ID   MT_AGABI       STANDARD;      PRT;    25 AA.
AC   P04358;
DT   20-MAR-1987 (Rel. 04, Created)
DT   20-MAR-1987 (Rel. 04, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Metallothionein (MT).
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   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
RT   and 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)
CC       ions.
CC   -!- MISCELLANEOUS: The absorption, luminescent, and stereoptical
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
CC       family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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CC   removed.
CC   --------------------------------------------------------------------------
DR   PIR; A03286; SMMR.
KW   Copper; Direct protein sequencing; Metal-binding;
KW   Metal-thiolate cluster.
SQ   SEQUENCE   25 AA;  2233 MW;  33AB70F21023CFF7 CRC64;
     GDCGCSGASS CTCASGQCTC SGCGK
//