ID MYG_ELEMA Reviewed; 154 AA. AC P02186; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 109. DE RecName: Full=Myoglobin; 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; OS Elephas maximus (Indian elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas. OX NCBI_TaxID=9783; RN [1] RP PROTEIN SEQUENCE OF 2-154. RC TISSUE=Skeletal muscle; RX PubMed=6102395; DOI=10.1098/rspb.1980.0016; RA Dene H., Goodman M., Romero-Herrera A.E.; RT "The amino acid sequence of elephant (Elephas maximus) myoglobin and the RT phylogeny of Proboscidea."; RL Proc. R. Soc. Lond., B, Biol. Sci. 207:111-127(1980). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME, AND RP SEQUENCE REVISION TO 28 AND 30. RX PubMed=7657658; DOI=10.1074/jbc.270.35.20754; RA Bisig D.A., di Iorio E.E., Diederichs K., Winterhalter K.H., Piontek K.; RT "Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin RT at 1.78-A resolution. Phe29(B10) accounts for its unusual ligand binding RT properties."; RL J. Biol. Chem. 270:20754-20762(1995). 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. Depending on the oxidative conditions of tissues and cells, and CC in addition to its ability to bind oxygen, it also has a nitrite CC reductase activity whereby it regulates the production of bioactive CC nitric oxide. Under stress conditions, like hypoxia and anoxia, it also CC protects cells against reactive oxygen species thanks to its CC pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b- CC [protein] + 2 H(+) + nitrite; 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=AH2 + H2O2 = 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 -!- 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 PIR; A94228; MYELI. DR PDB; 1EMY; X-ray; 1.78 A; A=2-154. DR PDBsum; 1EMY; -. DR AlphaFoldDB; P02186; -. DR SMR; P02186; -. DR EvolutionaryTrace; P02186; -. DR GO; GO:0016528; C:sarcoplasm; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0098809; F:nitrite reductase activity; ISS:UniProtKB. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen carrier activity; ISS:UniProtKB. DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB. 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 3D-structure; Cytoplasm; Direct protein sequencing; Heme; Iron; KW Metal-binding; Muscle protein; Oxidoreductase; Oxygen transport; KW Phosphoprotein; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6102395" FT CHAIN 2..154 FT /note="Myoglobin" FT /id="PRO_0000053290" 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:7657658, FT ECO:0007744|PDB:1EMY" 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 28 FT /note="T -> F (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="F -> L (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 5..19 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 22..36 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 38..43 FT /evidence="ECO:0007829|PDB:1EMY" FT TURN 45..49 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 60..78 FT /evidence="ECO:0007829|PDB:1EMY" FT TURN 79..81 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 102..119 FT /evidence="ECO:0007829|PDB:1EMY" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:1EMY" FT HELIX 126..149 FT /evidence="ECO:0007829|PDB:1EMY" SQ SEQUENCE 154 AA; 17127 MW; F1031658D39BEAD5 CRC64; MGLSDGEWEL VLKTWGKVEA DIPGHGETVF VRLFTGHPET LEKFDKFKHL KTEGEMKASE DLKKQGVTVL TALGGILKKK GHHEAEIQPL AQSHATKHKI PIKYLEFISD AIIHVLQSKH PAEFGADAQG AMKKALELFR NDIAAKYKEL GFQG //