MT_ARIAR
ID MT_ARIAR Reviewed; 66 AA.
AC P55946;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Metallothionein;
DE Short=MT;
OS Arianta arbustorum (Land snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Helicidae; Arianta.
OX NCBI_TaxID=45985;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT SER-1, AND POLYMORPHISM.
RX PubMed=7487956; DOI=10.1042/bj3110951;
RA Berger B., Hunziker P.E., Hauer C.R., Birchler N., Dallinger R.;
RT "Mass spectrometry and amino acid sequencing of two cadmium-binding
RT metallothionein isoforms from the terrestrial gastropod Arianta
RT arbustorum.";
RL Biochem. J. 311:951-957(1995).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions and regulation of essential trace
CC elements.
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 -!- POLYMORPHISM: The sequence shown is that of variant A (MTA); variant B
CC (MTB) differs in a single position. {ECO:0000269|PubMed:7487956}.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family.
CC {ECO:0000305}.
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DR PIR; S59621; S59621.
DR PIR; S59622; S59622.
DR AlphaFoldDB; P55946; -.
DR SMR; P55946; -.
DR iPTMnet; P55946; -.
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 Acetylation; Cadmium; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster.
FT CHAIN 1..66
FT /note="Metallothionein"
FT /id="PRO_0000197335"
FT BINDING 9
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 13
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 13
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 18
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 20
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 24
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 30
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 32
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 35
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 35
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 38
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 40
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 45
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 47
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 47
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 51
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 51
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 57
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 59
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 63
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 65
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 65
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7487956"
FT VARIANT 60
FT /note="N -> G (in MTB)"
FT /evidence="ECO:0000269|PubMed:7487956"
SQ SEQUENCE 66 AA; 6495 MW; 6CB977276CAC23D5 CRC64;
SGKGKGDLCT AACKNEPCQC GSKCQCGEGC ACASCKTCNC TSDGCKCGKE CTGAASCKCN
SSCSCK
