GenomeNet

Database: UniProt
Entry: Q9U620
LinkDB: Q9U620
Original site: Q9U620 
ID   MTCU_CALSI              Reviewed;          64 AA.
AC   Q9U620;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   20-JUN-2018, entry version 43.
DE   RecName: Full=Copper-specific metallothionein-2;
DE   AltName: Full=CuMT-II;
OS   Callinectes sapidus (Blue crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata;
OC   Brachyura; Eubrachyura; Portunoidea; Portunidae; Callinectes.
OX   NCBI_TaxID=6763;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11790353; DOI=10.1016/S0742-8413(99)00114-0;
RA   Syring R.A., Hoexum-Brouwer T.H., Brouwer M.;
RT   "Cloning and sequencing of cDNAs encoding for a novel copper-specific
RT   metallothionein and two cadmium-inducible metallothioneins from the
RT   blue crab Callinectes sapidus.";
RL   Comp. Biochem. Physiol. 125C:325-332(2000).
CC   -!- FUNCTION: The metallothioneins are involved in the cellular
CC       sequestration of toxic metal ions and regulation of essential
CC       trace elements. This isoform binds exclusively copper.
CC   -!- DOMAIN: 14 cysteine residues are arranged in C-X-C groups. These
CC       are thought to be the metal-binding sites in other
CC       metallothioneins.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 2
CC       family. {ECO:0000305}.
DR   EMBL; AF200420; AAF08966.1; -; mRNA.
DR   ProteinModelPortal; Q9U620; -.
DR   SMR; Q9U620; -.
DR   PRIDE; Q9U620; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Copper; Metal-binding; Metal-thiolate cluster.
FT   CHAIN         1     64       Copper-specific metallothionein-2.
FT                                /FTId=PRO_0000197337.
SQ   SEQUENCE   64 AA;  6277 MW;  B0B8767AD6CE978A CRC64;
     MPCGCGTSCK CGSGKCCCGS TCNCTTCPSK QSCSCNDGAC GSACQCKTSC CCGADCKCSP
     CPMK
//
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