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 03-APR-2013, entry version 65.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; Metallothionein_sfam; 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
//
