HEMT2_HEDDI
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 03-AUG-2022, entry version 82.
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 defence 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 GO; GO:0055072; P:iron ion homeostasis; IEA:UniProt.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR Pfam; PF01814; Hemerythrin; 1.
DR PIRSF; PIRSF002033; Hemerythrin; 1.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR TIGRFAMs; TIGR00058; Hemerythrin; 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
