Reviewed, UniProtKB/Swiss-Prot P02798 (MT2_MOUSE)

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:

Mt2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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.
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)
Biological process	cellular zinc ion homeostasis Inferred from mutant phenotype. Source: MGI detoxification of copper ion Inferred from mutant phenotype. Source: MGI nitric oxide mediated signal transduction Inferred from mutant phenotype. Source: MGI
Molecular function	zinc ion binding Traceable author statement. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 61	61	Metallothionein-2
Regions
	Region	1 – 29	29	Beta
	Region	30 – 61	32	Alpha
Sites
	Metal binding	5	1	Cluster B
	Metal binding	7	1	Cluster B
	Metal binding	13	1	Cluster B
	Metal binding	15	1	Cluster B
	Metal binding	19	1	Cluster B
	Metal binding	21	1	Cluster B
	Metal binding	24	1	Cluster B
	Metal binding	26	1	Cluster B
	Metal binding	29	1	Cluster B
	Metal binding	33	1	Cluster A
	Metal binding	34	1	Cluster A
	Metal binding	36	1	Cluster A
	Metal binding	37	1	Cluster A
	Metal binding	41	1	Cluster A
	Metal binding	44	1	Cluster A
	Metal binding	48	1	Cluster A
	Metal binding	50	1	Cluster A
	Metal binding	57	1	Cluster A
	Metal binding	59	1	Cluster A
	Metal binding	60	1	Cluster A
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine
	Modified residue	51	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	52	1	E → Q AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P02798-1 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: A20D1311166672EC	FASTA	61	6,115
	10 20 30 40 50 60 MDPNCSCASD GSCSCAGACK CKQCKCTSCK KSCCSCCPVG CAKCSQGCIC KEASDKCSCC A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of mouse liver metallothionein-II." Huang I.-Y., Kimura M., Hata A., Tsunoo H., Yoshida A. J. Biochem. 89:1839-1845(1981) [PubMed: 7287658] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Regulation, linkage, and sequence of mouse metallothionein I and II genes." Searle P.F., Davison B.L., Stuart G.W., Wilkie T.M., Norstedt G., Palmiter R.D. Mol. Cell. Biol. 4:1221-1230(1984) [PubMed: 6095054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	K02236 Genomic DNA. Translation: AAA39528.1. AK002567 mRNA. Translation: BAB22192.1. BC031758 mRNA. Translation: AAH31758.1.
PIR	SMMS2. A03275. I57572.
RefSeq	NP_032656.1.
UniGene	Mm.147226
3D structure databases
HSSP	HSSP built from PDB template 1MRT based on UniProtKB P04355.
SMR	P02798. Positions 1-61.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000031762. Mus musculus. [Contig view]
GeneID	17750.
KEGG	mmu:17750.
Organism-specific databases
MGI	MGI:97172. Mt2.
Phylogenomic databases
HOGENOM	P02798.
HOVERGEN	P02798.
Gene expression databases
ArrayExpress	P02798.
CleanEx	MM_MT2.
GermOnline	ENSMUSG00000031762. Mus musculus.
Family and domain databases
InterPro	IPR002400. GF_cysknot. IPR003019. Metallothionein_sfam_euk. IPR000006. Metallothionein_vert. [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	PR00438. GFCYSKNOT. PR00860. MTVERTEBRATE.
PROSITE	PS00203. METALLOTHIONEIN_VRT. 1 hit. [Graphical view]
ProDom	P02798. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

MT2_MOUSE

Accession

Primary (citable) accession number: P02798

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1991
Last modified:	July 22, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)