MT1G_HUMAN
ID MT1G_HUMAN Reviewed; 62 AA.
AC P13640; P80296;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Metallothionein-1G;
DE Short=MT-1G;
DE AltName: Full=Metallothionein-1K;
DE Short=MT-1K;
DE AltName: Full=Metallothionein-IG;
DE Short=MT-IG;
GN Name=MT1G; Synonyms=MT1K, MT1M;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3403543; DOI=10.1016/s0021-9258(18)37990-0;
RA Foster R., Jahroudi N., Varshney U., Gedamu L.;
RT "Structure and expression of the human metallothionein-IG gene.
RT Differential promoter activity of two linked metallothionein-I genes in
RT response to heavy metals.";
RL J. Biol. Chem. 263:11528-11535(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2444457; DOI=10.1007/978-3-0348-6784-9_34;
RA Gedamu L., Varshney U., Jahroudi N., Foster R., Shworak N.W.;
RT "Structure and expression of the human metallothionein genes.";
RL Experientia Suppl. 52:361-372(1987).
RN [3]
RP PROTEIN SEQUENCE (ISOFORM 1).
RC TISSUE=Liver;
RA Hunziker P.E.;
RL Submitted (NOV-1993) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-31 (ISOFORM 2), AND ACETYLATION AT MET-1.
RX PubMed=8119276; DOI=10.1111/j.1432-1033.1994.tb18603.x;
RA Pauwels M., van Weyenbergh J., Soumillion A., Proost P., Ley M.;
RT "Induction by zinc of specific metallothionein isoforms in human
RT monocytes.";
RL Eur. J. Biochem. 220:105-110(1994).
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: Monomer.
CC -!- INTERACTION:
CC P13640; P58062: SPINK7; NbExp=3; IntAct=EBI-1182473, EBI-1182445;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13640-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13640-2; Sequence=VSP_017230;
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}.
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DR EMBL; J03910; AAA59873.1; -; Genomic_DNA.
DR EMBL; BC020757; AAH20757.1; -; mRNA.
DR EMBL; S68954; AAB30083.1; -; mRNA.
DR CCDS; CCDS10766.1; -. [P13640-2]
DR CCDS; CCDS76873.1; -. [P13640-1]
DR PIR; A29236; SMHU1G.
DR RefSeq; NP_001288196.1; NM_001301267.1. [P13640-1]
DR RefSeq; NP_005941.1; NM_005950.2. [P13640-2]
DR AlphaFoldDB; P13640; -.
DR SMR; P13640; -.
DR BioGRID; 110601; 6.
DR IntAct; P13640; 2.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; P13640; -.
DR PhosphoSitePlus; P13640; -.
DR BioMuta; MT1G; -.
DR DMDM; 90109444; -.
DR EPD; P13640; -.
DR jPOST; P13640; -.
DR MassIVE; P13640; -.
DR MaxQB; P13640; -.
DR PaxDb; P13640; -.
DR PeptideAtlas; P13640; -.
DR PRIDE; P13640; -.
DR ProteomicsDB; 52948; -. [P13640-1]
DR ProteomicsDB; 52949; -. [P13640-2]
DR TopDownProteomics; P13640-2; -. [P13640-2]
DR Antibodypedia; 71774; 39 antibodies from 8 providers.
DR DNASU; 4495; -.
DR Ensembl; ENST00000379811.4; ENSP00000369139.4; ENSG00000125144.14. [P13640-1]
DR Ensembl; ENST00000444837.6; ENSP00000391397.2; ENSG00000125144.14. [P13640-2]
DR GeneID; 4495; -.
DR KEGG; hsa:4495; -.
DR MANE-Select; ENST00000379811.4; ENSP00000369139.4; NM_001301267.2; NP_001288196.1.
DR UCSC; uc002eju.2; human. [P13640-1]
DR CTD; 4495; -.
DR DisGeNET; 4495; -.
DR GeneCards; MT1G; -.
DR HGNC; HGNC:7399; MT1G.
DR HPA; ENSG00000125144; Tissue enhanced (kidney, liver, thyroid gland).
DR MIM; 156353; gene.
DR neXtProt; NX_P13640; -.
DR OpenTargets; ENSG00000125144; -.
DR PharmGKB; PA31204; -.
DR VEuPathDB; HostDB:ENSG00000125144; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P13640; -.
DR OMA; CCKECIC; -.
DR PhylomeDB; P13640; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P13640; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P13640; -.
DR SIGNOR; P13640; -.
DR BioGRID-ORCS; 4495; 21 hits in 671 CRISPR screens.
DR ChiTaRS; MT1G; human.
DR GeneWiki; Metallothionein_1G; -.
DR GenomeRNAi; 4495; -.
DR Pharos; P13640; Tbio.
DR PRO; PR:P13640; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P13640; protein.
DR Bgee; ENSG00000125144; Expressed in mucosa of transverse colon and 196 other tissues.
DR ExpressionAtlas; P13640; baseline and differential.
DR Genevisible; P13640; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEP:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IDA:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0042117; P:monocyte activation; NAS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; NAS:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; 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 Acetylation; Alternative splicing; Cadmium; Copper;
KW Direct protein sequencing; Metal-binding; Metal-thiolate cluster;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..62
FT /note="Metallothionein-1G"
FT /id="PRO_0000197238"
FT REGION 1..29
FT /note="Beta"
FT REGION 31..62
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 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 58
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="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="6"
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8119276"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT VAR_SEQ 10
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8119276"
FT /id="VSP_017230"
SQ SEQUENCE 62 AA; 6141 MW; A1B390F5899DD040 CRC64;
MDPNCSCAAA GVSCTCASSC KCKECKCTSC KKSCCSCCPV GCAKCAQGCI CKGASEKCSC
CA
