ID   GLBD_MOLAR              Reviewed;         159 AA.
AC   P80017;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Globin D, coelomic;
OS   Molpadia arenicola (Sea cucumber) (Caudina arenicola).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Apodacea; Molpadida; Molpadiidae; Molpadia.
OX   NCBI_TaxID=7698;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-159, AND ACETYLATION AT GLY-2.
RC   TISSUE=Coelomic fluid;
RX   PubMed=2049384; DOI=10.1016/0167-4838(91)90093-f;
RA   Mauri F., Omnaas J., Davidson L., Whitfill C., Kitto G.B.;
RT   "Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia)
RT   arenicola.";
RL   Biochim. Biophys. Acta 1078:63-67(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SEQUENCE REVISION.
RX   PubMed=15299806; DOI=10.1107/s0907444995001491;
RA   Mitchell D.T., Ernst S.R., Hackert M.L.;
RT   "X-ray structure determination of a dimeric hemoglobin from Caudina
RT   arenicola.";
RL   Acta Crystallogr. D 51:760-766(1995).
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: Caudina arenicola coelomocytes contain four hemoglobin
CC       chains labeled A, B, C, D.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S15979; S15979.
DR   PDB; 1HLM; X-ray; 2.90 A; A=2-159.
DR   PDBsum; 1HLM; -.
DR   AlphaFoldDB; P80017; -.
DR   SMR; P80017; -.
DR   iPTMnet; P80017; -.
DR   EvolutionaryTrace; P80017; -.
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   3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2049384"
FT   CHAIN           2..159
FT                   /note="Globin D, coelomic"
FT                   /id="PRO_0000052497"
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   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   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:2049384"
FT   CONFLICT        3..5
FT                   /note="ATQ -> QAT (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="T -> W (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           33..43
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   TURN            55..59
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           69..87
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           94..108
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           112..125
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           138..149
FT                   /evidence="ECO:0007829|PDB:1HLM"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1HLM"
SQ   SEQUENCE   159 AA;  17806 MW;  93FBC89BB9FF33EF CRC64;
     MGATQSFQSV GDLTPAEKDL IRSTWDQLMT HRTGFVADVF IRIFHNDPTA QRKFPQMAGL
     SPAELRTSRQ MHAHAIRVSA LMTTYIDEMD TEVLPELLAT LTRTHDKNHV GKKNYDLFGK
     VLMEAIKAEL GVGFTKQVHD AWAKTFAIVQ GVLITKHAS