MYG_LEPMU
ID MYG_LEPMU Reviewed; 154 AA.
AC P02169;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Myoglobin;
GN Name=MB;
OS Lepilemur mustelinus (Weasel sportive lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lepilemuridae; Lepilemur.
OX NCBI_TaxID=9453;
RN [1]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=4582928;
RA Romero-Herrera A.E., Lehmann H.;
RT "The myoglobin of primates. V. Prosimians: Galago crassicaudatus (thick-
RT tailed galago) and Lepilemur mustelinus (sportive lemur).";
RL Biochim. Biophys. Acta 322:10-22(1973).
CC -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC movement of oxygen within muscles.
CC -!- MISCELLANEOUS: Some amides were assigned by electrophoretic mobility or
CC by homology.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02491; MYLEM.
DR AlphaFoldDB; P02169; -.
DR SMR; P02169; -.
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 CHAIN 1..154
FT /note="Myoglobin"
FT /id="PRO_0000053310"
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"
SQ SEQUENCE 154 AA; 17074 MW; D52C2D2FA2B7FC9A CRC64;
MGLSDGEWQL VLNVWGKVEA DVGGHGQEVL IRLFTGHPET LEKFDKFKHL KTADEMKASE
DLKKHGTTVL TALGGILKKK GQHEAELKPL AQSHATKHKI PIKYLEFISD AIVHVLHSKH
PAEFGADAQA AMKKALELFR NDIAAKYKEL GFQG