ID   MYG_PHOPH               Reviewed;         154 AA.
AC   P68278; P02176;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Phocoena phocoena (Harbor porpoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Phocoenidae; Phocoena.
OX   NCBI_TaxID=9742;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=5782005; DOI=10.1016/s0021-9258(18)94381-4;
RA   Bradshaw R.A., Gurd F.R.N.;
RT   "Comparison of myoglobins from harbor seal, porpoise, and sperm whale. V.
RT   The complete amino acid sequences of harbor seal and porpoise myoglobins.";
RL   J. Biol. Chem. 244:2167-2181(1969).
RN   [2]
RP   SEQUENCE REVISION TO 84 AND 86.
RX   PubMed=687594; DOI=10.1021/bi00610a001;
RA   Meuth J.L., Jones B.N., Garner W.H., Gurd F.R.N.;
RT   "Complete amino acid sequence of the myoglobin from the Dall porpoise
RT   (Phocoenoides dalli dalli) and reinvestigation of the primary structure of
RT   the myoglobin from common porpoise (Phocoena phocoena).";
RL   Biochemistry 17:3429-3431(1978).
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; B92045; MYPE.
DR   AlphaFoldDB; P68278; -.
DR   SMR; P68278; -.
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:5782005"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053332"
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: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:0000255|PROSITE-ProRule:PRU00238"
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"
SQ   SEQUENCE   154 AA;  17232 MW;  9682498B3EA8CC67 CRC64;
     MGLSEGEWQL VLNVWGKVEA DLAGHGQDVL IRLFKGHPET LEKFDKFKHL KTEAEMKASE
     DLKKHGNTVL TALGGILKKK GHHDAELKPL AQSHATKHKI PIKYLEFISE AIIHVLHSRH
     PAEFGADAQG AMNKALELFR KDIATKYKEL GFHG