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Database: UniProt
Entry: MTA_COLVI
LinkDB: MTA_COLVI
Original site: MTA_COLVI 
ID   MTA_COLVI               Reviewed;          43 AA.
AC   P27086;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   09-JUL-2014, entry version 67.
DE   RecName: Full=Metallothionein A;
DE            Short=MTA;
DE   Flags: Fragment;
OS   Colinus virginianus (Northern bobwhite) (Tetrao virginianus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes;
OC   Odontophoridae; Colinus.
OX   NCBI_TaxID=9014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8483164; DOI=10.1007/BF00160481;
RA   Shartzer K.L., Kage K., Sobieski R.J., Andrews G.K.;
RT   "Evolution of avian metallothionein: DNA sequence analyses of the
RT   turkey metallothionein gene and metallothionein cDNAs from pheasant
RT   and quail.";
RL   J. Mol. Evol. 36:255-262(1993).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine
CC       residues that bind various heavy metals.
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   EMBL; X62511; CAA44370.1; -; mRNA.
DR   PIR; S33378; S18173.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   PANTHER; PTHR23299; PTHR23299; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   PRINTS; PR00860; MTVERTEBRATE.
DR   SUPFAM; SSF57868; SSF57868; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Metal-thiolate cluster.
FT   CHAIN        <1    >43       Metallothionein A.
FT                                /FTId=PRO_0000197263.
FT   REGION       <1     16       Beta.
FT   REGION       17    >43       Alpha.
FT   METAL         2      2       Divalent metal cation; cluster B.
FT   METAL         6      6       Divalent metal cation; cluster B.
FT   METAL         8      8       Divalent metal cation; cluster B.
FT   METAL        11     11       Divalent metal cation; cluster B.
FT   METAL        13     13       Divalent metal cation; cluster B.
FT   METAL        16     16       Divalent metal cation; cluster B.
FT   METAL        20     20       Divalent metal cation; cluster A.
FT   METAL        21     21       Divalent metal cation; cluster A.
FT   METAL        23     23       Divalent metal cation; cluster A.
FT   METAL        24     24       Divalent metal cation; cluster A.
FT   METAL        28     28       Divalent metal cation; cluster A.
FT   METAL        31     31       Divalent metal cation; cluster A.
FT   METAL        35     35       Divalent metal cation; cluster A.
FT   METAL        37     37       Divalent metal cation; cluster A.
FT   NON_TER       1      1
FT   NON_TER      43     43
SQ   SEQUENCE   43 AA;  4401 MW;  1612EB52656EB875 CRC64;
     SCAGSCKCKN CRCRSCRKSC CSCCPAGCNN CAKGCVCKEP ASS
//
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