Reviewed, UniProtKB/Swiss-Prot P18055 (MT2A_RABIT)

Names and origin

Protein names	Recommended name:     Metallothionein-2A       Short name=MT-2A Alternative name(s):     Metallothionein-IIA       Short name=MT-IIA
Organism	Oryctolagus cuniculus (Rabbit)
Taxonomic identifier	9986 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	62 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.
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	Cadmium Copper Metal-binding Metal-thiolate cluster Zinc
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	cadmium ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc 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 – 62

62

Metallothionein-2A

PRO_0000197216

Regions

Region

1 – 30

30

Beta

Region

31 – 62

32

Alpha

Sites

Metal binding

5

1

Cluster B

Metal binding

7

1

Cluster B

Metal binding

14

1

Cluster B

Metal binding

16

1

Cluster B

Metal binding

20

1

Cluster B

Metal binding

22

1

Cluster B

Metal binding

25

1

Cluster B

Metal binding

27

1

Cluster B

Metal binding

30

1

Cluster B

Metal binding

34

1

Cluster A

Metal binding

35

1

Cluster A

Metal binding

37

1

Cluster A

Metal binding

38

1

Cluster A

Metal binding

42

1

Cluster A

Metal binding

45

1

Cluster A

Metal binding

49

1

Cluster A

Metal binding

51

1

Cluster A

Metal binding

58

1

Cluster A

Metal binding

60

1

Cluster A

Metal binding

61

1

Cluster A

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Secondary structure

1

.

.

.

.

.

.

.

62

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Beta strand

36 – 38

3

Beta strand

46 – 48

3

Sequences

	Sequence		Length	Mass (Da)
	P18055-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: C3FEA7B701081B3E	FASTA	62	6,083
	10 20 30 40 50 60 MDPNCSCAAA GDSCTCANSC TCKACKCTSC KKSCCSCCPP GCAKCAQGCI CKGASDKCSC CA

References

[1]	"Amino acid sequence determination." Hunziker P.E. Methods Enzymol. 205:421-426(1991) [PubMed: 1779803] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: New Zealand white. Tissue: Kidney and Liver.
[2]	"Primary structures of seven metallothioneins from rabbit tissue." Hunziker P.E., Kaur P., Wan M., Kaenzig A. Biochem. J. 306:265-270(1995) [PubMed: 7864820] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: New Zealand white. Tissue: Kidney and Liver.
[3]	"Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2." Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K. Eur. J. Biochem. 157:275-289(1986) [PubMed: 3709538] [Abstract] Cited for: STRUCTURE BY NMR, PROTEIN SEQUENCE.
[4]	"Nuclear magnetic resonance identification of 'half-turn' and 3(10)-helix secondary structure in rabbit liver metallothionein-2." Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K. J. Mol. Biol. 187:131-135(1986) [PubMed: 3959079] [Abstract] Cited for: STRUCTURE BY NMR.
[5]	"Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance." Arseniev A., Schultze P., Worgotter E., Braun W., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K. J. Mol. Biol. 201:637-657(1988) [PubMed: 3418714] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

PIR

A37425.
S54336.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MRB	NMR	-	A	32-62	[»]
2MRB	NMR	-	A	1-31	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P18055.

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

MT2A_RABIT

Accession

Primary (citable) accession number: P18055

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	November 24, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)