MT_CRAVI
ID MT_CRAVI Reviewed; 75 AA.
AC P23038;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Metallothionein;
DE Short=MT;
OS Crassostrea virginica (Eastern oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=6565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1888750; DOI=10.1016/0304-4165(91)90087-w;
RA Unger M.E., Chen T.T., Murphy C.M., Vestling M.M., Fenselau C.,
RA Roesijadi G.;
RT "Primary structure of molluscan metallothioneins deduced from PCR-amplified
RT cDNA and mass spectrometry of purified proteins.";
RL Biochim. Biophys. Acta 1074:371-377(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-28.
RC TISSUE=Gill;
RX PubMed=2774559; DOI=10.1016/0003-9861(89)90499-2;
RA Roesijadi G., Kielland S., Klerks P.;
RT "Purification and properties of novel molluscan metallothioneins.";
RL Arch. Biochem. Biophys. 273:403-413(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-25, AND ACETYLATION AT SER-2.
RC TISSUE=Gill;
RX PubMed=2065077; DOI=10.1016/0304-4165(91)90157-c;
RA Roesijadi G., Vestling M.M., Murphy C.M., Klerks P.L., Fenselau C.C.;
RT "Structure and time-dependent behavior of acetylated and non-acetylated
RT forms of a molluscan metallothionein.";
RL Biochim. Biophys. Acta 1074:230-236(1991).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions.
CC -!- INDUCTION: By cadmium.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2 family.
CC {ECO:0000305}.
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DR EMBL; X59862; CAA42522.1; -; mRNA.
DR PIR; S17156; S17156.
DR AlphaFoldDB; P23038; -.
DR SMR; P23038; -.
DR iPTMnet; P23038; -.
DR Proteomes; UP000694844; Genome assembly.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2065077,
FT ECO:0000269|PubMed:2774559"
FT CHAIN 2..75
FT /note="Metallothionein"
FT /id="PRO_0000197322"
FT BINDING 15
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 19
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 24
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
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="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 32
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="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 36
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 38
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 41
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 41
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 45
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
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 53
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 55
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 55
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 59
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="5"
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 67
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 71
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 73
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT BINDING 73
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P33187"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2065077"
SQ SEQUENCE 75 AA; 7345 MW; 636480D23D314667 CRC64;
MSDPCNCIET GTCACSDSCP ATGCKCGPGC KCGDDCKCAG CKVKCSCTSE GGCKCGEKCT
GPATCKCGSG CSCKK
