Reviewed, UniProtKB/Swiss-Prot P04355 (MT2_RAT)

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

61

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Beta strand

16 – 18

3

Beta strand

35 – 37

3

Turn

38 – 40

3

Turn

43 – 46

4

Sequences

	Sequence		Length	Mass (Da)
	P04355-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: D50D1306A5ED08E9	FASTA	61	6,145
	10 20 30 40 50 60 MDPNCSCATD GSCSCAGSCK CKQCKCTSCK KSCCSCCPVG CAKCSQGCIC KEASDKCSCC A

References

[1]	"Structural characterization of the isoforms of neonatal and adult rat liver metallothionein." Winge D.R., Nielson K.B., Zeikus R.D., Gray W.R. J. Biol. Chem. 259:11419-11425(1984) [PubMed: 6470004] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.
[2]	"Rat metallothionein multigene family." Andersen R.D., Taplitz S.J., Birren B.W., Bristol G., Herschman H.R. Experientia Suppl. 52:373-384(1987) [PubMed: 2959527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Single crystals of cadmium, zinc metallothionein." Melis K.A., Carter D.C., Stout C.D., Winge D.R. J. Biol. Chem. 258:6255-6257(1983) [PubMed: 6853483] [Abstract] Cited for: CRYSTALLIZATION.
[4]	"Crystal structure of Cd,Zn metallothionein." Furey W.F. Jr., Robbins A.H., Clancy L.L., Winge D.R., Wand B.C., Stout C.D. Science 231:704-710(1986) [PubMed: 3945804] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]	"Refined crystal structure of Cd, Zn metallothionein at 2.0-A resolution." Robbins A.H., McRee D.E., Williamson M., Collett S.A., Xuong N.H., Furey W.F. Jr., Wang B.C., Stout C.D. J. Mol. Biol. 221:1269-1293(1991) [PubMed: 1942051] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]	"Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy." Schultze P., Woergotter E., Braun W., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K. J. Mol. Biol. 203:251-268(1988) [PubMed: 3184190] [Abstract] Cited for: STRUCTURE BY NMR.
[7]	"Sequence-specific 1H-NMR assignments in rat-liver metallothionein-2." Woergoetter E., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K. Eur. J. Biochem. 167:457-466(1987) [PubMed: 3653102] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M11794 Genomic DNA. Translation: AAA41640.1.

PIR

SMRT2. B61561.

RefSeq

XP_001062488.1.
XP_001070713.1.

UniGene

Rn.115549
Rn.54397

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MRT	NMR	-	A	31-61	[»]
2MRT	NMR	-	A	1-30	[»]
4MT2	X-ray	2.00	A	1-61	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04355.

Genome annotation databases

Ensembl

ENSRNOG00000028841. Rattus norvegicus. [Contig view]

GeneID

689415.

KEGG

rno:682651.
rno:689415.

Phylogenomic databases

HOVERGEN

P04355.

Gene expression databases

ArrayExpress

P04355.

GermOnline

ENSRNOG00000028841. Rattus norvegicus.

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

P04355.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

P04355.

ProtoNet

Search...

Entry information

Entry name

MT2_RAT

Accession

Primary (citable) accession number: P04355

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	September 2, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)