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Metallothionein-2 (MT-2) (Metallothionein-II) (MT-II)

 MT2_CANLF               Reviewed;          61 AA.
Q9XST5;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 116.
RecName: Full=Metallothionein-2;
Short=MT-2;
AltName: Full=Metallothionein-II;
Short=MT-II;
Name=MT2A; Synonyms=MT2; ORFNames=B28;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=4062298; DOI=10.1016/0003-9861(85)90778-7;
Lerch K., Johnson G.F., Grushoff P.S., Sternlieb I.;
"Canine hepatic lysosomal copper protein: identification as
metallothionein.";
Arch. Biochem. Biophys. 243:108-114(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle; TISSUE=Kidney;
Kobayashi K., Morita T., Shimada A.;
"Molecular cloning and expression of canine metallothionein-II.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thyroid;
PubMed=10964405; DOI=10.1006/abio.2000.4674;
Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C.,
Christophe D.;
"A method for the large-scale cloning of nuclear proteins and nuclear
targeting sequences on a functional basis.";
Anal. Biochem. 284:231-239(2000).
-!- FUNCTION: Metallothioneins have a high content of cysteine
residues that bind various heavy metals; these proteins are
transcriptionally regulated by both heavy metals and
glucocorticoids.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains:
four divalent ions are chelated within cluster A of the alpha
domain and are coordinated via cysteinyl thiolate bridges to 11
cysteine ligands. Cluster B, the corresponding region within the
beta domain, can ligate three divalent ions to 9 cysteines.
-!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1
family. {ECO:0000305}.
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EMBL; AB028042; BAA87327.1; -; mRNA.
EMBL; AJ388530; CAB46832.1; -; mRNA.
RefSeq; NP_001003149.1; NM_001003149.1.
UniGene; Cfa.3542; -.
ProteinModelPortal; Q9XST5; -.
SMR; Q9XST5; -.
STRING; 9615.ENSCAFP00000013399; -.
PaxDb; Q9XST5; -.
PRIDE; Q9XST5; -.
Ensembl; ENSCAFT00000014487; ENSCAFP00000013399; ENSCAFG00000023759.
GeneID; 403768; -.
KEGG; cfa:403768; -.
CTD; 4502; -.
eggNOG; ENOG410JFS1; Eukaryota.
eggNOG; ENOG41113QR; LUCA.
GeneTree; ENSGT00730000110883; -.
HOGENOM; HOG000236262; -.
InParanoid; Q9XST5; -.
KO; K14739; -.
OMA; CNCAGSC; -.
TreeFam; TF336054; -.
Proteomes; UP000002254; Chromosome 2.
Bgee; ENSCAFG00000023759; Expressed in 3 organ(s), highest expression level in liver.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
Gene3D; 4.10.10.10; -; 1.
InterPro; IPR003019; Metalthion.
InterPro; IPR017854; Metalthion_dom_sf.
InterPro; IPR023587; Metalthion_dom_sf_vert.
InterPro; IPR000006; Metalthion_vert.
InterPro; IPR018064; Metalthion_vert_metal_BS.
PANTHER; PTHR23299; PTHR23299; 1.
Pfam; PF00131; Metallothio; 1.
PRINTS; PR00860; MTVERTEBRATE.
SUPFAM; SSF57868; SSF57868; 1.
PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Metal-binding; Metal-thiolate cluster; Phosphoprotein;
Reference proteome.
CHAIN 1 61 Metallothionein-2.
/FTId=PRO_0000197199.
REGION 1 29 Beta.
REGION 30 61 Alpha.
METAL 5 5 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 7 7 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 13 13 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 15 15 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 19 19 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 21 21 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 24 24 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 26 26 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 29 29 Divalent metal cation; cluster B.
{ECO:0000250}.
METAL 33 33 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 34 34 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 36 36 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 37 37 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 41 41 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 44 44 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 48 48 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 50 50 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 57 57 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 59 59 Divalent metal cation; cluster A.
{ECO:0000250}.
METAL 60 60 Divalent metal cation; cluster A.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P68301}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P02795}.
SEQUENCE 61 AA; 6012 MW; 7B0A7C54E272C448 CRC64;
MDPNCSCAAG GSCTCAGSCK CKECRCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC
A


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