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Protein

Metallothionein-1

Gene
N/A
Organism
Homarus americanus (American lobster)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Metallothioneins have a high content of cysteine residues that bind various heavy metals. The different forms of lobster metallothioneins may have different biological functions. Class I MTS in marine crustacea are involved in the sequestration of elevated levels of heavy-metal ions. Binds 6 metal ions. Known to bind cadmium.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi4Divalent metal cation; cluster B1
Metal bindingi5Divalent metal cation; cluster B1
Metal bindingi9Divalent metal cation; cluster B1
Metal bindingi11Divalent metal cation; cluster B1
Metal bindingi16Divalent metal cation; cluster B1
Metal bindingi20Divalent metal cation; cluster B1
Metal bindingi22Divalent metal cation; cluster B1
Metal bindingi25Divalent metal cation; cluster B1
Metal bindingi27Divalent metal cation; cluster B1
Metal bindingi30Divalent metal cation; cluster A1
Metal bindingi33Divalent metal cation; cluster A1
Metal bindingi37Divalent metal cation; cluster A1
Metal bindingi39Divalent metal cation; cluster A1
Metal bindingi45Divalent metal cation; cluster A1
Metal bindingi49Divalent metal cation; cluster A1
Metal bindingi53Divalent metal cation; cluster A1
Metal bindingi55Divalent metal cation; cluster A1
Metal bindingi56Divalent metal cation; cluster A1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Cadmium, Copper, Metal-binding, Metal-thiolate cluster

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein-1
Alternative name(s):
CuMT-1
OrganismiHomarus americanus (American lobster)
Taxonomic identifieri6706 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaNephropoideaNephropidaeHomarus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001973421 – 58Metallothionein-1Add BLAST58

Structurei

Secondary structure

158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi11 – 14Combined sources4
Helixi31 – 33Combined sources3
Helixi45 – 48Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J5LNMR-A29-56[»]
1J5MNMR-A1-28[»]
ProteinModelPortaliP29499.
SMRiP29499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29499.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 28BetaAdd BLAST28
Regioni29 – 58AlphaAdd BLAST30

Sequence similaritiesi

Family and domain databases

InterProiIPR002045. Metalthion_crustacean.
IPR017854. Metalthion_dom.
[Graphical view]
PRINTSiPR00858. MTCRUSTACEAN.
SUPFAMiSSF57868. SSF57868. 2 hits.

Sequencei

Sequence statusi: Complete.

P29499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PGPCCKDKCE CAEGGCKTGC KCTSCRCAPC EKCTSGCKCP SKDECAKTCS

KPCSCCXX
Length:58
Mass (Da):5,977
Last modified:November 1, 1997 - v2
Checksum:i176ABAAF60A32F96
GO

Sequence databases

PIRiA37039.

Cross-referencesi

Sequence databases

PIRiA37039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J5LNMR-A29-56[»]
1J5MNMR-A1-28[»]
ProteinModelPortaliP29499.
SMRiP29499.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP29499.

Family and domain databases

InterProiIPR002045. Metalthion_crustacean.
IPR017854. Metalthion_dom.
[Graphical view]
PRINTSiPR00858. MTCRUSTACEAN.
SUPFAMiSSF57868. SSF57868. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiMT1_HOMAM
AccessioniPrimary (citable) accession number: P29499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Metallothioneins
    Classification of metallothioneins and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.