MYG_DELDE
ID MYG_DELDE Reviewed; 154 AA.
AC P68276; P02172; P02175;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Delphinus delphis (Short-beaked common dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Delphinus.
OX NCBI_TaxID=9728;
RN [1]
RP PROTEIN SEQUENCE OF 2-154.
RC TISSUE=Skeletal muscle;
RX PubMed=911808; DOI=10.1021/bi00642a007;
RA Wang C.-C., Avila R., Jones B.N., Gurd F.R.N.;
RT "Complete primary structure of the major component myoglobin of Pacific
RT common dolphin (Delphinus delphis).";
RL Biochemistry 16:4978-4981(1977).
RN [2]
RP PROTEIN SEQUENCE OF 2-32.
RX PubMed=11945989; DOI=10.1016/0014-5793(71)80556-2;
RA Kluh I., Bakardjieva A.;
RT "Primary structure of N-terminal part of molecule of dolphin myoglobin.";
RL FEBS Lett. 17:31-34(1971).
RN [3]
RP PROTEIN SEQUENCE OF 32-154.
RX PubMed=5473803; DOI=10.1016/0005-2795(70)90208-4;
RA Karadjova M., Nedkov P., Bakardjieva A., Genov N.;
RT "Differences in amino acid sequence between dolphin and sperm whale
RT myoglobins.";
RL Biochim. Biophys. Acta 221:136-139(1970).
RN [4]
RP SEQUENCE REVISION TO 27.
RA Kluh I.;
RL Submitted (DEC-1977) to the PIR data bank.
CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC movement of oxygen within muscles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A26230; MYDDBS.
DR AlphaFoldDB; P68276; -.
DR SMR; P68276; -.
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; Phosphoprotein; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11945989,
FT ECO:0000269|PubMed:911808"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /id="PRO_0000053287"
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 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 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 22
FT /note="L -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="V -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17188 MW; 0D2879547F28AC1A CRC64;
MGLSDGEWQL VLNVWGKVEA DLAGHGQDVL IRLFKGHPET LEKFDKFKHL KTEADMKASE
DLKKHGNTVL TALGAILKKK GHHDAELKPL AQSHATKHKI PIKYLEFISE AIIHVLHSRH
PAEFGADAQG AMNKALELFR KDIAAKYKEL GFHG
