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}.
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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   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.
DR   Genevisible; P04732; HS.
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
//