ID MT_PODSI Reviewed; 63 AA.
AC Q708T3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-APR-2013, entry version 36.
DE RecName: Full=Metallothionein;
DE Short=MT;
OS Podarcis sicula (Italian wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Scleroglossa; Scincomorpha; Lacertoidea;
OC Lacertidae; Podarcis.
OX NCBI_TaxID=65484;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=14579413; DOI=10.1002/mrd.10365;
RA Riggio M., Trinchella F., Filosa S., Parisi E., Scudiero R.;
RT "Accumulation of zinc, copper and metallothionein mRNA in lizard ovary
RT proceeds without a concomitant increase in metallothionein content.";
RL Mol. Reprod. Dev. 66:374-382(2003).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine
CC residues that bind various heavy metals (By similarity).
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; AJ609541; CAE81349.1; -; mRNA.
DR ProteinModelPortal; Q708T3; -.
DR SMR; Q708T3; 32-63.
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 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 3: Inferred from homology;
KW Metal-binding; Metal-thiolate cluster.
FT CHAIN 1 63 Metallothionein.
FT /FTId=PRO_0000197267.
FT REGION 1 30 Beta.
FT REGION 31 63 Alpha.
FT METAL 6 6 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 8 8 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 14 14 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 16 16 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 20 20 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 22 22 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 25 25 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 27 27 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 30 30 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 34 34 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 35 35 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 37 37 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 38 38 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 42 42 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 45 45 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 49 49 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 51 51 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 59 59 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 61 61 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 62 62 Divalent metal cation; cluster A (By
FT similarity).
SQ SEQUENCE 63 AA; 6356 MW; 4A892600DE378C51 CRC64;
MDPQDCACAT GASCTCAGSC KCKNCKCTSC KKSCCSCCPA GCAKCAKSCV CKEPLSDKCS
CCT
//
