P02802 (MT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metallothionein-1
Short name=MT-1

Alternative name(s):
Metallothionein-I
Short name=MT-I

Gene names

Name:

Mt1

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 › Mus

Protein attributes

Sequence length	61 AA.
Sequence status	Complete.
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular metal ion homeostasis Inferred from direct assay. Source: MGI cellular response to chromate Inferred from direct assay. Source: MGI cellular response to zinc ion Inferred from direct assay. Source: MGI cellular zinc ion homeostasis Inferred from mutant phenotype. Source: MGI negative regulation of growth Inferred from sequence or structural similarity. Source: UniProtKB nitric oxide mediated signal transduction Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI lysosome Inferred from direct assay. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	copper ion binding Inferred from direct assay. Source: MGI zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 61

61

Metallothionein-1

PRO_0000197206

Regions

Region

1 – 29

29

Beta

Region

30 – 61

32

Alpha

Sites

Metal binding

5

1

Divalent metal cation; cluster B

Metal binding

7

1

Divalent metal cation; cluster B

Metal binding

13

1

Divalent metal cation; cluster B

Metal binding

15

1

Divalent metal cation; cluster B

Metal binding

19

1

Divalent metal cation; cluster B

Metal binding

21

1

Divalent metal cation; cluster B

Metal binding

24

1

Divalent metal cation; cluster B

Metal binding

26

1

Divalent metal cation; cluster B

Metal binding

29

1

Divalent metal cation; cluster B

Metal binding

33

1

Divalent metal cation; cluster A

Metal binding

34

1

Divalent metal cation; cluster A

Metal binding

36

1

Divalent metal cation; cluster A

Metal binding

37

1

Divalent metal cation; cluster A

Metal binding

41

1

Divalent metal cation; cluster A

Metal binding

44

1

Divalent metal cation; cluster A

Metal binding

48

1

Divalent metal cation; cluster A

Metal binding

50

1

Divalent metal cation; cluster A

Metal binding

57

1

Divalent metal cation; cluster A

Metal binding

59

1

Divalent metal cation; cluster A

Metal binding

60

1

Divalent metal cation; cluster A

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.1

Experimental info

Sequence conflict

23

1

N → D AA sequence Ref.1

Sequence conflict

32

1

S → G Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

61

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Beta strand

20 – 23

4

Beta strand

25 – 28

4

Beta strand

35 – 37

3

Beta strand

42 – 47

6

Sequences

	Sequence		Length	Mass (Da)
	P02802 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 4B3754EC759C0ADB	FASTA	61	6,018
	10 20 30 40 50 60 MDPNCSCSTG GSCTCTSSCA CKNCKCTSCK KSCCSCCPVG CSKCAQGCVC KGAADKCTCC A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse liver metallothioneins. Complete amino acid sequence of metallothionein-I." Huang I.-Y., Yoshida A., Tsunoo H., Nakajima H. J. Biol. Chem. 252:8217-8221(1977) [PubMed: 914867] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.
[2]	"Structure of mouse metallothionein-I gene and its mRNA." Glanville N., Durnam D.M., Palmiter R.D. Nature 292:267-269(1981) [PubMed: 7254320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Isolation and characterization of the mouse metallothionein-I gene." Durnam D.M., Perrin F., Gannon F., Palmiter R.D. Proc. Natl. Acad. Sci. U.S.A. 77:6511-6515(1980) [PubMed: 6935664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[4]	"Cloning and sequencing of cDNA for mouse liver metallothionein-I." Mbikay M., Maiti I.B., Thirion J.-P. Biochem. Biophys. Res. Commun. 103:825-832(1981) [PubMed: 6277322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Production of a bifunctional hybrid molecule B72.3/metallothionein-1 by protein engineering." Xiang J., Koropatnick J., Qi Y., Luo X., Moyana T., Li K., Chen Y. Immunology 78:574-581(1993) [PubMed: 8495976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[6]	"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.
[7]	"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: FVB/N. Tissue: Colon.
[8]	"Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy." Zangger K., Oez G., Otvos J.D., Armitage I.M. Protein Sci. 8:2630-2638(1999) [PubMed: 10631978] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S62785 mRNA. Translation: AAB26768.1.
J00605 Genomic DNA. Translation: AAA39527.2.
AK018727 mRNA. Translation: BAC25563.1.
BC036990 mRNA. Translation: AAH36990.1.

IPI

IPI00113696.

PIR

SMMSI. A93261.

RefSeq

NP_038630.1. NM_013602.3.

UniGene

Mm.192991.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DFS	NMR	-	A	31-61	[»]
1DFT	NMR	-	A	1-30	[»]

ProteinModelPortal

P02802.

SMR

P02802. Positions 1-61.

ModBase

Search...

Protein-protein interaction databases

STRING

P02802.

PTM databases

PhosphoSite

P02802.

Proteomic databases

PRIDE

P02802.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034215; ENSMUSP00000034215; ENSMUSG00000031765.

GeneID

17748.

KEGG

mmu:17748.

UCSC

uc009mvw.2. mouse.

Organism-specific databases

CTD

17748.

MGI

MGI:97171. Mt1.

Phylogenomic databases

eggNOG

maNOG21730.

GeneTree

ENSGT00390000010461.

HOVERGEN

HBG009063.

Gene expression databases

ArrayExpress

P02802.

Bgee

P02802.

CleanEx

MM_MT1.

Genevestigator

P02802.

GermOnline

ENSMUSG00000031765. Mus musculus.

Family and domain databases

InterPro

IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]

Gene3D

G3DSA:4.10.10.10. Metallothionein_vert. 1 hit.

KO

K14739.

PANTHER

PTHR23299. Metallothionein_vert. 1 hit.

Pfam

PF00131. Metallothio. 1 hit.
[Graphical view]

PRINTS

PR00860. MTVERTEBRATE.

SUPFAM

SSF57868. Metallothionein_sfam. 1 hit.

PROSITE

PS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

292401.

SOURCE

Search...

Entry information

Entry name

MT1_MOUSE

Accession

Primary (citable) accession number: P02802
Secondary accession number(s): Q64485

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 14, 2011
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program