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Database: UniProt
Entry: MTB_SALAL
LinkDB: MTB_SALAL
Original site: MTB_SALAL 
ID   MTB_SALAL               Reviewed;          60 AA.
AC   P68502; P09862; Q7ZZW6;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   01-OCT-2014, entry version 35.
DE   RecName: Full=Metallothionein B;
DE            Short=MT-B;
GN   Name=mtb;
OS   Salvelinus alpinus (Arctic char) (Salmo alpinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Salvelinus.
OX   NCBI_TaxID=8036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RA   Gerpe M., Kling P., Olsson P.-E.;
RT   "Metallothionein cDNA sequences and gene expression in arctic char
RT   (Salvelinus alpinus) following metal and PCB exposure.";
RL   Mar. Environ. Res. 46:551-554(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   McGowan C., Davidson E.A., Davidson W.S.;
RT   "Discovering single nucleotide polymorphisms in the introns of fish
RT   genes.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine
CC       residues that bind various heavy metals. {ECO:0000250}.
CC   -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains:
CC       four divalent ions are chelated within cluster A of the alpha
CC       domain and are coordinated via cysteinyl thiolate bridges to 11
CC       cysteine ligands. Cluster B, the corresponding region within the
CC       beta domain, can ligate three divalent ions to 9 cysteines.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1
CC       family. {ECO:0000305}.
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DR   EMBL; AF013801; AAB66343.1; -; mRNA.
DR   EMBL; AY267818; AAP31402.2; -; Genomic_DNA.
DR   ProteinModelPortal; P68502; -.
DR   SMR; P68502; 2-29, 31-60.
DR   HOVERGEN; HBG096123; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.10.10; -; 1.
DR   InterPro; IPR017854; Metalthion_dom.
DR   InterPro; IPR023587; Metalthion_dom_vert.
DR   InterPro; IPR003019; Metalthion_sfam_euk.
DR   InterPro; IPR000006; Metalthion_vert.
DR   InterPro; IPR018064; Metalthion_vert_metal_BS.
DR   PANTHER; PTHR23299; PTHR23299; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   PRINTS; PR00860; MTVERTEBRATE.
DR   SUPFAM; SSF57868; SSF57868; 1.
DR   PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Metal-thiolate cluster.
FT   CHAIN         1     60       Metallothionein B.
FT                                /FTId=PRO_0000197313.
FT   REGION        1     28       Beta.
FT   REGION       29     60       Alpha.
FT   METAL         4      4       Divalent metal cation; cluster B.
FT   METAL         6      6       Divalent metal cation; cluster B.
FT   METAL        12     12       Divalent metal cation; cluster B.
FT   METAL        14     14       Divalent metal cation; cluster B.
FT   METAL        18     18       Divalent metal cation; cluster B.
FT   METAL        20     20       Divalent metal cation; cluster B.
FT   METAL        23     23       Divalent metal cation; cluster B.
FT   METAL        25     25       Divalent metal cation; cluster B.
FT   METAL        28     28       Divalent metal cation; cluster B.
FT   METAL        32     32       Divalent metal cation; cluster A.
FT   METAL        33     33       Divalent metal cation; cluster A.
FT   METAL        35     35       Divalent metal cation; cluster A.
FT   METAL        36     36       Divalent metal cation; cluster A.
FT   METAL        40     40       Divalent metal cation; cluster A.
FT   METAL        43     43       Divalent metal cation; cluster A.
FT   METAL        47     47       Divalent metal cation; cluster A.
FT   METAL        49     49       Divalent metal cation; cluster A.
FT   METAL        54     54       Divalent metal cation; cluster A.
FT   METAL        58     58       Divalent metal cation; cluster A.
FT   METAL        59     59       Divalent metal cation; cluster A.
FT   CONFLICT     54     60       CDTSCCQ -> LRYQLLSV (in Ref. 2;
FT                                AAP31402). {ECO:0000305}.
SQ   SEQUENCE   60 AA;  6033 MW;  9EA1E70FBE59B4EE CRC64;
     MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCPCCPSDC SKCASGCVCK GKTCDTSCCQ
//
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