MT2B_COLES
ID MT2B_COLES Reviewed; 84 AA.
AC Q19LA2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Metallothionein type 2b;
DE Short=CeMT2b;
OS Colocasia esculenta (Wild taro) (Arum esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC Colocasia.
OX NCBI_TaxID=4460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF 82-CYS--CYS-84.
RX PubMed=21979068; DOI=10.1271/bbb.110289;
RA Kim Y.O., Patel D.H., Lee D.S., Song Y., Bae H.J.;
RT "High cadmium-binding ability of a novel Colocasia esculenta
RT metallothionein increases cadmium tolerance in Escherichia coli and
RT Tobacco.";
RL Biosci. Biotechnol. Biochem. 75:1912-1920(2011).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS.
RX PubMed=22610130; DOI=10.1007/s10265-012-0492-8;
RA Kim Y.O., Lee Y.G., Patel D.H., Kim H.M., Ahn S.J., Bae H.J.;
RT "Zn tolerance of novel Colocasia esculenta metallothionein and its domains
RT in Escherichia coli and tobacco.";
RL J. Plant Res. 125:793-804(2012).
RN [3]
RP FUNCTION, AND INDUCTION.
RA Parmar P., Patel M., Dave B., Subramanian R.B., Bae H.J.;
RT "Isolation, cloning and expression of novel metallothionine type II protein
RT from Colocassia esculentum.";
RL Univers. J. Med. Dent. 1:37-45(2012).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC that bind various heavy metals. Probably involved in maintaining
CC homeostasis of essential transition metals and detoxification of toxic
CC metals. Increases cadmium and zinc tolerance when expressed in
CC heterologous systems. Metal chelator binding 6 cadmium or 5 zinc atoms
CC per protein. {ECO:0000269|PubMed:21979068, ECO:0000269|PubMed:22610130,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22610130}. Nucleus
CC {ECO:0000269|PubMed:22610130}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots.
CC {ECO:0000269|PubMed:22610130}.
CC -!- INDUCTION: Up-regulated by cadmium treatment. {ECO:0000269|Ref.3}.
CC -!- DOMAIN: The N-terminal (1-23) and C-terminal (66-84) Cys-rich domains
CC are both involved in zinc binding.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family.
CC {ECO:0000305}.
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DR EMBL; DQ521570; ABF71737.1; -; mRNA.
DR AlphaFoldDB; Q19LA2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR000347; Metalthion_15p.
DR PANTHER; PTHR33543; PTHR33543; 1.
DR Pfam; PF01439; Metallothio_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Metal-thiolate cluster; Nucleus.
FT CHAIN 1..84
FT /note="Metallothionein type 2b"
FT /id="PRO_0000421160"
FT MUTAGEN 82..84
FT /note="Missing: Decreased protein stability and cadmium
FT binding."
FT /evidence="ECO:0000269|PubMed:21979068"
SQ SEQUENCE 84 AA; 8414 MW; 5685ABAF658179E0 CRC64;
MSCCGGNCGC GSGCQCGNGC GGCKMFPDFG SDEKITTTHT LVLGFAPAKG SVEGFEMVAG
AAENDCKCGS NCSCTDCRCD PCNC