Metallothionein B - Oncorhynchus mykiss (Rainbow trout)

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P68501 (MTB_ONCMY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 33. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Metallothionein B
Short name=MT-B

Gene names

Name:

mtb

Organism

Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	60 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Metallothioneins have a high content of cysteine residues that bind various heavy metals 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
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

60

Metallothionein B

PRO_0000197296

Regions

Region

28

Beta

Region

32

Alpha

Sites

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster B

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Metal binding

1

Divalent metal cation; cluster A

Sequences

Sequence

Length

Mass (Da)

Tools

P68501 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9EA1E70FBE59B4EE
Show »

60

6,033

        10         20         30         40         50         60 
MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCPCCPSDC SKCASGCVCK GKTCDTSCCQ

References

[1]	"The rainbow trout metallothioneins: molecular cloning and characterization of two distinct cDNA sequences." Bonham K., Zafarullah M., Gedamu L. DNA 6:519-528(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the rainbow trout metallothionein B gene and characterization of its metal-responsive region." Zafarullah M., Bonham K., Gedamu L. Mol. Cell. Biol. 8:4469-4476(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Elucidation of cDNA sequences for metallothioneins from rainbow trout, stone loach and pike liver using the polymerase chain reaction." Kille P., Stephens P.E., Kay J. Biochim. Biophys. Acta 1089:407-410(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M18104 mRNA. Translation: AAA49566.1. M22487 Genomic DNA. Translation: AAA49567.1. X59394 mRNA. Translation: CAA42037.1.
PIR	B27490. A30818.
UniGene	Omy.11783.
3D structure databases
ProteinModelPortal	P68501.
SMR	P68501. Positions 2-29, 31-60.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG096123.
Family and domain databases
Gene3D	4.10.10.10. 1 hit.
InterPro	IPR017854. Metalthion_dom. IPR023587. Metalthion_dom_vert. IPR003019. Metalthion_sfam_euk. IPR000006. Metalthion_vert. IPR018064. Metalthion_vert_metal_BS. [Graphical view]
PANTHER	PTHR23299. PTHR23299. 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...

Entry information

Entry name

MTB_ONCMY

Accession

Primary (citable) accession number: P68501
Secondary accession number(s): P09862

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 23, 2004
Last modified:	April 3, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Metallothioneins

Classification of metallothioneins and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents