ID MT1E_HUMAN Reviewed; 61 AA.
AC P04732; A2RRF7; Q86YX4; Q8TD51;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 27-MAR-2024, entry version 193.
DE RecName: Full=Metallothionein-1E;
DE Short=MT-1E;
DE AltName: Full=Metallothionein-IE;
DE Short=MT-IE;
GN Name=MT1E;
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], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=2581970; DOI=10.1016/s0021-9258(17)39668-0;
RA Schmidt C.J., Jubier M.-F., Hamer D.H.;
RT "Structure and expression of two human metallothionein-I isoform genes and
RT a related pseudogene.";
RL J. Biol. Chem. 260:7731-7737(1985).
RN [2]
RP PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1.
RC TISSUE=Liver;
RX PubMed=1779803; DOI=10.1016/0076-6879(91)05125-f;
RA Hunziker P.E.;
RT "Amino acid sequence determination.";
RL Methods Enzymol. 205:421-426(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Guo J.H., Huang X.H., Yu L.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yu L.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-31 (ISOFORM 1/2).
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 P04732; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-12310079, EBI-10961624;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04732-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04732-2; Sequence=VSP_041603;
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}.
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; M10942; AAA59587.1; -; Genomic_DNA.
DR EMBL; AF495759; AAM15968.1; -; mRNA.
DR EMBL; AF348996; AAO32956.2; -; mRNA.
DR EMBL; AC026461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW82872.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW82874.1; -; Genomic_DNA.
DR EMBL; BC009699; AAH09699.1; -; mRNA.
DR EMBL; BC062734; AAH62734.1; -; mRNA.
DR EMBL; BC131609; AAI31610.1; -; mRNA.
DR EMBL; S68949; AAB30082.1; -; mRNA.
DR CCDS; CCDS10764.2; -. [P04732-1]
DR CCDS; CCDS86530.1; -. [P04732-2]
DR PIR; A22634; SMHU1E.
DR RefSeq; NP_783316.2; NM_175617.3. [P04732-1]
DR RefSeq; XP_005256013.1; XM_005255956.4.
DR AlphaFoldDB; P04732; -.
DR SMR; P04732; -.
DR BioGRID; 110599; 5.
DR IntAct; P04732; 2.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; P04732; -.
DR PhosphoSitePlus; P04732; -.
DR BioMuta; MT1E; -.
DR jPOST; P04732; -.
DR MassIVE; P04732; -.
DR MaxQB; P04732; -.
DR PaxDb; 9606-ENSP00000307706; -.
DR PeptideAtlas; P04732; -.
DR ProteomicsDB; 51738; -. [P04732-1]
DR ProteomicsDB; 51739; -. [P04732-2]
DR Pumba; P04732; -.
DR TopDownProteomics; P04732-1; -. [P04732-1]
DR Antibodypedia; 51264; 76 antibodies from 14 providers.
DR DNASU; 4493; -.
DR Ensembl; ENST00000306061.10; ENSP00000307706.5; ENSG00000169715.15. [P04732-1]
DR Ensembl; ENST00000330439.7; ENSP00000328137.6; ENSG00000169715.15. [P04732-2]
DR GeneID; 4493; -.
DR KEGG; hsa:4493; -.
DR MANE-Select; ENST00000330439.7; ENSP00000328137.6; NM_001363555.2; NP_001350484.1. [P04732-2]
DR UCSC; uc002ejl.5; human. [P04732-1]
DR AGR; HGNC:7397; -.
DR CTD; 4493; -.
DR DisGeNET; 4493; -.
DR GeneCards; MT1E; -.
DR HGNC; HGNC:7397; MT1E.
DR HPA; ENSG00000169715; Tissue enhanced (liver).
DR MIM; 156351; gene.
DR neXtProt; NX_P04732; -.
DR OpenTargets; ENSG00000169715; -.
DR PharmGKB; PA31202; -.
DR VEuPathDB; HostDB:ENSG00000169715; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P04732; -.
DR OMA; PNCSCGT; -.
DR OrthoDB; 4706064at2759; -.
DR PhylomeDB; P04732; -.
DR TreeFam; TF336054; -.
DR PathwayCommons; P04732; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P04732; -.
DR BioGRID-ORCS; 4493; 263 hits in 1081 CRISPR screens.
DR ChiTaRS; MT1E; human.
DR GeneWiki; MT1E; -.
DR GenomeRNAi; 4493; -.
DR Pharos; P04732; Tbio.
DR PRO; PR:P04732; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P04732; Protein.
DR Bgee; ENSG00000169715; Expressed in mucosa of transverse colon and 201 other cell types or tissues.
DR ExpressionAtlas; P04732; baseline and differential.
DR Genevisible; P04732; 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; ISS:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0045926; P:negative regulation of growth; 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:SF51; METALLOTHIONEIN-1E-RELATED; 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; Alternative splicing; Cadmium; Copper;
KW Direct protein sequencing; Metal-binding; Metal-thiolate cluster;
KW Reference proteome; Zinc.
FT CHAIN 1..61
FT /note="Metallothionein-1E"
FT /id="PRO_0000197236"
FT REGION 1..29
FT /note="Beta"
FT REGION 30..61
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 13
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 15
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 15
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 19
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 21
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 24
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 24
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 26
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 29
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 33
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 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 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 36
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 37
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 41
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 44
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 44
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 48
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 50
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 50
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 57
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 59
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="6"
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1779803"
FT VAR_SEQ 33..61
FT /note="CCSCCPVGCAKCAQGCVCKGASEKCSCCA -> ECGAISRNLGLWLRLGGNS
FT RLALSASFWGTGLSLPSLPVSFPLQAFCPKFRWGRTAFFSWDTNPNCTPYGFRTELCQT
FT KKSILWVWVLSSSQACY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_041603"
SQ SEQUENCE 61 AA; 6014 MW; 8E0A7C54F623A1D2 CRC64;
MDPNCSCATG GSCTCAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCVC KGASEKCSCC
A
//
