ID   GLBC_MOLAR              Reviewed;         159 AA.
AC   P80018;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Globin C, 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=1515032; DOI=10.1007/bf01025089;
RA   McDonald G.D., Davidson L., Kitto G.B.;
RT   "Amino acid sequence of the coelomic C globin from the sea cucumber Caudina
RT   (Molpadia) arenicola.";
RL   J. Protein Chem. 11:29-37(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-159.
RA   Thomas P.W.;
RL   Thesis (1994), University of Texas / Austin, United States.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=15299794; DOI=10.1107/s0907444994013958;
RA   Mitchell D.T., Ernst S.R., Wu W.X., Hackert M.L.;
RT   "Three-dimensional structure of a hemichrome hemoglobin from Caudina
RT   arenicola.";
RL   Acta Crystallogr. D 51:647-653(1995).
CC   -!- SUBUNIT: Monomer.
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; A53881; A53881.
DR   PDB; 1HLB; X-ray; 2.50 A; A=2-158.
DR   PDBsum; 1HLB; -.
DR   AlphaFoldDB; P80018; -.
DR   SMR; P80018; -.
DR   iPTMnet; P80018; -.
DR   EvolutionaryTrace; P80018; -.
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   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:1515032, ECO:0000269|Ref.2"
FT   CHAIN           2..159
FT                   /note="Globin C, coelomic"
FT                   /id="PRO_0000052496"
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:1515032"
FT   CONFLICT        3
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="D -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..31
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           35..46
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           62..65
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           69..86
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           99..107
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           112..130
FT                   /evidence="ECO:0007829|PDB:1HLB"
FT   HELIX           137..151
FT                   /evidence="ECO:0007829|PDB:1HLB"
SQ   SEQUENCE   159 AA;  17780 MW;  B98B4EDD76AB8F84 CRC64;
     MGGTLAIQAQ GDLTLAQKKI VRKTWHQLMR NKTSFVTDVF IRIFAYDPSA QNKFPQMAGM
     SASQLRSSRQ MQAHAIRVSS IMSEYVEELD SDILPELLAT LARTHDLNKV GADHYNLFAK
     VLMEALQAEL GSDFNEKTRD AWAKAFSVVQ AVLLVKHGN