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GLB_DOLAU
ID   GLB_DOLAU               Reviewed;         146 AA.
AC   P09965;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Globin;
DE   AltName: Full=Myoglobin;
OS   Dolabella auricularia (Shoulderblade sea cat).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Dolabella.
OX   NCBI_TaxID=6511;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX   PubMed=3949784; DOI=10.1016/s0021-9258(17)35703-4;
RA   Suzuki T.;
RT   "Amino acid sequence of myoglobin from the mollusc Dolabella auricularia.";
RL   J. Biol. Chem. 261:3692-3699(1986).
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: This molluscan globin lacks one of the heme-binding
CC       histidine residues found in most other globins.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A25331; GGGDA.
DR   AlphaFoldDB; P09965; -.
DR   SMR; P09965; -.
DR   iPTMnet; P09965; -.
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:0005506; F:iron ion binding; IEA:InterPro.
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; IPR013314; Globin_lamprey/hagfish.
DR   InterPro; IPR044399; Mb-like_M.
DR   PANTHER; PTHR46783; PTHR46783; 1.
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..146
FT                   /note="Globin"
FT                   /id="PRO_0000052479"
FT   BINDING         95
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-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:3949784"
SQ   SEQUENCE   146 AA;  15319 MW;  08D5EFC0170A0D23 CRC64;
     ALSAAEAEVV AKSWGPVFAN KDANGDNFLI ALFEAYPDSP NFFADFKGKS IADIRASPKL
     RNVSSRIVSR LNEFVSSAAD AGKMAAMLDQ FSKEHAGFGV GSQQFQNVSA MFPGFVASIA
     APPAGADAAW GKLFGLIIDA MKKAGK
 
 
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