ID MT3_PIG Reviewed; 68 AA. AC P55944; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 10-JUN-2026, entry version 132. DE RecName: Full=Metallothionein-3; DE Short=MT-3; DE AltName: Full=Growth inhibitory factor; DE Short=GIF; DE AltName: Full=Metallothionein-III; DE Short=MT-III; GN Name=MT3; 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=Brain; RX PubMed=8896330; DOI=10.1016/0305-0491(96)00080-6; RA Chen C.-F., Wang S.-H., Lin L.-Y.; RT "Identification and characterization of metallothionein III (growth RT inhibitory factor) from porcine brain."; RL Comp. Biochem. Physiol. 115B:27-32(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9426250; DOI=10.1016/s0378-1119(97)00513-1; RA Wang S.-H., Chang C.-Y., Chen C.-F., Tam M.F., Shih Y.H., Lin L.-Y.; RT "Cloning of porcine neuron growth inhibitory factor (metallothionein III) RT cDNA and expression of the gene in Saccharomyces cerevisiae."; RL Gene 203:189-197(1997). CC -!- FUNCTION: Binds heavy metals. Contains three zinc and three copper CC atoms per polypeptide chain and only a negligible amount of cadmium. CC Inhibits survival and neurite formation of cortical neurons in vitro CC (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Brain. 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; U95969; AAC39165.1; -; mRNA. DR PIR; JC6521; JC6521. DR RefSeq; NP_999221.1; NM_214056.1. DR AlphaFoldDB; P55944; -. DR SMR; P55944; -. DR FunCoup; P55944; 501. DR STRING; 9823.ENSSSCP00000033186; -. DR PaxDb; 9823-ENSSSCP00000033186; -. DR PeptideAtlas; P55944; -. DR Ensembl; ENSSSCT00000027420.4; ENSSSCP00000026223.2; ENSSSCG00000024305.4. DR Ensembl; ENSSSCT00045056893.1; ENSSSCP00045039740.1; ENSSSCG00045033264.1. DR Ensembl; ENSSSCT00060099559.1; ENSSSCP00060043196.1; ENSSSCG00060072837.1. DR GeneID; 397123; -. DR KEGG; ssc:397123; -. DR CTD; 4504; -. DR VGNC; VGNC:107155; MT3. DR eggNOG; KOG4738; Eukaryota. DR GeneTree; ENSGT00950000182967; -. DR InParanoid; P55944; -. DR OMA; CEDSCKC; -. DR Reactome; R-SSC-5661231; Metallothioneins bind metals. DR Proteomes; UP000008227; Chromosome 6. DR Bgee; ENSSSCG00000024305; Expressed in frontal cortex and 43 other cell types or tissues. DR ExpressionAtlas; P55944; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB. DR GO; GO:0046870; F:cadmium ion binding; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB. DR GO; GO:1990748; P:cellular detoxification; 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:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB. DR GO; GO:0006829; P:zinc ion transport; ISS:UniProtKB. 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:SF18; METALLOTHIONEIN-3; 1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR SUPFAM; SSF57868; Metallothionein; 1. DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1. PE 2: Evidence at transcript level; KW Acetylation; Copper; Metal-binding; Metal-thiolate cluster; Phosphoprotein; KW Reference proteome; Zinc. FT CHAIN 1..68 FT /note="Metallothionein-3" FT /id="PRO_0000197252" FT REGION 1..30 FT /note="Beta" FT REGION 31..68 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 64 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 66 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 67 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 67 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:P37359" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28184" SQ SEQUENCE 68 AA; 6927 MW; ED801B8331E53300 CRC64; MDPETCPCPT GGSCTCAGSC KCEGCKCTSC KKSCCSCCPA ECEKCAKDCV CKGGEGAEAE EEKCSCCQ //