MTCU_HELPO
ID MTCU_HELPO Reviewed; 64 AA.
AC P55947;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Copper-metallothionein;
DE AltName: Full=Cu-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=Mantle;
RX PubMed=9230430; DOI=10.1038/40785;
RA Dallinger R., Berger B., Hunziker P.E., Kaegi J.H.R.;
RT "Metallothionein in snail Cd and Cu metabolism.";
RL Nature 388:237-238(1997).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions and regulation of essential trace
CC elements. This isoform binds exclusively copper.
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 AlphaFoldDB; P55947; -.
DR SMR; P55947; -.
DR iPTMnet; P55947; -.
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; Copper; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster.
FT CHAIN 1..64
FT /note="Copper-metallothionein"
FT /id="PRO_0000197338"
FT BINDING 7
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 11
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 11
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 22
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 24
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 24
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 28
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 30
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 33
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 33
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 36
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 38
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 43
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 45
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 45
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 49
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 49
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 55
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 57
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 61
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 63
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:9230430"
FT BINDING 63
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:9230430"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9230430"
SQ SEQUENCE 64 AA; 6205 MW; 96CC1998B7E12297 CRC64;
SGRGKNCGGA CNSNPCSCGN DCKCGAGCNC DRCSSCHCSN DDCKCGSQCT GSGSCKCGSA
CGCK
