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Protein

Glutathione S-transferase 8.2

Gene
N/A
Organism
Dicentrarchus labrax (European seabass) (Morone labrax)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 8.2 (EC:2.5.1.18)
Short name:
GST-8.2
Alternative name(s):
GST class-alpha
OrganismiDicentrarchus labrax (European seabass) (Morone labrax)
Taxonomic identifieri13489 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaMoronidaeDicentrarchus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›32›32Glutathione S-transferase 8.2PRO_0000185804Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Subunit structurei

Homodimer.

Family & Domainsi

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated

Sequencei

Sequence statusi: Fragments.

P82608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
MESIRWLLTV AQFDFDMKLV QSXAIVNYVA NK
Length:32
Mass (Da):3,743
Last modified:October 1, 2000 - v1
Checksum:i806C6F142ED3C3EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi16 – 172Curated
Non-terminal residuei32 – 321

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Purification and characterization of glutathione transferases from the sea bass (Dicentrarchus labrax) liver."
    Angelucci S., Sacchetta P., Moio P., Melino S., Petruzzelli R., Gervasi P., Di Ilio C.
    Arch. Biochem. Biophys. 373:435-441(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiGST82_DICLA
AccessioniPrimary (citable) accession number: P82608
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.