ID   HEMT2_HEDDI             Reviewed;         120 AA.
AC   P80255;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Hemerythrin;
DE   AltName: Full=MP II;
DE            Short=MPII;
DE   AltName: Full=Non-metallothionein cadmium-binding protein;
DE            Short=CD-BP;
OS   Hediste diversicolor (Sandworm) (Nereis diversicolor).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Hediste;
OC   Hediste diversicolor species group.
OX   NCBI_TaxID=126592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12743530;
RA   Deloffre L., Salzet-Raveillon B., Vieau D., Andries J.-C., Salzet M.;
RT   "Antibacterial properties of hemerythrin of the sand worm Nereis
RT   diversicolor.";
RL   Neuroendocrinol. Lett. 24:39-45(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-120.
RX   PubMed=8223553; DOI=10.1111/j.1432-1033.1993.tb18230.x;
RA   Demuynck S., Li K.W., van der Schors R., Dhainaut-Courtois N.;
RT   "Amino acid sequence of the small cadmium-binding protein (MP II) from
RT   Nereis diversicolor (annelida, polychaeta). Evidence for a myohemerythrin
RT   structure.";
RL   Eur. J. Biochem. 217:151-156(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-34.
RX   PubMed=1908740;
RA   Demuynck S., Sautiere P., van Beeumen J., Dhainaut-Courtois N.;
RT   "Homologies between hemerythrins of sipunculids and cadmium-binding
RT   metalloprotein (MP II) from a polychaete annelid, Nereis diversicolor.";
RL   C. R. Acad. Sci. III, Sci. Vie 312:317-322(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-79.
RA   Salzet-Raveillon B., Rentier-Delrue F., Dhainaut A.;
RT   "Detection of mRNA encoding an antibacterial-metalloprotein (MPII) by in
RT   situ hybridization with a cDNA probe generated by polymerase chain reaction
RT   in the worm Nereis diversicolor.";
RL   Cell. Mol. Biol. 39:105-114(1993).
CC   -!- FUNCTION: May act as a buffer to control the concentration and
CC       therefore the toxicity of cadmium. Also involved in defense towards
CC       bacteria growth by acting as an iron scavenger.
CC       {ECO:0000269|PubMed:12743530}.
CC   -!- TISSUE SPECIFICITY: Expressed and produced in a hematopoietic center
CC       that floats freely in the coelomic fluid before being stored in a
CC       particular hemocyte type: the granulocyte type 1.
CC       {ECO:0000269|PubMed:12743530}.
CC   -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR   EMBL; S57799; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S38261; S38261.
DR   AlphaFoldDB; P80255; -.
DR   SMR; P80255; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd12107; Hemerythrin; 1.
DR   Gene3D; 1.20.120.50; Hemerythrin-like; 1.
DR   InterPro; IPR002063; Haemerythrin.
DR   InterPro; IPR016131; Haemerythrin_Fe_BS.
DR   InterPro; IPR050669; Hemerythrin.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR035938; Hemerythrin-like_sf.
DR   InterPro; IPR012827; Hemerythrin_metal-bd.
DR   NCBIfam; TIGR02481; hemeryth_dom; 1.
DR   NCBIfam; TIGR00058; Hemerythrin; 1.
DR   PANTHER; PTHR37164; BACTERIOHEMERYTHRIN; 1.
DR   PANTHER; PTHR37164:SF1; BACTERIOHEMERYTHRIN; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   PIRSF; PIRSF002033; Hemerythrin; 1.
DR   PRINTS; PR00186; HEMERYTHRIN.
DR   SUPFAM; SSF47188; Hemerythrin-like; 1.
DR   PROSITE; PS00550; HEMERYTHRINS; 1.
PE   1: Evidence at protein level;
KW   Cadmium; Cadmium resistance; Direct protein sequencing; Iron;
KW   Metal-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1908740,
FT                   ECO:0000269|PubMed:8223553"
FT   CHAIN           2..120
FT                   /note="Hemerythrin"
FT                   /id="PRO_0000191834"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         75
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   CONFLICT        7
FT                   /note="E -> Q (in Ref. 4; S57799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        11
FT                   /note="W -> Q (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..28
FT                   /note="KQ -> GK (in Ref. 4; S57799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="D -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="F -> P (in Ref. 4; S57799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="D -> E (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="M -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="G -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="N -> D (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   120 AA;  13647 MW;  93AA715E7E695422 CRC64;
     MGFEIPEPYK WDESFQVFYE KLDEEHKQIF NAIFALCGGN NADNLKSLVD VTANHFADEE
     AMMKASGSYG DFDSHKKKHE DFLAVIRGLG APVPQDKINY AKEWLVNHIK GTDFGYKGKL
//