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Protein

Metallothionein

Gene

mt

Organism
Gobiomorphus cotidianus (New Zealand common bully)
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

Keywordsi

LigandMetal-binding, Metal-thiolate cluster

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein
Short name:
MT
Gene namesi
Name:mt
OrganismiGobiomorphus cotidianus (New Zealand common bully)
Taxonomic identifieri226931 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataGobiariaGobiiformesEleotroideiEleotridaeEleotrinaeGobiomorphus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001972851 – 60MetallothioneinAdd BLAST60

Structurei

3D structure databases

ProteinModelPortaliQ800D3.
SMRiQ800D3.
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

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR003019. Metalthion.
IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
PANTHERiPTHR23299. PTHR23299. 1 hit.
PfamiView protein in Pfam
PF00131. Metallothio. 1 hit.
PRINTSiPR00860. MTVERTEBRATE.
SUPFAMiSSF57868. SSF57868. 1 hit.
PROSITEiView protein in PROSITE
PS00203. METALLOTHIONEIN_VRT. 1 hit.

Sequencei

Sequence statusi: Complete.

Q800D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPCECSKTG NCTCGGSCTC KNCSCTSCKK SCCSCCPSGC SKCASGCVCK
60
GKTCDTSCCQ
Length:60
Mass (Da):6,009
Last modified:June 1, 2003 - v1
Checksum:i360ECE267E8C4714
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY239389 mRNA. Translation: AAO89258.1.

Similar proteinsi

Entry informationi

Entry nameiMT_GOBCO
AccessioniPrimary (citable) accession number: Q800D3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2003
Last modified: May 10, 2017
This is version 47 of the entry and version 1 of the sequence. See 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