Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi4 – 41Divalent metal cation; cluster B
Metal bindingi6 – 61Divalent metal cation; cluster B
Metal bindingi12 – 121Divalent metal cation; cluster B
Metal bindingi14 – 141Divalent metal cation; cluster B
Metal bindingi18 – 181Divalent metal cation; cluster B
Metal bindingi20 – 201Divalent metal cation; cluster B
Metal bindingi23 – 231Divalent metal cation; cluster B
Metal bindingi25 – 251Divalent metal cation; cluster B
Metal bindingi28 – 281Divalent metal cation; cluster B
Metal bindingi32 – 321Divalent metal cation; cluster A
Metal bindingi33 – 331Divalent metal cation; cluster A
Metal bindingi35 – 351Divalent metal cation; cluster A
Metal bindingi36 – 361Divalent metal cation; cluster A
Metal bindingi40 – 401Divalent metal cation; cluster A
Metal bindingi43 – 431Divalent metal cation; cluster A
Metal bindingi47 – 471Divalent metal cation; cluster A
Metal bindingi49 – 491Divalent metal cation; cluster A
Metal bindingi54 – 541Divalent metal cation; cluster A
Metal bindingi58 – 581Divalent metal cation; cluster A
Metal bindingi59 – 591Divalent metal cation; cluster A

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6060MetallothioneinPRO_0000197292Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP25128.
SMRiP25128. Positions 2-29, 31-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2828BetaAdd
BLAST
Regioni29 – 6032AlphaAdd
BLAST

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.
InterProiIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
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.
SMRiP25128. Positions 2-29, 31-60.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG009063.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
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...

Publicationsi

  1. "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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Analysis of regulatory elements flanking metallothionein genes in Cd-tolerant fish (pike and stone loach)."
    Kille P., Kay J., Sweeney G.E.
    Biochim. Biophys. Acta 1216:55-64(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Kidney.

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 1, 2014
This is version 69 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

External Data

Dasty 3

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 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.