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 06-MAR-2013, entry version 32.
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; Euteleostei;
OC Protacanthopterygii; Salmoniformes; Salmonidae; Salmoninae;
OC 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 (By similarity).
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.
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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; Metallothionein_sfam; 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).
SQ SEQUENCE 60 AA; 6033 MW; 9EA1E70FBE59B4EE CRC64;
MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCPCCPSDC SKCASGCVCK GKTCDTSCCQ
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