ID MT23B_MYTED Reviewed; 71 AA. AC P80258; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 1. DT 02-SEP-2026, entry version 53. DE RecName: Full=Metallothionein 20-III isoform B; DE Short=MT-20-IIIB; OS Mytilus edulis (Blue mussel). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae; OC Mytilus. OX NCBI_TaxID=6550; RN [1] RP PROTEIN SEQUENCE. RX PubMed=8243463; DOI=10.1111/j.1432-1033.1993.tb18364.x; RA Mackay E.A., Overnell J., Dunbar B., Davidson I., Hunziker P.E., RA Kaegi J.H.R., Fothergill J.E.; RT "Complete amino acid sequences of five dimeric and four monomeric forms of RT metallothionein from the edible mussel Mytilus edulis."; RL Eur. J. Biochem. 218:183-194(1993). CC -!- FUNCTION: The metallothioneins are involved in the cellular CC sequestration of toxic metal ions. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: By cadmium. CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; S47577; S47577. DR AlphaFoldDB; P80258; -. DR SMR; P80258; -. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR InterPro; IPR061935; Metallothionein. DR InterPro; IPR001008; Metalthion_mollusc. DR Pfam; PF30063; Metallothionein; 1. DR PRINTS; PR00875; MTMOLLUSC. PE 1: Evidence at protein level; KW Cadmium; Direct protein sequencing; Metal-binding; Metal-thiolate cluster. FT CHAIN 1..71 FT /note="Metallothionein 20-III isoform B" FT /id="PRO_0000197332" FT BINDING 14 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 18 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 18 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 23 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 25 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 29 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 31 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 31 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 35 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 37 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 40 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 40 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 44 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 46 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 50 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 52 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 52 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 56 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 56 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 62 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 64 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 68 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 70 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P33187" FT BINDING 70 FT /ligand="Cd(2+)" FT /ligand_id="ChEBI:CHEBI:48775" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P33187" SQ SEQUENCE 71 AA; 6873 MW; D4BFD9FFB08577E7 CRC64; PGPCNCIETN VCICGTGCSG KCCQCGDACK CASGCGCSGC KVVCRCSGTC ACGCDCTGPT NCKCDSGCSC K //