDBsum; 1MNK; -.
DR PDBsum; 1MNO; -.
DR PDBsum; 1MWC; -.
DR PDBsum; 1MWD; -.
DR PDBsum; 1MYG; -.
DR PDBsum; 1MYH; -.
DR PDBsum; 1MYI; -.
DR PDBsum; 1MYJ; -.
DR PDBsum; 1PMB; -.
DR PDBsum; 1YCA; -.
DR PDBsum; 1YCB; -.
DR AlphaFoldDB; P02189; -.
DR SMR; P02189; -.
DR CarbonylDB; P02189; -.
DR PeptideAtlas; P02189; -.
DR PRIDE; P02189; -.
DR Ensembl; ENSSSCT00005025786; ENSSSCP00005015616; ENSSSCG00005016417.
DR Ensembl; ENSSSCT00005025817; ENSSSCP00005015636; ENSSSCG00005016417.
DR Ensembl; ENSSSCT00005025838; ENSSSCP00005015652; ENSSSCG00005016417.
DR Ensembl; ENSSSCT00030031982; ENSSSCP00030014409; ENSSSCG00030023027.
DR Ensembl; ENSSSCT00040092074; ENSSSCP00040040622; ENSSSCG00040067247.
DR Ensembl; ENSSSCT00045029098; ENSSSCP00045020148; ENSSSCG00045017115.
DR Ensembl; ENSSSCT00045029138; ENSSSCP00045020182; ENSSSCG00045017115.
DR Ensembl; ENSSSCT00045029160; ENSSSCP00045020198; ENSSSCG00045017115.
DR Ensembl; ENSSSCT00050074045; ENSSSCP00050031909; ENSSSCG00050054308.
DR Ensembl; ENSSSCT00070018337; ENSSSCP00070015233; ENSSSCG00070009373.
DR Ensembl; ENSSSCT00070018457; ENSSSCP00070015335; ENSSSCG00070009373.
DR GeneID; 397467; -.
DR CTD; 4151; -.
DR InParanoid; P02189; -.
DR EvolutionaryTrace; P02189; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 5.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Muscle protein; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:952959"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /id="PRO_0000053336"
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:0000269|PubMed:9843395"
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:0000269|PubMed:2383370,
FT ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C,
FT ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN,
FT ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI,
FT ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK,
FT ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC,
FT ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG,
FT ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI,
FT ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB,
FT ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB"
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 HELIX 5..19
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:1MWC"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:1MWC"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1M6M"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1MWC"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1MWC"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:1MWC"
SQ SEQUENCE 154 AA; 17085 MW; 1CF92ACD400A76D0 CRC64;
MGLSDGEWQL VLNVWGKVEA DVAGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE
DLKKHGNTVL TALGGILKKK GHHEAELTPL AQSHATKHKI PVKYLEFISE AIIQVLQSKH
PGDFGADAQG AMSKALELFR NDMAAKYKEL GFQG
