ID MTA_CHIHA Reviewed; 60 AA.
AC P68506; O13258;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-APR-2013, entry version 34.
DE RecName: Full=Metallothionein A;
DE Short=MT-A;
DE Short=MT-I;
GN Name=mta;
OS Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys
OS rhinoceratus hamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes;
OC Notothenioidei; Channichthyidae; Chionodraco.
OX NCBI_TaxID=36188;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9601077;
RA Carginale V., Scudiero R., Capasso C., Capasso A., Kille P.,
RA di Prisco G., Parisi E.;
RT "Cadmium-induced differential accumulation of metallothionein isoforms
RT in the Antarctic icefish, which exhibits no basal metallothionein
RT protein but high endogenous mRNA levels.";
RL Biochem. J. 332:475-481(1998).
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; Y12580; CAA73159.1; -; mRNA.
DR ProteinModelPortal; P68506; -.
DR SMR; P68506; 2-29, 31-60.
DR HOVERGEN; HBG096111; -.
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; Zinc.
FT CHAIN 1 60 Metallothionein A.
FT /FTId=PRO_0000197275.
FT REGION 1 28 Beta.
FT REGION 29 60 Alpha.
FT METAL 4 4 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 6 6 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 12 12 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 14 14 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 18 18 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 20 20 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 23 23 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 25 25 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 28 28 Divalent metal cation; cluster B (By
FT similarity).
FT METAL 32 32 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 33 33 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 35 35 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 36 36 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 40 40 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 43 43 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 47 47 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 49 49 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 54 54 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 58 58 Divalent metal cation; cluster A (By
FT similarity).
FT METAL 59 59 Divalent metal cation; cluster A (By
FT similarity).
SQ SEQUENCE 60 AA; 6005 MW; 5966E6145A2C424B CRC64;
MDPCDCSKSG TCNCGGSCTC TNCSCKSCKK SCCPCCPSGC TKCASGCVCK GKTCDTSCCQ
//
