MYG_MELGA
ID MYG_MELGA Reviewed; 154 AA.
AC G1NJB6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Myoglobin {ECO:0000303|Ref.2, ECO:0000303|Ref.3};
GN Name=MB;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-154.
RC TISSUE=Heart muscle {ECO:0000269|Ref.2};
RX DOI=10.1016/j.foodchem.2011.04.024;
RA Joseph P., Suman S.P., Li S., Claus J.R., Fontaine M., Steinke L.;
RT "Primary structure of turkey myoglobin.";
RL Food Chem. 129:175-178(2011).
RN [3] {ECO:0000305}
RP MASS SPECTROMETRY.
RC TISSUE=Heart muscle {ECO:0000269|Ref.3};
RX DOI=10.1016/j.lwt.2009.08.019;
RA Joseph P., Suman S.P., Li S., Beach C.M., Claus J.R.;
RT "Mass spectrometric characterization and thermostability of turkey
RT myoglobin.";
RL LWT Food Sci. Technol. 43:273-278(2010).
CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC movement of oxygen within muscles. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=17295; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR RefSeq; XP_003202395.1; XM_003202347.3.
DR AlphaFoldDB; G1NJB6; -.
DR SMR; G1NJB6; -.
DR Ensembl; ENSMGAT00000014318; ENSMGAP00000013412; ENSMGAG00000012726.
DR GeneID; 100539180; -.
DR KEGG; mgp:100539180; -.
DR CTD; 4151; -.
DR GeneTree; ENSGT00940000157534; -.
DR HOGENOM; CLU_003827_18_0_1; -.
DR InParanoid; G1NJB6; -.
DR OMA; MRLFQDH; -.
DR OrthoDB; 1405713at2759; -.
DR TreeFam; TF332967; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000012726; Expressed in gizzard and 10 other tissues.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Muscle protein;
KW Oxygen transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000415950"
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:0000250|UniProtKB:P02197,
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:P02197,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 154 AA; 17422 MW; AE8AEA7C9E83BCD5 CRC64;
MGLSDQEWQQ VLTIWGKVEA DIAGHGHEVL MRLFHDHPET LDRFDKFKGL KTPDQMKGSE
DLKKHGATVL TQLGKILKQK GNHESELKPL AQTHATKHKI PVKYLEFISE VIIKVIAEKH
AADFGADSQA AMKKALELFR NDMASKYKEF GFQG
