Reviewed, UniProtKB/Swiss-Prot Q9XST5 (MT2_CANFA)

Names and origin

Protein names

Recommended name:
    Metallothionein-2
      Short name=MT-2
Alternative name(s):
    Metallothionein-II
      Short name=MT-II

Gene names

Name:	MT2A
Synonyms:	MT2
ORF Names:	B28

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	61 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 structure	Monomer By similarity.
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.
Sequence similarities	Belongs to the metallothionein superfamily. Type 1 family.

Ontologies

Keywords
Ligand	Metal-binding Metal-thiolate cluster
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 61	61	Metallothionein-2		PRO_0000197199
Regions
	Region	1 – 29	29	Beta
	Region	30 – 61	32	Alpha
Sites
	Metal binding	5	1	Cluster B By similarity
	Metal binding	7	1	Cluster B By similarity
	Metal binding	13	1	Cluster B By similarity
	Metal binding	15	1	Cluster B By similarity
	Metal binding	19	1	Cluster B By similarity
	Metal binding	21	1	Cluster B By similarity
	Metal binding	24	1	Cluster B By similarity
	Metal binding	26	1	Cluster B By similarity
	Metal binding	29	1	Cluster B By similarity
	Metal binding	33	1	Cluster A By similarity
	Metal binding	34	1	Cluster A By similarity
	Metal binding	36	1	Cluster A By similarity
	Metal binding	37	1	Cluster A By similarity
	Metal binding	41	1	Cluster A By similarity
	Metal binding	44	1	Cluster A By similarity
	Metal binding	48	1	Cluster A By similarity
	Metal binding	50	1	Cluster A By similarity
	Metal binding	57	1	Cluster A By similarity
	Metal binding	59	1	Cluster A By similarity
	Metal binding	60	1	Cluster A By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	51	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XST5-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7B0A7C54E272C448	FASTA	61	6,012
	10 20 30 40 50 60 MDPNCSCAAG GSCTCAGSCK CKECRCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Canine hepatic lysosomal copper protein: identification as metallothionein." Lerch K., Johnson G.F., Grushoff P.S., Sternlieb I. Arch. Biochem. Biophys. 243:108-114(1985) [PubMed: 4062298] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.
[2]	"Molecular cloning and expression of canine metallothionein-II." Kobayashi K., Morita T., Shimada A. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Beagle. Tissue: Kidney.
[3]	"A method for the large-scale cloning of nuclear proteins and nuclear targeting sequences on a functional basis." Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D. Anal. Biochem. 284:231-239(2000) [PubMed: 10964405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB028042 mRNA. Translation: BAA87327.1. AJ388530 mRNA. Translation: CAB46832.1.
RefSeq	NP_001003149.1.
UniGene	Cfa.3542
3D structure databases
SMR	Q9XST5. Positions 1-61.
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000014487; ENSCAFP00000013399; ENSCAFG00000023759; Canis familiaris. [Genome view]
GeneID	403768.
KEGG	cfa:403768.
Organism-specific databases
CTD	403768.
Phylogenomic databases
HOVERGEN	Q9XST5.
OMA	SQGCICK
OrthoDB	EOG91ZHW5
Family and domain databases
InterPro	IPR017854. Metallothionein_sfam. IPR003019. Metallothionein_sfam_euk. IPR000006. Metallothionein_vert. IPR018064. Metallothionein_vert_metal_BS. [Graphical view]
Gene3D	G3DSA:4.10.10.10. Metallothionein_vert. 1 hit.
PANTHER	PTHR23299. Metallothionein_vert. 1 hit.
Pfam	PF00131. Metallothio. 1 hit. [Graphical view]
PRINTS	PR00860. MTVERTEBRATE.
PROSITE	PS00203. METALLOTHIONEIN_VRT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MT2_CANFA

Accession

Primary (citable) accession number: Q9XST5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1999
Last modified:	November 24, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)