Glutathione S-transferase Mu 3 - Homo sapiens (Human)

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P21266 (GSTM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 150. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutathione S-transferase Mu 3
EC=2.5.1.18

Alternative name(s):
GST class-mu 3
GSTM3-3
Short name=hGSTM3-3

Gene names

Name:	GSTM3
Synonyms:	GST5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers. Ref.8
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.8
Subunit structure	Homodimer. Ref.8
Subcellular location	Cytoplasm.
Tissue specificity	Testis and brain.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Biophysicochemical properties	Kinetic parameters: K_M=1.1 mM for 1-chloro-2,4-dinitrobenzene Ref.8 K_M=0.084 mM for glutathione

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular detoxification of nitrogen compound Inferred from direct assay Ref.5. Source: BHF-UCL establishment of blood-nerve barrier Traceable author statement Ref.1. Source: ProtInc glutathione metabolic process Inferred from direct assay Ref.8. Source: UniProtKB nitrobenzene metabolic process Inferred from direct assay Ref.5. Source: BHF-UCL response to estrogen stimulus Inferred from expression pattern PubMed 10037815. Source: UniProtKB xenobiotic catabolic process Inferred from direct assay Ref.5. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: BHF-UCL
Molecular_function	glutathione binding Inferred from direct assay Ref.5. Source: BHF-UCL glutathione transferase activity Inferred from direct assay Ref.8. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 9545290. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-350350,EBI-350350

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 225

225

Glutathione S-transferase Mu 3

PRO_0000185822

Regions

Domain

5 – 92

GST N-terminal

Domain

94 – 212

119

GST C-terminal

Region

11 – 12

Glutathione binding By similarity

Region

50 – 54

Glutathione binding By similarity

Region

63 – 64

Glutathione binding By similarity

Region

76 – 77

Glutathione binding By similarity

Sites

Binding site

120

Substrate By similarity

Natural variations

Natural variant

224

V → I. Ref.4
Corresponds to variant rs7483 [ dbSNP | Ensembl ].

VAR_014498

Experimental info

Mutagenesis

120

Y → A: No effect. Ref.8

Mutagenesis

120

Y → F: Strongly increased catalytic activity. Ref.8

Mutagenesis

213

N → F: Strongly increased catalytic activity. Ref.8

Mutagenesis

213

N → G: No effect. Ref.8

Sequence conflict

147

G → W in AAA60964. Ref.1

Secondary structure

225

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P21266 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 79093161ECEF5396
Show »

FASTA

225

26,560

        10         20         30         40         50         60 
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD 

        70         80         90        100        110        120 
FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY 

       130        140        150        160        170        180 
SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD 

       190        200        210        220 
EFPNLKAFMC RFEALEKIAA YLQSDQFCKM PINNKMAQWG NKPVC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes." Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I. J. Biol. Chem. 265:9188-9193(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain and Testis.
[2]	"Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster." Patskovsky Y.V., Huang M.Q., Takayama T., Listowsky I., Pearson W.R. Arch. Biochem. Biophys. 361:85-93(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-224. Tissue: Brain and Uterus.
[5]	"Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript." Ross V.L., Board P.G. Biochem. J. 294:373-380(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS. Tissue: Testis.
[6]	"Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue." Hussey A.J., Hayes J.D. Biochim. Biophys. Acta 1203:131-141(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 190-209.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases." Patskovsky Y.V., Patskovska L.N., Listowsky I. Biochemistry 38:16187-16194(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TYR-120 AND ASN-213.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05459 mRNA. Translation: AAA60964.1.
AF043105 Genomic DNA. Translation: AAC17866.1.
BT019945 mRNA. Translation: AAV38748.1.
BC000088 mRNA. Translation: AAH00088.1.
BC008790 mRNA. Translation: AAH08790.1.

IPI

IPI00246975.

PIR

A35295.

RefSeq

NP_000840.2. NM_000849.4.

UniGene

Hs.2006.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GTU	X-ray	2.80	B/D	2-225	[»]

ProteinModelPortal

P21266.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21266. 2 interactions.

STRING

9606.ENSP00000256594.

PTM databases

PhosphoSite

P21266.

Polymorphism databases

DMDM

21264423.

2D gel databases

OGP

P21266.

REPRODUCTION-2DPAGE

IPI00246975.

Proteomic databases

PaxDb

P21266.

PeptideAtlas

P21266.

PRIDE

P21266.

Protocols and materials databases

DNASU

2947.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256594; ENSP00000256594; ENSG00000134202.
ENST00000361066; ENSP00000354357; ENSG00000134202.
ENST00000540225; ENSP00000444978; ENSG00000134202.

GeneID

2947.

KEGG

hsa:2947.

UCSC

uc001dyo.2. human.

Organism-specific databases

CTD

2947.

GeneCards

GC01M110276.

HGNC

HGNC:4635. GSTM3.

HPA

CAB017130.
CAB040583.
HPA035190.

MIM

138390. gene.

neXtProt

NX_P21266.

PharmGKB

PA29024.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300089.

HOVERGEN

HBG106842.

InParanoid

P21266.

K00799.

OMA

MSCESSM.

OrthoDB

EOG47D9H2.

PhylomeDB

P21266.

Gene expression databases

ArrayExpress

P21266.

Bgee

P21266.

CleanEx

HS_GSTM3.

Genevestigator

P21266.

GermOnline

ENSG00000134202. Homo sapiens.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01267. GSTRNSFRASEM.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2242.

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

P21266.

GenomeRNAi

2947.

NextBio

11678.

SOURCE

Search...

Entry information

Entry name

GSTM3_HUMAN

Accession

Primary (citable) accession number: P21266
Secondary accession number(s): O60550, Q96HA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 150 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents