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Database: UniProt
Entry: P52723
LinkDB: P52723
Original site: P52723 
ID   MT_CARAU                Reviewed;          60 AA.
AC   P52723;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   23-MAY-2018, entry version 70.
DE   RecName: Full=Metallothionein;
DE            Short=MT;
GN   Name=mt;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Kille P., Olsson P.-E.;
RT   "The use of metallothionein genes for determining the phylogenetic and
RT   evolutionary relationship between extant teleosts.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7999050; DOI=10.1006/bbrc.1994.2674;
RA   Chan K.M.;
RT   "PCR-cloning of goldfish and tilapia metallothionein complementary
RT   DNAs.";
RL   Biochem. Biophys. Res. Commun. 205:368-374(1994).
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}.
DR   EMBL; X97271; CAA65926.1; -; mRNA.
DR   EMBL; S75039; AAB32777.1; -; mRNA.
DR   PIR; JC2419; JC2419.
DR   ProteinModelPortal; P52723; -.
DR   SMR; P52723; -.
DR   PRIDE; P52723; -.
DR   HOVERGEN; HBG009063; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.10.10; -; 1.
DR   InterPro; IPR003019; Metalthion.
DR   InterPro; IPR017854; Metalthion_dom_sf.
DR   InterPro; IPR023587; Metalthion_dom_sf_vert.
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.
FT                                /FTId=PRO_0000197270.
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      5      5       D -> E (in Ref. 2; AAB32777).
FT                                {ECO:0000305}.
FT   CONFLICT     34     34       S -> F (in Ref. 2; AAB32777).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       K -> N (in Ref. 2; AAB32777).
FT                                {ECO:0000305}.
SQ   SEQUENCE   60 AA;  5932 MW;  54223F7D2D3BB701 CRC64;
     MDPCDCAKTG ACNCGATCKC TNCQCTTCKK SCCSCCPSGC SKCASGCVCK GNSCGSSCCQ
//
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