ID   GLB_CERRH               Reviewed;         151 AA.
AC   P02215;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Globin;
DE   AltName: Full=Myoglobin;
OS   Cerithidea rhizophorarum (Water snail) (Horn shell).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Sorbeoconcha; Cerithioidea; Potamididae; Cerithidea.
OX   NCBI_TaxID=6472;
RN   [1]
RP   PROTEIN SEQUENCE, SUBUNIT, AND ACETYLATION AT SER-1.
RC   TISSUE=Radular muscle;
RX   PubMed=6849938; DOI=10.1016/0167-4838(83)90166-8;
RA   Takagi T., Tobita M., Shikama K.;
RT   "Amino acid sequence of dimeric myoglobin from Cerithidea rhizophorarum.";
RL   Biochim. Biophys. Acta 745:32-36(1983).
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6849938}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A02537; GGGACR.
DR   AlphaFoldDB; P02215; -.
DR   SMR; P02215; -.
DR   iPTMnet; P02215; -.
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..151
FT                   /note="Globin"
FT                   /id="PRO_0000052478"
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"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6849938"
SQ   SEQUENCE   151 AA;  16210 MW;  3493BAE8F4A4BD90 CRC64;
     SLQPASKSAL ASSWKTLAKD AATIQNNGAT LFSLLFKQFP DTRNYFTHFG NMSDAEMKTT
     GVGKAHSMAV FAGIGSMIDS MDDADCMNGL ALKLSRNHIQ RKIGASRFGE MRQVFPNFLD
     EALGGGASGD VKGAWDALLA YLQDNKQAQA L