ID   GLB1_PARCH              Reviewed;         158 AA.
AC   P15161;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Globin-1;
DE   AltName: Full=Globin I;
OS   Paracaudina chilensis (Sea cucumber) (Caudina chilensis).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Apodacea; Molpadida; Caudinidae; Paracaudina.
OX   NCBI_TaxID=7700;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-158, AND ACETYLATION AT GLY-2.
RX   PubMed=2804131; DOI=10.1016/0167-4838(89)90287-2;
RA   Suzuki T.;
RT   "Amino acid sequence of a major globin from the sea cucumber Paracaudina
RT   chilensis.";
RL   Biochim. Biophys. Acta 998:292-296(1989).
CC   -!- SUBUNIT: In the oxy-form exist as a dimer, it disassociates into
CC       monomer in the inactive Met-form. Upon deoxygenation it aggregates into
CC       tetramer and higher oligomers.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S06134; S06134.
DR   AlphaFoldDB; P15161; -.
DR   SMR; P15161; -.
DR   iPTMnet; P15161; -.
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; 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   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   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2804131"
FT   CHAIN           2..158
FT                   /note="Globin-1"
FT                   /id="PRO_0000052495"
FT   BINDING         74
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         105
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-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:2804131"
SQ   SEQUENCE   158 AA;  17715 MW;  0FD80798EF5E7455 CRC64;
     MGGTLAIQSH GDLTLAQKKI VRKTWHQLMR NKTSFVTDLF IRIFAYDPAA QNKFPQMAGM
     SASQLRSSRQ MQAHAIRVSS IMSEYIEELD SDILPELLAT LARTHDLNKV GPAHYDLFAK
     VLMEALQAEL GSDFNQKTRD SWAKAFSIVQ AVLLVKHG