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Protein

Copper-metallothionein

Gene
N/A
Organism
Helix pomatia (Roman snail) (Edible 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. This isoform binds exclusively copper.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi7Copper1
Metal bindingi11Copper1
Metal bindingi16Copper1
Metal bindingi18Copper1
Metal bindingi22Copper1
Metal bindingi24Copper1
Metal bindingi28Copper1
Metal bindingi30Copper1
Metal bindingi33Copper1
Metal bindingi36Copper1
Metal bindingi38Copper1
Metal bindingi43Copper1
Metal bindingi45Copper1
Metal bindingi49Copper1
Metal bindingi55Copper1
Metal bindingi57Copper1
Metal bindingi61Copper1
Metal bindingi63Copper1

GO - Molecular functioni

Keywordsi

LigandCopper, Metal-binding, Metal-thiolate cluster

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-metallothionein
Alternative name(s):
Cu-MT
OrganismiHelix pomatia (Roman snail) (Edible snail)
Taxonomic identifieri6536 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataEupulmonataStylommatophoraSigmurethraHelicoideaHelicidaeHelix

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001973381 – 64Copper-metallothioneinAdd BLAST64

Amino acid modifications

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

Keywords - PTMi

Acetylation

PTM databases

iPTMnetiP55947.

Structurei

3D structure databases

SMRiP55947.
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.

P55947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SGRGKNCGGA CNSNPCSCGN DCKCGAGCNC DRCSSCHCSN DDCKCGSQCT
60
GSGSCKCGSA CGCK
Length:64
Mass (Da):6,205
Last modified:November 1, 1997 - v1
Checksum:i96CC1998B7E12297
GO

Similar proteinsi

Entry informationi

Entry nameiMTCU_HELPO
AccessioniPrimary (citable) accession number: P55947
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 25, 2017
This is version 45 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