ID   MT3_SHEEP               Reviewed;          65 AA.
AC   Q8MKE4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Metallothionein-3;
DE            Short=MT-3;
DE   AltName: Full=Metallothionein-III;
DE            Short=MT-III;
GN   Name=MT3;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11931634; DOI=10.1042/bj20011751;
RA   Chung R.S., Holloway A.F., Eckhardt B.L., Harris J.A., Vickers J.C.,
RA   Chuah M.I., West A.K.;
RT   "Sheep have an unusual variant of the brain-specific metallothionein,
RT   metallothionein-III.";
RL   Biochem. J. 365:323-328(2002).
CC   -!- FUNCTION: Binds heavy metals. Contains five zinc and one copper atoms
CC       per polypeptide chain and only a negligible amount of cadmium (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF500199; AAM21134.1; -; mRNA.
DR   RefSeq; NP_001009755.1; NM_001009755.1.
DR   AlphaFoldDB; Q8MKE4; -.
DR   STRING; 9940.ENSOARP00000019709; -.
DR   PaxDb; 9940-ENSOARP00000019709; -.
DR   Ensembl; ENSOART00020036937; ENSOARP00020030573; ENSOARG00020023684.
DR   GeneID; 443168; -.
DR   KEGG; oas:443168; -.
DR   CTD; 4504; -.
DR   eggNOG; KOG4738; Eukaryota.
DR   OrthoDB; 4705808at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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: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:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
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   PANTHER; PTHR23299; METALLOTHIONEIN; 1.
DR   PANTHER; PTHR23299:SF18; METALLOTHIONEIN-3; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   SUPFAM; SSF57868; Metallothionein; 1.
PE   3: Inferred from homology;
KW   Acetylation; Copper; Metal-binding; Metal-thiolate cluster; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..65
FT                   /note="Metallothionein-3"
FT                   /id="PRO_0000253583"
FT   REGION          1..30
FT                   /note="Beta"
FT   REGION          31..65
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         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         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         35
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         39
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="4"
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         46
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         48
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         48
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         63
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="6"
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   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   65 AA;  6574 MW;  EC5778D87D508798 CRC64;
     MDPEACPCPT GGSCTCSDSC KCEGCTCASS KKSCCPAECE KCAKDCVCKG GEGAEAEEKK
     CGCCQ
//