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 25-OCT-2017, entry version 73. DE RecName: Full=Metallothionein; DE Short=MT; GN Name=mt; OS Esox lucius (Northern pike). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Esociformes; Esocidae; Esox. OX NCBI_TaxID=8010; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX 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 [GENOMIC DNA]. RX 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. {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}. 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 RefSeq; XP_010882273.1; XM_010883971.3. DR ProteinModelPortal; P25127; -. DR SMR; P25127; -. DR GeneID; 105018493; -. DR KEGG; els:105018493; -. DR KO; K14739; -. DR GO; GO:0005623; C:cell; ISS:AgBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046688; P:response to copper ion; ISS:AgBase. DR Gene3D; 4.10.10.10; -; 1. DR InterPro; IPR003019; Metalthion. DR InterPro; IPR017854; Metalthion_dom. DR InterPro; IPR023587; Metalthion_dom_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_0000197283. 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. SQ SEQUENCE 60 AA; 5979 MW; 9EA1E43F95F8D97E CRC64; MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCSCCPSGC SKCASGCICK GKTCDTSCCQ //