MT_NEUCR
ID MT_NEUCR Reviewed; 26 AA.
AC P02807; Q7S702; V5ILF3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Metallothionein;
DE Short=MT;
GN Name=cmt; Synonyms=ccg-12; ORFNames=NCU05561;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2932331; DOI=10.1002/j.1460-2075.1985.tb03985.x;
RA Muenger K., Germann U.A., Lerch K.;
RT "Isolation and structural organization of the Neurospora crassa copper
RT metallothionein gene.";
RL EMBO J. 4:2665-2668(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2148862; DOI=10.1128/aem.56.9.2748-2754.1990;
RA Romeyer F.M., Jacobs F.A., Brousseau R.;
RT "Expression of a Neurospora crassa metallothionein and its variants in
RT Escherichia coli.";
RL Appl. Environ. Microbiol. 56:2748-2754(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2959528; DOI=10.1007/978-3-0348-6784-9_37;
RA Muenger K., Germann U.A., Lerch K.;
RT "Isolation and regulation of expression of the Neurospora crassa copper
RT metallothionein gene.";
RL Experientia Suppl. 52:393-400(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [5]
RP PROTEIN SEQUENCE OF 2-26, AND COPPER BINDING SITES.
RX PubMed=6444697; DOI=10.1038/284368a0;
RA Lerch K.;
RT "Copper metallothionein, a copper-binding protein from Neurospora crassa.";
RL Nature 284:368-370(1980).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=2525920; DOI=10.1021/bi00433a038;
RA Malikayil J.A., Lerch K., Armitage I.M.;
RT "Proton NMR studies of a metallothionein from Neurospora crassa: sequence-
RT specific assignments by NOE measurements in the rotating frame.";
RL Biochemistry 28:2991-2995(1989).
CC -!- INDUCTION: By copper.
CC -!- MISCELLANEOUS: The seven cysteines bind six copper (cuprous) ions.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 8 family.
CC {ECO:0000305}.
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DR EMBL; X03009; CAA26793.1; -; Genomic_DNA.
DR EMBL; M59836; AAA33594.1; -; Genomic_DNA.
DR EMBL; M27709; AAA33595.1; -; Genomic_DNA.
DR EMBL; CM002241; ESA42185.1; -; Genomic_DNA.
DR PIR; A24641; SMNC.
DR RefSeq; XP_011394960.1; XM_011396658.1.
DR PDB; 1T2Y; NMR; -; A=2-26.
DR PDBsum; 1T2Y; -.
DR AlphaFoldDB; P02807; -.
DR BMRB; P02807; -.
DR SMR; P02807; -.
DR EnsemblFungi; ESA42185; ESA42185; NCU05561.
DR GeneID; 23568444; -.
DR KEGG; ncr:NCU05561; -.
DR VEuPathDB; FungiDB:NCU05561; -.
DR EvolutionaryTrace; P02807; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR SUPFAM; SSF57868; SSF57868; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6444697"
FT PEPTIDE 2..26
FT /note="Metallothionein"
FT /id="PRO_0000197364"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Cys residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 6
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 6
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 12
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 12
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 14
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 20
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 20
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 23
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:6444697"
FT BINDING 23
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:6444697"
FT CONFLICT 22
FT /note="N -> T (in Ref. 2; AAA33594)"
FT /evidence="ECO:0000305"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1T2Y"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1T2Y"
SQ SEQUENCE 26 AA; 2366 MW; 252562AE5FD422FC CRC64;
MGDCGCSGAS SCNCGSGCSC SNCGSK
