MYG_PHOVI
ID MYG_PHOVI Reviewed; 154 AA.
AC P68080; P02162;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Phoca vitulina (Harbor seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Phoca.
OX NCBI_TaxID=9720;
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 X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-154 IN COMPLEX WITH HEME.
RX PubMed=745243; DOI=10.1016/0022-2836(78)90013-x;
RA Scouloudi H., Baker E.N.;
RT "X-ray crystallographic studies of seal myoglobin. The molecule at 2.5-A
RT resolution.";
RL J. Mol. Biol. 126:637-660(1978).
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}.
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DR PIR; A92045; MYSLH.
DR PDB; 1MBS; X-ray; 2.50 A; A=2-154.
DR PDBsum; 1MBS; -.
DR AlphaFoldDB; P68080; -.
DR SMR; P68080; -.
DR EvolutionaryTrace; P68080; -.
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:5782005"
FT CHAIN 2..154
FT /note="Myoglobin"
FT /id="PRO_0000053334"
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:0000269|PubMed:745243"
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:745243, ECO:0007744|PDB:1MBS"
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 HELIX 4..19
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1MBS"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 60..78
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:1MBS"
FT HELIX 126..150
FT /evidence="ECO:0007829|PDB:1MBS"
SQ SEQUENCE 154 AA; 17428 MW; 4A653EED8CF0E9FD CRC64;
MGLSDGEWHL VLNVWGKVET DLAGHGQEVL IRLFKSHPET LEKFDKFKHL KSEDDMRRSE
DLRKHGNTVL TALGGILKKK GHHEAELKPL AQSHATKHKI PIKYLEFISE AIIHVLHSKH
PAEFGADAQA AMKKALELFR NDIAAKYKEL GFHG
