MT1_NEOLU
ID MT1_NEOLU Reviewed; 24 AA.
AC P84865;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Metallothionein;
OS Neonectria lugdunensis (Aquatic fungus) (Heliscus lugdunensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=57155;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, INDUCTION, MASS SPECTROMETRY, DISULFIDE BONDS,
RP AND CADMIUM BINDING.
RC TISSUE=Mycelium {ECO:0000269|PubMed:15939401};
RX PubMed=15939401; DOI=10.1016/j.bbrc.2005.05.083;
RA Jaeckel P., Krauss G., Menge S., Schierhorn A., Ruecknagel P., Krauss G.J.;
RT "Cadmium induces a novel metallothionein and phytochelatin 2 in an aquatic
RT fungus.";
RL Biochem. Biophys. Res. Commun. 333:150-155(2005).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC that bind various heavy metals. {ECO:0000269|PubMed:15939401}.
CC -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:15939401}.
CC -!- PTM: Contains 4 disulfide bonds. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2321.5; Method=MALDI; Note=The measured mass is
CC that of apo-metallothionein with intact disulfide bonds.;
CC Evidence={ECO:0000269|PubMed:15939401};
CC -!- MASS SPECTROMETRY: Mass=2329.7; Method=MALDI; Note=The measured mass is
CC that of apo-metallothionein treated with acid to cleave disulfide
CC bonds.; Evidence={ECO:0000269|PubMed:15939401};
CC -!- MASS SPECTROMETRY: Mass=2431.5; Method=MALDI; Note=The measured mass is
CC that of metallothionein with intact disulfide bonds chelating one
CC cadmium ion.; Evidence={ECO:0000269|PubMed:15939401};
CC -!- MASS SPECTROMETRY: Mass=2541.5; Method=MALDI; Note=The measured mass is
CC that of metallothionein with intact disulfide bonds chelating 2 cadmium
CC ions.; Evidence={ECO:0000269|PubMed:15939401};
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 8 family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P84865; -.
DR GO; GO:0046911; F:metal chelating activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Cadmium; Direct protein sequencing; Disulfide bond; Metal-binding;
KW Metal-thiolate cluster.
FT PEPTIDE 1..24
FT /note="Metallothionein"
FT /evidence="ECO:0000269|PubMed:15939401"
FT /id="PRO_0000244521"
FT BINDING 3
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 5
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 5
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 8
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 8
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 10
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 17
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 17
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 22
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:15939401"
FT BINDING 22
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:15939401"
SQ SEQUENCE 24 AA; 2331 MW; 6568E5C8BE87E8FF CRC64;
SPCTCSTCNC AGACNSCSCT SCSH
