ID MT3_HORSE Reviewed; 68 AA. AC P37360; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 113. 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 Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796; RN [1] RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1. RC TISSUE=Brain; RX PubMed=8200454; DOI=10.1016/0014-5793(94)00452-8; RA Pountney D.L., Fundel S.M., Faller P., Birchler N.E., Hunziker P., RA Vasak M.; RT "Isolation, primary structures and metal binding properties of neuronal RT growth inhibitory factor (GIF) from bovine and equine brain."; RL FEBS Lett. 345:193-197(1994). CC -!- FUNCTION: Binds heavy metals. Contains three zinc and three copper CC atoms per polypeptide chain and only a negligible amount of cadmium. 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 PIR; S44392; S44392. DR AlphaFoldDB; P37360; -. DR SMR; P37360; -. DR STRING; 9796.ENSECAP00000012822; -. DR iPTMnet; P37360; -. DR PaxDb; 9796-ENSECAP00000012822; -. DR InParanoid; P37360; -. DR Proteomes; UP000002281; Unplaced. 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:0006112; P:energy reserve metabolic process; ISS:UniProtKB. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; ISS:UniProtKB. DR GO; GO:0033210; P:leptin-mediated signaling pathway; 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:2000376; P:positive regulation of oxygen metabolic process; 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:0032095; P:regulation of response to food; 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:0051238; P:sequestering of metal ion; ISS:UniProtKB. DR GO; GO:0006829; P:zinc ion transport; 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: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 1: Evidence at protein level; KW Acetylation; Copper; Direct protein sequencing; Metal-binding; KW Metal-thiolate cluster; Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..68 FT /note="Metallothionein-3" FT /id="PRO_0000197249" 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:0000269|PubMed:8200454" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28184" SQ SEQUENCE 68 AA; 6927 MW; 5998E0F17FC52CE6 CRC64; MDPETCPCPT GGSCTCSGEC KCEGCKCTSC KKSCCSCCPA ECEKCAKDCV CKGGEGAEAE AEKCSCCQ //