MT12_MYTED
ID MT12_MYTED Reviewed; 73 AA.
AC P80247; O62555;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Metallothionein 10-II;
DE Short=MT-10-II;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Digestive gland;
RX PubMed=10190057; DOI=10.1016/s0742-8413(98)10126-3;
RA Barsyte D., White K.N., Lovejoy D.A.;
RT "Cloning and characterization of metallothionein cDNAs in the mussel
RT Mytilus edulis L. digestive gland.";
RL Comp. Biochem. Physiol. 122C:287-296(1999).
RN [2]
RP PROTEIN SEQUENCE OF 2-73.
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: Monomer.
CC -!- INDUCTION: By cadmium.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ005453; CAA06550.1; -; mRNA.
DR PIR; S39417; S39417.
DR AlphaFoldDB; P80247; -.
DR SMR; P80247; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003019; Metalthion.
DR InterPro; IPR001008; Metalthion_mollusc.
DR Pfam; PF00131; Metallothio; 1.
DR PRINTS; PR00875; MTMOLLUSC.
PE 1: Evidence at protein level;
KW Cadmium; Direct protein sequencing; Metal-binding; Metal-thiolate cluster.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8243463"
FT CHAIN 2..73
FT /note="Metallothionein 10-II"
FT /id="PRO_0000197326"
FT BINDING 15
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 24
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 30
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 32
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 32
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 37
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 39
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 42
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 42
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 46
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 48
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 54
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 54
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 58
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 58
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 64
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 66
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="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 72
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 72
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT CONFLICT 22
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 73 AA; 7153 MW; 20CFA4CB3A0CDE19 CRC64;
MPAPCNCIET NVCICDTGCS GDGCRCGDAC KCSGADCKCS GCKVVCKCSG SCECGKGCTG
PSTCKCAPGC SCK
