MYG_ELEMA
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 03-AUG-2022, entry version 106.
DE RecName: Full=Myoglobin;
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: 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}.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
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; 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