MT3_MOUSE
ID MT3_MOUSE Reviewed; 68 AA.
AC P28184;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1631128; DOI=10.1073/pnas.89.14.6333;
RA Palmiter R.D., Findley S.D., Whitmore T.E., Durnam D.M.;
RT "MT-III, a brain-specific member of the metallothionein gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6333-6337(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8039715; DOI=10.1016/0378-1119(94)90391-3;
RA Naruse S., Igarashi S., Furuya T., Kobayashi H., Miyatake T., Tsuji S.;
RT "Structures of the human and mouse growth inhibitory factor-encoding
RT genes.";
RL Gene 144:283-287(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007744|PDB:1JI9}
RP STRUCTURE BY NMR OF 32-68 IN COMPLEX WITH CADMIUM IONS.
RX PubMed=11560491; DOI=10.1021/bi010827l;
RA Oz G., Zangger K., Armitage I.M.;
RT "Three-dimensional structure and dynamics of a brain specific growth
RT inhibitory factor: metallothionein-3.";
RL Biochemistry 40:11433-11441(2001).
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}.
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DR EMBL; M93310; AAA39529.1; -; Genomic_DNA.
DR EMBL; S72046; AAB31397.1; -; Genomic_DNA.
DR EMBL; BC059725; AAH59725.1; -; mRNA.
DR CCDS; CCDS40436.1; -.
DR PIR; A46034; A46034.
DR RefSeq; NP_038631.1; NM_013603.2.
DR PDB; 1JI9; NMR; -; A=32-68.
DR PDBsum; 1JI9; -.
DR AlphaFoldDB; P28184; -.
DR SMR; P28184; -.
DR BioGRID; 201581; 7.
DR CORUM; P28184; -.
DR STRING; 10090.ENSMUSP00000034211; -.
DR iPTMnet; P28184; -.
DR PhosphoSitePlus; P28184; -.
DR EPD; P28184; -.
DR PaxDb; P28184; -.
DR PeptideAtlas; P28184; -.
DR PRIDE; P28184; -.
DR ProteomicsDB; 290106; -.
DR Ensembl; ENSMUST00000034211; ENSMUSP00000034211; ENSMUSG00000031760.
DR GeneID; 17751; -.
DR KEGG; mmu:17751; -.
DR UCSC; uc009mvu.2; mouse.
DR CTD; 4504; -.
DR MGI; MGI:97173; Mt3.
DR VEuPathDB; HostDB:ENSMUSG00000031760; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00940000168571; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P28184; -.
DR OMA; CCPAECK; -.
DR Reactome; R-MMU-5661231; Metallothioneins bind metals.
DR BioGRID-ORCS; 17751; 2 hits in 73 CRISPR screens.
DR EvolutionaryTrace; P28184; -.
DR PRO; PR:P28184; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P28184; protein.
DR Bgee; ENSMUSG00000031760; Expressed in choroid plexus of fourth ventricle and 211 other tissues.
DR ExpressionAtlas; P28184; baseline and differential.
DR Genevisible; P28184; MM.
DR GO; GO:0097450; C:astrocyte end-foot; ISO:MGI.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0046870; F:cadmium ion binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR GO; GO:0014002; P:astrocyte development; IDA:UniProtKB.
DR GO; GO:0055073; P:cadmium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0044242; P:cellular lipid catabolic process; IMP:UniProtKB.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IDA:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:UniProtKB.
DR GO; GO:0006707; P:cholesterol catabolic process; IMP:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP: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:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:2000296; P:negative regulation of hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IMP:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; IMP:UniProtKB.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISS:UniProtKB.
DR GO; GO:2000376; P:positive regulation of oxygen metabolic process; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0060049; P:regulation of protein glycosylation; IMP:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; IMP: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:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0055069; P:zinc ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006829; P:zinc ion transport; IDA:UniProtKB.
DR Gene3D; 4.10.10.10; -; 1.
DR InterPro; IPR003019; Metalthion.
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; PTHR23299; 1.
DR Pfam; PF00131; Metallothio; 1.
DR PRINTS; PR00860; MTVERTEBRATE.
DR SUPFAM; SSF57868; SSF57868; 1.
DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Copper; Metal-binding; Metal-thiolate cluster;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..68
FT /note="Metallothionein-3"
FT /id="PRO_0000197251"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
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:0000269|PubMed:11560491,
FT ECO:0007744|PDB:1JI9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P37359"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1JI9"
FT TURN 43..48
FT /evidence="ECO:0007829|PDB:1JI9"
SQ SEQUENCE 68 AA; 7009 MW; 791AF60E38FED3CA CRC64;
MDPETCPCPT GGSCTCSDKC KCKGCKCTNC KKSCCSCCPA GCEKCAKDCV CKGEEGAKAE
AEKCSCCQ
