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Protein

Metallothionein

Gene

mt

Organism
Barbatula barbatula (Stone loach) (Noemacheilus barbatulus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Metallothioneins have a high content of cysteine residues that bind various heavy metals.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi4Divalent metal cation; cluster B1
Metal bindingi6Divalent metal cation; cluster B1
Metal bindingi12Divalent metal cation; cluster B1
Metal bindingi14Divalent metal cation; cluster B1
Metal bindingi18Divalent metal cation; cluster B1
Metal bindingi20Divalent metal cation; cluster B1
Metal bindingi23Divalent metal cation; cluster B1
Metal bindingi25Divalent metal cation; cluster B1
Metal bindingi28Divalent metal cation; cluster B1
Metal bindingi32Divalent metal cation; cluster A1
Metal bindingi33Divalent metal cation; cluster A1
Metal bindingi35Divalent metal cation; cluster A1
Metal bindingi36Divalent metal cation; cluster A1
Metal bindingi40Divalent metal cation; cluster A1
Metal bindingi43Divalent metal cation; cluster A1
Metal bindingi47Divalent metal cation; cluster A1
Metal bindingi49Divalent metal cation; cluster A1
Metal bindingi54Divalent metal cation; cluster A1
Metal bindingi58Divalent metal cation; cluster A1
Metal bindingi59Divalent metal cation; cluster A1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Metal-thiolate cluster

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein
Short name:
MT
Gene namesi
Name:mt
OrganismiBarbatula barbatula (Stone loach) (Noemacheilus barbatulus)
Taxonomic identifieri135647 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesNemacheilidaeBarbatula

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001972921 – 60MetallothioneinAdd BLAST60

Structurei

3D structure databases

ProteinModelPortaliP25128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 28BetaAdd BLAST28
Regioni29 – 60AlphaAdd BLAST32

Domaini

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 similaritiesi

Phylogenomic databases

HOVERGENiHBG009063.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR003019. Metalthion.
IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERiPTHR23299. PTHR23299. 1 hit.
PfamiPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSiPR00860. MTVERTEBRATE.
SUPFAMiSSF57868. SSF57868. 1 hit.
PROSITEiPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPCDCSKTG TCNCGATCKC TNCQCTTCKK SCCSCCPSGC SKCASGCVCK
60
GNSCDSSCCQ
Length:60
Mass (Da):6,036
Last modified:February 1, 1996 - v2
Checksum:i462A8F7D37968701
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59393 mRNA. Translation: CAA42036.1.
X70043 Genomic DNA. Translation: CAA49637.1. Sequence problems.
PIRiS38335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59393 mRNA. Translation: CAA42036.1.
X70043 Genomic DNA. Translation: CAA49637.1. Sequence problems.
PIRiS38335.

3D structure databases

ProteinModelPortaliP25128.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG009063.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR003019. Metalthion.
IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERiPTHR23299. PTHR23299. 1 hit.
PfamiPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSiPR00860. MTVERTEBRATE.
SUPFAMiSSF57868. SSF57868. 1 hit.
PROSITEiPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMT_BARBB
AccessioniPrimary (citable) accession number: P25128
Secondary accession number(s): Q91127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: October 5, 2016
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Metallothioneins
    Classification of metallothioneins and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.