ID MT_CHICK Reviewed; 63 AA. AC P68497; P09576; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 18-JUN-2025, entry version 99. DE RecName: Full=Metallothionein; DE Short=MT; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=2448773; DOI=10.1073/pnas.85.2.309; RA McCormick C.C., Fullmer C.S., Garvey J.S.; RT "Amino acid sequence and comparative antigenicity of chicken RT metallothionein."; RL Proc. Natl. Acad. Sci. U.S.A. 85:309-313(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=White leghorn; RX PubMed=3340548; DOI=10.1093/nar/16.2.537; RA Wei D., Andrews G.K.; RT "Molecular cloning of chicken metallothionein. Deduction of the complete RT amino acid sequence and analysis of expression using cloned cDNA."; RL Nucleic Acids Res. 16:537-553(1988). RN [3] RP PROTEIN SEQUENCE. RX PubMed=2645390; DOI=10.1093/jn/119.2.309; RA Fernando L.P., Wei D., Andrews G.K.; RT "Structure and expression of chicken metallothionein."; RL J. Nutr. 119:309-318(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2806910; DOI=10.1016/0378-1119(89)90349-1; RA Fernando L.P., Andrews G.K.; RT "Cloning and expression of an avian metallothionein-encoding gene."; RL Gene 81:177-183(1989). CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues CC that bind various heavy metals. 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; X06749; CAA29924.1; -; mRNA. DR EMBL; X13545; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A34958; A34958. DR RefSeq; NP_990606.1; NM_205275.2. DR AlphaFoldDB; P68497; -. DR SMR; P68497; -. DR FunCoup; P68497; 17. DR STRING; 9031.ENSGALP00000042113; -. DR PaxDb; 9031-ENSGALP00000042113; -. DR Ensembl; ENSGALT00010057893.1; ENSGALP00010035125.1; ENSGALG00010023744.1. DR GeneID; 396212; -. DR KEGG; gga:396212; -. DR CTD; 84560; -. DR VEuPathDB; HostDB:geneid_396212; -. DR eggNOG; KOG4738; Eukaryota. DR GeneTree; ENSGT00950000182967; -. DR HOGENOM; CLU_171204_2_0_1; -. DR InParanoid; P68497; -. DR OMA; KECKCSS; -. DR PhylomeDB; P68497; -. DR Reactome; R-GGA-5661231; Metallothioneins bind metals. DR PRO; PR:P68497; -. DR Proteomes; UP000000539; Chromosome 11. DR Bgee; ENSGALG00000028451; Expressed in kidney and 14 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; ISS:AgBase. DR GO; GO:0071276; P:cellular response to cadmium ion; IBA:GO_Central. DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central. DR GO; GO:0071294; P:cellular response to zinc ion; IBA:GO_Central. DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IBA:GO_Central. DR GO; GO:0070555; P:response to interleukin-1; IDA:AgBase. DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:AgBase. DR FunFam; 4.10.10.10:FF:000001; Metallothionein; 1. DR Gene3D; 4.10.10.10; Metallothionein Isoform II; 1. 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; METALLOTHIONEIN; 1. DR PANTHER; PTHR23299:SF24; METALLOTHIONEIN-1X; 1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR SUPFAM; SSF57868; Metallothionein; 1. DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Metal-binding; Metal-thiolate cluster; KW Reference proteome; Zinc. FT CHAIN 1..63 FT /note="Metallothionein" FT /id="PRO_0000197260" FT REGION 1..30 FT /note="Beta" FT REGION 31..63 FT /note="Alpha" FT BINDING 6 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 14 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 16 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 16 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 20 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 22 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 25 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 25 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 27 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 30 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="3" FT /ligand_note="in cluster B" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 34 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="4" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 35 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="4" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 35 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="5" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 37 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="5" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 38 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="5" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 38 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="6" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 42 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="6" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 45 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="4" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 45 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="6" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 49 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="4" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 51 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="5" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 51 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="7" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 59 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="7" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 61 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="7" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 62 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="6" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" FT BINDING 62 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="7" FT /ligand_note="in cluster A" FT /evidence="ECO:0000250|UniProtKB:P02795" SQ SEQUENCE 63 AA; 6462 MW; 0062422501B9CC84 CRC64; MDPQDCTCAA GDSCSCAGSC KCKNCRCRSC RKSCCSCCPA GCNNCAKGCV CKEPASSKCS CCH //