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Database: UniProt
Entry: Q98SI5_SQUCE
LinkDB: Q98SI5_SQUCE
Original site: Q98SI5_SQUCE 
ID   Q98SI5_SQUCE            Unreviewed;        49 AA.
AC   Q98SI5;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Metallothionein {ECO:0000256|RuleBase:RU000621};
DE   Flags: Fragment;
GN   Name=MT {ECO:0000313|EMBL:AAK31301.1};
OS   Squalius cephalus (Chub) (Leuciscus cephalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Leuciscidae; Leuciscinae; Squalius.
OX   NCBI_TaxID=8284 {ECO:0000313|EMBL:AAK31301.1};
RN   [1] {ECO:0000313|EMBL:AAK31301.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AAK31301.1};
RX   PubMed=15178096; DOI=10.1016/j.marenvres.2004.03.059;
RA   Hayes R.A., Regondi S., Winter M.J., Butler P.J., Agradi E., Taylor E.W.,
RA   Chipman J.K.;
RT   "Cloning of a chub metallothionein cDNA and development of competitive RT-
RT   PCR of chub metallothionein mRNA as a potential biomarker of heavy metal
RT   exposure.";
RL   Mar. Environ. Res. 58:665-669(2004).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC       that bind various heavy metals. {ECO:0000256|ARBA:ARBA00002568,
CC       ECO:0000256|RuleBase:RU000621}.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC       {ECO:0000256|ARBA:ARBA00007283, ECO:0000256|RuleBase:RU000621}.
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DR   EMBL; AY029370; AAK31301.1; -; mRNA.
DR   AlphaFoldDB; Q98SI5; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF18; METALLOTHIONEIN-3; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   SUPFAM; SSF57868; Metallothionein; 1.
DR   PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000621};
KW   Metal-thiolate cluster {ECO:0000256|ARBA:ARBA00022851,
KW   ECO:0000256|RuleBase:RU000621}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK31301.1"
FT   NON_TER         49
FT                   /evidence="ECO:0000313|EMBL:AAK31301.1"
SQ   SEQUENCE   49 AA;  4803 MW;  AFCDC7534D883CBA CRC64;
     AKTGTCNCGA TCKCTNCQCT TCKKSCCTCC PSGCSKCASG CVCKGNSCG
//
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