ID   GLB_APLKU               Reviewed;         145 AA.
AC   P02211; O01417;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Globin;
DE   AltName: Full=Myoglobin;
OS   Aplysia kurodai (Kuroda's sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yuasa H.J., Matsuoka A., Tajima G.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-145, AND ACETYLATION AT SER-2.
RX   PubMed=7295773; DOI=10.1016/0005-2795(81)90225-7;
RA   Suzuki T., Takagi T., Shikama K.;
RT   "Amino acid sequence of myoglobin from Aplysia kurodai.";
RL   Biochim. Biophys. Acta 669:79-83(1981).
RN   [3]
RP   STABILITY.
RX   PubMed=1730027; DOI=10.1016/0167-4838(92)90138-4;
RA   Matsuoka A., Shikama K.;
RT   "Stability properties of Aplysia oxymyoglobin: effect of esterification of
RT   the heme propionates.";
RL   Biochim. Biophys. Acta 1118:123-129(1992).
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   EMBL; AB003278; BAA32240.1; -; mRNA.
DR   PIR; A02532; GGGA2A.
DR   AlphaFoldDB; P02211; -.
DR   SMR; P02211; -.
DR   iPTMnet; P02211; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7295773"
FT   CHAIN           2..145
FT                   /note="Globin"
FT                   /id="PRO_0000052472"
FT   BINDING         96
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         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:7295773"
FT   CONFLICT        25
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..28
FT                   /note="DA -> AN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   145 AA;  15460 MW;  3A96DEDEF1D16BE5 CRC64;
     MSLSAAEADL VGKSWAPVYA NKDANGDAFL LSLFEKFPNN ANYFADFKGK SIADIKASPK
     LRDVSSRIFT RLNEFVNNAA DAGKMSAMLS QFASEHVGFG VGSAQFENVR SMFPAFVASL
     SAPPADDAWN KLFGLIVAAL KAAGK