ID   GLB_NERAL               Reviewed;         157 AA.
AC   P0C227;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Globin;
DE   AltName: Full=Myoglobin;
OS   Nerita albicilla (Ox-palate nerite) (Theliostyla albicilla).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Neritimorpha; Cycloneritida; Neritoidea; Neritidae; Nerita.
OX   NCBI_TaxID=52928;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT GLY-1.
RC   TISSUE=Muscle;
RX   PubMed=12672482; DOI=10.1016/s1357-2725(03)00034-7;
RA   Suzuki T., Takao H., Yamanaka K., Gotoh H., Furukohri T., Takagi T.;
RT   "Evidence of met-form myoglobin from Theliostyla albicilla radular
RT   muscle.";
RL   Int. J. Biochem. Cell Biol. 35:1119-1126(2003).
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P0C227; -.
DR   SMR; P0C227; -.
DR   iPTMnet; P0C227; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR002336; Erythrocruorin.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00611; ERYTHCRUORIN.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Muscle protein; Oxygen transport; Transport.
FT   CHAIN           1..157
FT                   /note="Globin"
FT                   /id="PRO_0000260273"
FT   BINDING         70
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         102
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         1
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:12672482"
SQ   SEQUENCE   157 AA;  17137 MW;  EFF1958DB2F96F4B CRC64;
     GDVDVLKSLS ADQKAAIKSS WAAFAADITG NGSNVLVQFF KDYPGDQSYF KKFDGKKPDE
     LKGDAQLATH ASQVFGSLNN MIDSMDDPDK MVGLLCKNAS DHIPRGVRQQ QYKELFSTLM
     NYMQSLPGAN VAGDTKAAWD KALNAMANII DAEQKRL