ID MT_ESOLU Reviewed; 60 AA. AC P25127; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 31-OCT-2006, entry version 37. DE Metallothionein (MT). GN Name=MT; OS Esox lucius (Northern pike). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Esociformes; OC Esocidae; Esox. OX NCBI_TaxID=8010; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver; RX MEDLINE=91316146; PubMed=1859844; DOI=10.1016/0167-4781(91)90187-Q; RA Kille P., Stephens P.E., Kay J.; RT "Elucidation of cDNA sequences for metallothioneins from rainbow RT trout, stone loach and pike liver using the polymerase chain RT reaction."; RL Biochim. Biophys. Acta 1089:407-410(1991). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=94032489; PubMed=8218416; DOI=10.1016/0167-4781(93)90037-E; RA Kille P., Kay J., Sweeney G.E.; RT "Analysis of regulatory elements flanking metallothionein genes in Cd- RT tolerant fish (pike and stone loach)."; RL Biochim. Biophys. Acta 1216:55-64(1993). 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59392; CAA42035.1; -; mRNA. DR EMBL; X70042; CAA49636.1; -; Genomic_DNA. DR PIR; S38334; S31723. DR HSSP; O73914; 1M0G. DR InterPro; IPR003019; Metallthion_. DR InterPro; IPR000006; Metallthion_1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1. KW Metal-binding; Metal-thiolate cluster. FT CHAIN 1 60 Metallothionein. FT /FTId=PRO_0000197283. FT REGION 1 28 Beta. FT REGION 29 60 Alpha. FT METAL 4 4 Cluster B. FT METAL 6 6 Cluster B. FT METAL 12 12 Cluster B. FT METAL 14 14 Cluster B. FT METAL 18 18 Cluster B. FT METAL 20 20 Cluster B. FT METAL 23 23 Cluster B. FT METAL 25 25 Cluster B. FT METAL 28 28 Cluster B. FT METAL 32 32 Cluster A. FT METAL 33 33 Cluster A. FT METAL 35 35 Cluster A. FT METAL 36 36 Cluster A. FT METAL 40 40 Cluster A. FT METAL 43 43 Cluster A. FT METAL 47 47 Cluster A. FT METAL 49 49 Cluster A. FT METAL 54 54 Cluster A. FT METAL 58 58 Cluster A. FT METAL 59 59 Cluster A. SQ SEQUENCE 60 AA; 5979 MW; 9EA1E43F95F8D97E CRC64; MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCSCCPSGC SKCASGCICK GKTCDTSCCQ //