MTCD_HELPO
ID MTCD_HELPO Reviewed; 66 AA.
AC P33187;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Cadmium-metallothionein;
DE Short=CD-MT;
OS Helix pomatia (Roman snail) (Edible snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Helicidae; Helix.
OX NCBI_TaxID=6536;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC TISSUE=Midgut;
RX PubMed=8404892; DOI=10.1111/j.1432-1033.1993.tb18193.x;
RA Dallinger R., Berger B., Hunziker P.E., Birchler N., Hauer C.R.,
RA Kaegi J.H.R.;
RT "Purification and primary structure of snail metallothionein. Similarity of
RT the N-terminal sequence with histones H4 and H2A.";
RL Eur. J. Biochem. 216:739-746(1993).
RN [2] {ECO:0007744|PDB:6QK5, ECO:0007744|PDB:6QK6}
RP STRUCTURE BY NMR IN COMPLEXES WITH CADMIUM AND ZINC IONS.
RX PubMed=31633358; DOI=10.1021/acs.biochem.9b00830;
RA Beil A., Jurt S., Walser R., Schonhut T., Guntert P., Palacios O.,
RA Atrian S., Capdevila M., Dallinger R., Zerbe O.;
RT "The Solution Structure and Dynamics of Cd-Metallothionein from Helix
RT pomatia Reveal Optimization for Binding Cd over Zn.";
RL Biochemistry 58:4570-4581(2019).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions and regulation of essential trace
CC elements. Binds almost exclusively cadmium.
CC -!- INDUCTION: By cadmium.
CC -!- DOMAIN: 14 cysteine residues are arranged in C-X-C groups. These are
CC thought to be the metal-binding sites in other metallothioneins.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family.
CC {ECO:0000305}.
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DR PIR; S36866; S36866.
DR PDB; 6QK5; NMR; -; A=1-66.
DR PDB; 6QK6; NMR; -; A=1-66.
DR PDBsum; 6QK5; -.
DR PDBsum; 6QK6; -.
DR AlphaFoldDB; P33187; -.
DR BMRB; P33187; -.
DR SMR; P33187; -.
DR iPTMnet; P33187; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR001008; Metalthion_mollusc.
DR PRINTS; PR00875; MTMOLLUSC.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cadmium; Direct protein sequencing;
KW Metal-binding; Metal-thiolate cluster.
FT CHAIN 1..66
FT /note="Cadmium-metallothionein"
FT /id="PRO_0000197336"
FT BINDING 9
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 13
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 13
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 18
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 20
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 24
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 30
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 32
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 35
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 35
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 38
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 40
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 45
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 47
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 47
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 51
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 51
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 57
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 59
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 63
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 65
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT BINDING 65
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31633358,
FT ECO:0007744|PDB:6QK6"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:8404892"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:6QK5"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6QK5"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6QK5"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6QK5"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6QK5"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6QK5"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6QK6"
SQ SEQUENCE 66 AA; 6568 MW; 6E5EFC5E0A239603 CRC64;
SGKGKGEKCT SACRSEPCQC GSKCQCGEGC TCAACKTCNC TSDGCKCGKE CTGPDSCKCG
SSCSCK
