ID MT4_HUMAN Reviewed; 62 AA. AC P47944; Q14DA1; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 2. DT 24-JAN-2024, entry version 153. DE RecName: Full=Metallothionein-4; DE Short=MT-4; DE AltName: Full=Metallothionein-IV; DE Short=MT-IV; GN Name=MT4; 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 VARIANTS CYS-30 AND ARG-31. RX PubMed=8003488; DOI=10.1021/bi00189a029; RA Quaife C.J., Findley S.D., Erickson J.C., Froelick G.J., Kelly E.J., RA Zambrowicz B.P., Palmiter R.D.; RT "Induction of a new metallothionein isoform (MT-IV) occurs during RT differentiation of stratified squamous epithelia."; RL Biochemistry 33:7250-7259(1994). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS CYS-30 AND ARG-31. 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). CC -!- FUNCTION: Seems to bind zinc and copper. Could play a special role in CC regulating zinc metabolism during the differentiation of stratified CC epithelia. 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; U07807; AAA20232.1; -; Genomic_DNA. DR EMBL; AC026461; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC113442; AAI13443.1; -; mRNA. DR EMBL; BC113444; AAI13445.1; -; mRNA. DR CCDS; CCDS42165.1; -. DR PIR; A53640; A53640. DR RefSeq; NP_116324.1; NM_032935.2. DR AlphaFoldDB; P47944; -. DR SMR; P47944; -. DR STRING; 9606.ENSP00000219162; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB12965; Silver. DR BioMuta; MT4; -. DR DMDM; 288558817; -. DR MassIVE; P47944; -. DR PaxDb; 9606-ENSP00000219162; -. DR PeptideAtlas; P47944; -. DR ProteomicsDB; 55825; -. DR Antibodypedia; 76693; 31 antibodies from 6 providers. DR DNASU; 84560; -. DR Ensembl; ENST00000219162.4; ENSP00000219162.3; ENSG00000102891.4. DR GeneID; 84560; -. DR KEGG; hsa:84560; -. DR MANE-Select; ENST00000219162.4; ENSP00000219162.3; NM_032935.3; NP_116324.2. DR UCSC; uc002eje.1; human. DR AGR; HGNC:18705; -. DR CTD; 84560; -. DR DisGeNET; 84560; -. DR GeneCards; MT4; -. DR HGNC; HGNC:18705; MT4. DR HPA; ENSG00000102891; Tissue enriched (skin). DR MIM; 606206; gene. DR neXtProt; NX_P47944; -. DR OpenTargets; ENSG00000102891; -. DR PharmGKB; PA38649; -. DR VEuPathDB; HostDB:ENSG00000102891; -. DR eggNOG; KOG4738; Eukaryota. DR GeneTree; ENSGT00950000182967; -. DR HOGENOM; CLU_171204_2_0_1; -. DR InParanoid; P47944; -. DR OMA; DKCGCCP; -. DR PhylomeDB; P47944; -. DR TreeFam; TF336054; -. DR PathwayCommons; P47944; -. DR Reactome; R-HSA-5661231; Metallothioneins bind metals. DR BioGRID-ORCS; 84560; 15 hits in 1107 CRISPR screens. DR ChiTaRS; MT4; human. DR GenomeRNAi; 84560; -. DR Pharos; P47944; Tbio. DR PRO; PR:P47944; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P47944; Protein. DR Bgee; ENSG00000102891; Expressed in primordial germ cell in gonad and 76 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0071276; P:cellular response to cadmium ion; IBA:GO_Central. DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central. DR GO; GO:0071294; P:cellular response to zinc ion; IBA:GO_Central. 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 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:SF12; METALLOTHIONEIN-4; 1. DR Pfam; PF00131; Metallothio; 1. DR PRINTS; PR00860; MTVERTEBRATE. DR SUPFAM; SSF57868; Metallothionein; 1. PE 3: Inferred from homology; KW Copper; Metal-binding; Metal-thiolate cluster; Reference proteome; Zinc. FT CHAIN 1..62 FT /note="Metallothionein-4" FT /id="PRO_0000197255" 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="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 VARIANT 30 FT /note="Y -> C (in dbSNP:rs666636)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8003488" FT /id="VAR_034110" FT VARIANT 31 FT /note="W -> R (in dbSNP:rs666647)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8003488" FT /id="VAR_034111" FT VARIANT 48 FT /note="G -> D (in dbSNP:rs11643815)" FT /id="VAR_034112" SQ SEQUENCE 62 AA; 6509 MW; 55DA475A17BF28C9 CRC64; MDPRECVCMS GGICMCGDNC KCTTCNCKTY WKSCCPCCPP GCAKCARGCI CKGGSDKCSC CP //