ID MT2_PIG Reviewed; 61 AA. AC P79379; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Metallothionein-2A; DE Short=MT-2A; DE AltName: Full=Metallothionein-IIA; DE Short=MT-IIA; GN Name=MT2A; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=9573337; DOI=10.1016/s0378-1119(98)00067-5; RA Huang M.-C., Pan P.K., Zheng T.F., Chen N.C., Peng J.Y., Huang P.C.; RT "Multiple isoforms of metallothionein are expressed in the porcine liver."; RL Gene 211:49-55(1998). CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues CC that bind various heavy metals; these proteins are transcriptionally CC regulated by both heavy metals and glucocorticoids. CC -!- SUBUNIT: Interacts with EOLA1. {ECO:0000250|UniProtKB:P02795}. 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; AB000794; BAA19183.1; -; mRNA. DR RefSeq; XP_003355856.1; XM_003355808.3. DR AlphaFoldDB; P79379; -. DR SMR; P79379; -. DR STRING; 9823.ENSSSCP00000022537; -. DR PaxDb; 9823-ENSSSCP00000022537; -. DR PeptideAtlas; P79379; -. DR Ensembl; ENSSSCT00000029059.4; ENSSSCP00000022537.1; ENSSSCG00000030300.4. DR Ensembl; ENSSSCT00005068183.1; ENSSSCP00005042401.1; ENSSSCG00005042511.1. DR Ensembl; ENSSSCT00015013884.1; ENSSSCP00015005387.1; ENSSSCG00015010574.1. DR Ensembl; ENSSSCT00025104572.1; ENSSSCP00025046512.1; ENSSSCG00025075743.1. DR Ensembl; ENSSSCT00030080241.1; ENSSSCP00030036757.1; ENSSSCG00030057548.1. DR Ensembl; ENSSSCT00035076496.1; ENSSSCP00035031255.1; ENSSSCG00035057202.1. DR Ensembl; ENSSSCT00040035994.1; ENSSSCP00040014920.1; ENSSSCG00040026909.1. DR Ensembl; ENSSSCT00045057812.1; ENSSSCP00045040423.1; ENSSSCG00045033767.1. DR Ensembl; ENSSSCT00050060894.1; ENSSSCP00050026179.1; ENSSSCG00050044734.1. DR Ensembl; ENSSSCT00060099893.1; ENSSSCP00060043336.1; ENSSSCG00060073107.1. DR Ensembl; ENSSSCT00065104451.1; ENSSSCP00065046298.1; ENSSSCG00065075661.1. DR Ensembl; ENSSSCT00070000714.1; ENSSSCP00070000625.1; ENSSSCG00070000389.1. DR GeneID; 396827; -. DR KEGG; ssc:396827; -. DR CTD; 396827; -. DR eggNOG; KOG4738; Eukaryota. DR GeneTree; ENSGT00950000182967; -. DR HOGENOM; CLU_171204_2_0_1; -. DR InParanoid; P79379; -. DR OMA; CCACCPV; -. DR TreeFam; TF336054; -. DR Reactome; R-SSC-5661231; Metallothioneins bind metals. DR Proteomes; UP000008227; Chromosome 6. DR Proteomes; UP000314985; Chromosome 6. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000030300; Expressed in right lobe of liver and 44 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. 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; ISS:UniProtKB. 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:0045926; P:negative regulation of growth; ISS:UniProtKB. 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:SF63; METALLOTHIONEIN 1H-LIKE PROTEIN 1-RELATED; 1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR SUPFAM; SSF57868; Metallothionein; 1. DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1. DR Genevisible; P79379; SS. PE 3: Inferred from homology; KW Acetylation; Metal-binding; Metal-thiolate cluster; Phosphoprotein; KW Reference proteome. FT CHAIN 1..61 FT /note="Metallothionein-2A" FT /id="PRO_0000197213" FT REGION 1..29 FT /note="Beta" FT REGION 30..61 FT /note="Alpha" FT BINDING 5 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 7 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 7 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 13 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 15 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 15 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 19 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 21 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 24 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 24 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 26 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 29 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 33 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 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 34 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 36 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 37 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 41 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 44 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 44 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 48 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 50 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 50 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 57 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 60 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 60 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 MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P18055" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02795" SQ SEQUENCE 61 AA; 5970 MW; 6E1F7C54F430A1D3 CRC64; MDPNCSCAAG GSCTCAGSCK CKDCKCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC A //