MT_AGABI
ID MT_AGABI Reviewed; 25 AA.
AC P04358;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Metallothionein;
DE Short=MT;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=A-32; TISSUE=Mycelium;
RA Muenger K., Lerch K.;
RT "Copper metallothionein from the fungus Agaricus bisporus: chemical and
RT spectroscopic properties.";
RL Biochemistry 24:6751-6756(1985).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions. Binds six copper (cuprous) ions.
CC -!- MISCELLANEOUS: The absorption, luminescent, and stereo-optical
CC properties of the copper MT are attributed to the metal-thiolate
CC complex because they are not present in the apoprotein.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 8 family.
CC {ECO:0000305}.
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DR PIR; A03286; SMMR.
DR AlphaFoldDB; P04358; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Metal-binding; Metal-thiolate cluster.
FT PEPTIDE 1..25
FT /note="Metallothionein"
FT /id="PRO_0000197361"
FT BINDING 3
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 5
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 5
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 11
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 11
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 13
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 20
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 20
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 23
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02807"
FT BINDING 23
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02807"
SQ SEQUENCE 25 AA; 2233 MW; 33AB70F21023CFF7 CRC64;
GDCGCSGASS CTCASGQCTC SGCGK