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Protein

Metallothionein

Gene
N/A
Organism
Arianta arbustorum (Land snail)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The metallothioneins are involved in the cellular sequestration of toxic metal ions and regulation of essential trace elements.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Sequence analysis1
Metal bindingi13Sequence analysis1
Metal bindingi18Sequence analysis1
Metal bindingi20Sequence analysis1
Metal bindingi24Sequence analysis1
Metal bindingi26Sequence analysis1
Metal bindingi30Sequence analysis1
Metal bindingi32Sequence analysis1
Metal bindingi35Sequence analysis1
Metal bindingi38Sequence analysis1
Metal bindingi40Sequence analysis1
Metal bindingi45Sequence analysis1
Metal bindingi47Sequence analysis1
Metal bindingi51Sequence analysis1
Metal bindingi57Sequence analysis1
Metal bindingi59Sequence analysis1
Metal bindingi63Sequence analysis1
Metal bindingi65Sequence analysis1

GO - Molecular functioni

Keywordsi

LigandCadmium, Metal-binding, Metal-thiolate cluster

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein
Short name:
MT
OrganismiArianta arbustorum (Land snail)
Taxonomic identifieri45985 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataEupulmonataStylommatophoraSigmurethraHelicoideaHelicidaeArianta

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001973351 – 66MetallothioneinAdd BLAST66

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Expressioni

Inductioni

By cadmium.

Structurei

3D structure databases

SMRiP55946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

14 cysteine residues are arranged in C-X-C groups. These are thought to be the metal-binding sites in other metallothioneins.

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR001008. Metalthion_mollusc.
PRINTSiPR00875. MTMOLLUSC.

Sequencei

Sequence statusi: Complete.

P55946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SGKGKGDLCT AACKNEPCQC GSKCQCGEGC ACASCKTCNC TSDGCKCGKE
60
CTGAASCKCN SSCSCK
Length:66
Mass (Da):6,495
Last modified:November 1, 1997 - v1
Checksum:i6CB977276CAC23D5
GO

Polymorphismi

The sequence shown is that of variant A (MTA); variant B (MTB) differs in a single position.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti60N → G in MTB. 1 Publication1

Sequence databases

PIRiS59621.
S59622.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMT_ARIAR
AccessioniPrimary (citable) accession number: P55946
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 10, 2017
This is version 46 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

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