ID   MYG_LAGLA               Reviewed;         154 AA.
AC   P02154;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Myoglobin;
GN   Name=MB;
OS   Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Lagothrix.
OX   NCBI_TaxID=9519;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-154.
RC   TISSUE=Skeletal muscle;
RX   PubMed=4198766;
RA   Romero-Herrera A.E., Lehmann H.;
RT   "The myoglobin of primates. 4. New World monkeys: Cebidae: (1) Saimiri
RT   sciureus (squirrel monkey); (2) Lagothrix lagothricha (Humboldt's woolly
RT   monkey). Callitrichidae: Callithrix jacchus (common marmoset).";
RL   Biochim. Biophys. Acta 317:65-84(1973).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE (MINOR COMPONENT).
RX   PubMed=11947108; DOI=10.1016/0014-5793(73)80097-3;
RA   Romero-Herrera A.E., Lehmann H.;
RT   "N-terminal chain elongation as evidence for duplication of myoglobin in
RT   three South American monkeys.";
RL   FEBS Lett. 31:175-180(1973).
CC   -!- FUNCTION: Serves as a reserve supply of oxygen and facilitates the
CC       movement of oxygen within muscles.
CC   -!- MISCELLANEOUS: Marmoset, woolly monkey, and squirrel monkey have a
CC       minor myoglobin component that appears to differ from each major
CC       component in having Phe-Lys preceding position 2.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; B90587; MYMQW.
DR   AlphaFoldDB; P02154; -.
DR   SMR; P02154; -.
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:4198766"
FT   CHAIN           2..154
FT                   /note="Myoglobin"
FT                   /id="PRO_0000053308"
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   VARIANT         2
FT                   /note="G -> FKG (in minor component)"
SQ   SEQUENCE   154 AA;  17166 MW;  DC7C257B2031D86A CRC64;
     MGLSDGEWQL VLNIWGKVEA DIPSHGQEVL ISLFKGHPET LEKFDKFKHL KSEDEMKASE
     ELKKHGVTVL TALGGILKKK GQHEAELKPL AQSHATKHKI PVKYLEFISD AIIHALQKKH
     PGDFGADAQG AMKKALELFR NDMAAKYKEL GFQG