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 17-JUN-2020, entry version 85. 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; Esociformes; OC 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 trout, RT stone loach and pike liver using the polymerase chain 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 residues CC that bind various heavy metals. {ECO:0000250}. CC -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four CC divalent ions are chelated within cluster A of the alpha domain and are CC coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. CC Cluster B, the corresponding region within the beta domain, can ligate CC three divalent ions to 9 cysteines. CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family. CC {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 SMR; P25127; -. DR PRIDE; P25127; -. DR Ensembl; ENSELUT00000039651; ENSELUP00000036627; ENSELUG00000015987. DR GeneID; 105018493; -. DR KEGG; els:105018493; -. DR GeneTree; ENSGT00950000182967; -. DR KO; K14739; -. DR OMA; CEGCTCA; -. DR Proteomes; UP000265140; LG19. DR GO; GO:0005623; C:cell; ISS:AgBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0046688; P:response to copper ion; ISS:AgBase. DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. 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; Reference proteome. FT CHAIN 1..60 FT /note="Metallothionein" FT /id="PRO_0000197283" FT REGION 1..28 FT /note="Beta" FT REGION 29..60 FT /note="Alpha" FT METAL 4 FT /note="Divalent metal cation; cluster B" FT METAL 6 FT /note="Divalent metal cation; cluster B" FT METAL 12 FT /note="Divalent metal cation; cluster B" FT METAL 14 FT /note="Divalent metal cation; cluster B" FT METAL 18 FT /note="Divalent metal cation; cluster B" FT METAL 20 FT /note="Divalent metal cation; cluster B" FT METAL 23 FT /note="Divalent metal cation; cluster B" FT METAL 25 FT /note="Divalent metal cation; cluster B" FT METAL 28 FT /note="Divalent metal cation; cluster B" FT METAL 32 FT /note="Divalent metal cation; cluster A" FT METAL 33 FT /note="Divalent metal cation; cluster A" FT METAL 35 FT /note="Divalent metal cation; cluster A" FT METAL 36 FT /note="Divalent metal cation; cluster A" FT METAL 40 FT /note="Divalent metal cation; cluster A" FT METAL 43 FT /note="Divalent metal cation; cluster A" FT METAL 47 FT /note="Divalent metal cation; cluster A" FT METAL 49 FT /note="Divalent metal cation; cluster A" FT METAL 54 FT /note="Divalent metal cation; cluster A" FT METAL 58 FT /note="Divalent metal cation; cluster A" FT METAL 59 FT /note="Divalent metal cation; cluster A" SQ SEQUENCE 60 AA; 5979 MW; 9EA1E43F95F8D97E CRC64; MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCSCCPSGC SKCASGCICK GKTCDTSCCQ //