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Database: UniProt
Entry: MT2_STECO
LinkDB: MT2_STECO
Original site: MT2_STECO 
ID   MT2_STECO               Reviewed;          61 AA.
AC   P14425;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   16-OCT-2013, entry version 66.
DE   RecName: Full=Metallothionein-2;
DE            Short=MT-2;
DE   AltName: Full=Metallothionein-II;
DE            Short=MT-II;
GN   Name=MT2;
OS   Stenella coeruleoalba (Striped dolphin) (Delphinus coeruleoalbus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
OC   Odontoceti; Delphinidae; Stenella.
OX   NCBI_TaxID=9737;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Kidney;
RA   Kwohn Y.-T., Okubo A., Hirano H., Kagawa H., Yamazaki S., Toda S.;
RT   "Primary structure of striped dolphin renal metallothionein II.";
RL   Agric. Biol. Chem. 52:837-841(1988).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine
CC       residues that bind various heavy metals; these proteins are
CC       transcriptionally regulated by both heavy metals and
CC       glucocorticoids.
CC   -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains:
CC       four divalent ions are chelated within cluster A of the alpha
CC       domain and are coordinated via cysteinyl thiolate bridges to 11
CC       cysteine ligands. Cluster B, the corresponding region within the
CC       beta domain, can ligate three divalent ions to 9 cysteines.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1
CC       family.
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DR   ProteinModelPortal; P14425; -.
DR   SMR; P14425; 1-61.
DR   HOVERGEN; HBG009063; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR   GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR   Gene3D; 4.10.10.10; -; 1.
DR   InterPro; IPR017854; Metalthion_dom.
DR   InterPro; IPR023587; Metalthion_dom_vert.
DR   InterPro; IPR003019; Metalthion_sfam_euk.
DR   InterPro; IPR000006; Metalthion_vert.
DR   InterPro; IPR018064; Metalthion_vert_metal_BS.
DR   PANTHER; PTHR23299; PTHR23299; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   PRINTS; PR00860; MTVERTEBRATE.
DR   SUPFAM; SSF57868; SSF57868; 1.
DR   PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Metal-binding;
KW   Metal-thiolate cluster; Zinc.
FT   CHAIN         1     61       Metallothionein-2.
FT                                /FTId=PRO_0000197231.
FT   REGION        1     29       Beta.
FT   REGION       30     61       Alpha.
FT   METAL         5      5       Divalent metal cation; cluster B.
FT   METAL         7      7       Divalent metal cation; cluster B.
FT   METAL        13     13       Divalent metal cation; cluster B.
FT   METAL        15     15       Divalent metal cation; cluster B.
FT   METAL        19     19       Divalent metal cation; cluster B.
FT   METAL        21     21       Divalent metal cation; cluster B.
FT   METAL        24     24       Divalent metal cation; cluster B.
FT   METAL        26     26       Divalent metal cation; cluster B.
FT   METAL        29     29       Divalent metal cation; cluster B.
FT   METAL        33     33       Divalent metal cation; cluster A.
FT   METAL        34     34       Divalent metal cation; cluster A.
FT   METAL        36     36       Divalent metal cation; cluster A.
FT   METAL        37     37       Divalent metal cation; cluster A.
FT   METAL        41     41       Divalent metal cation; cluster A.
FT   METAL        44     44       Divalent metal cation; cluster A.
FT   METAL        48     48       Divalent metal cation; cluster A.
FT   METAL        50     50       Divalent metal cation; cluster A.
FT   METAL        57     57       Divalent metal cation; cluster A.
FT   METAL        59     59       Divalent metal cation; cluster A.
FT   METAL        60     60       Divalent metal cation; cluster A.
FT   MOD_RES       1      1       N-acetylmethionine.
SQ   SEQUENCE   61 AA;  6010 MW;  056F66E4F43E557D CRC64;
     MDPNCSCTAG GSCACPGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC
     A
//
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