ID   GLB_TRIMF               Reviewed;         147 AA.
AC   P31331;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Globin;
DE   AltName: Full=Myoglobin;
OS   Tritia mutabilis (Sea snail) (Nassarius mutabilis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Buccinoidea; Nassariidae; Nassariinae;
OC   Tritia.
OX   NCBI_TaxID=1934731;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Radular muscle;
RX   PubMed=8448171; DOI=10.1016/0167-4838(93)90120-g;
RA   Parente A., Verde C., Malorni A., Montecucchi P., Aniello F., Geraci G.;
RT   "Amino-acid sequence of the cooperative dimeric myoglobin from the radular
RT   muscles of the marine gastropod Nassa mutabilis.";
RL   Biochim. Biophys. Acta 1162:1-9(1993).
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: In contrast to the other dimeric myoglobins, N.mutabilis
CC       myoglobin is a highly cooperative oxygen binding molecule.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S29824; S29824.
DR   AlphaFoldDB; P31331; -.
DR   SMR; P31331; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Muscle protein;
KW   Oxygen transport; Transport.
FT   CHAIN           1..147
FT                   /note="Globin"
FT                   /id="PRO_0000052481"
FT   BINDING         66
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         98
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"
SQ   SEQUENCE   147 AA;  15759 MW;  FE2D07817D61CC8C CRC64;
     GLSAEQKTAL KDSWKILAAN GETMVKNSAA MFGLLFEKYP DTKKHFKTFD GDHFAAMKAT
     GMGKAHGMSV FSGLGALVSS VDDGECVLGL AKKLSRNHTA RGVTANDFKL MRSIFGEFLD
     KATGGKATES MKSAWDALLG VLIENHQ