Reviewed, UniProtKB/Swiss-Prot Q16772 (GSTA3_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase A3
    EC=2.5.1.18
Alternative name(s):
    Glutathione S-transferase A3-3
    GST class-alpha member 3

Gene names

Name:

GSTA3

Organism

Homo sapiens (Human) [Complete 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	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione transferase activity Ref.5 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Glutathione S-transferase A3

PRO_0000185785

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 207

123

GST C-terminal

Natural variations

Natural variant

71

1

I → L: dbSNP rs1052661. Ref.5

VAR_049484

Natural variant

73

1

N → D: dbSNP rs41273858.

VAR_049485

Experimental info

Sequence conflict

63

1

M → I in AAH20619. Ref.4

Sequence conflict

113 – 114

2

RP → PA in AAA74634. Ref.1

Sequence conflict

128

1

T → I in AAA74634. Ref.1

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Turn

14 – 16

3

Helix

17 – 25

9

Beta strand

31 – 34

4

Helix

38 – 46

9

Beta strand

57 – 60

4

Beta strand

63 – 67

5

Helix

68 – 78

11

Helix

86 – 108

23

Helix

109 – 111

3

Helix

114 – 130

17

Helix

132 – 143

12

Beta strand

146 – 149

4

Helix

155 – 170

16

Turn

172 – 177

6

Helix

179 – 189

11

Helix

192 – 198

7

Helix

210 – 220

11

Sequences

	Sequence		Length	Mass (Da)
	Q16772-1 [UniParc]. Last modified May 27, 2002. Version 3. Checksum: 904AA17519B5343C	FASTA	222	25,302
	10 20 30 40 50 60 MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI 70 80 90 100 110 120 DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK 130 140 150 160 170 180 IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL 190 200 210 220 LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes." Suzuki T., Johnston P.N., Board P.G. Genomics 18:680-686(1993) [PubMed: 8307579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones." Johansson A.-S., Mannervik B. J. Biol. Chem. 276:33061-33065(2001) [PubMed: 11418619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	"Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4." Board P.G. Biochem. J. 330:827-831(1998) [PubMed: 9480897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-222, VARIANT LEU-71.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L13275 , L13270, L13271, L13272, L13273, L13274 Genomic DNA. Translation: AAA74634.1. Different initiation.
AF508266 mRNA. Translation: AAM33360.1.
AL121969 Genomic DNA. Translation: CAC10389.1.
BC020619 mRNA. Translation: AAH20619.1.
AF020919 mRNA. Translation: AAD04712.1. Different initiation.

IPI

IPI00003929.

PIR

A49365.

RefSeq

NP_000838.3.

UniGene

Hs.102484

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TDI	X-ray	2.40	A/B	1-222	[»]
2VCV	X-ray	1.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	1-222	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q16772.

Genome annotation databases

Ensembl

ENSG00000174156. Homo sapiens. [Contig view]

GeneID

2940.

KEGG

hsa:2940.

UCSC

uc003pbb.1. human.

Organism-specific databases

GeneCards

GC06M052869.

H-InvDB

HIX0005957.

HGNC

HGNC:4628. GSTA3.

HPA

HPA004342.

MIM

605449. gene.

PharmGKB

PA29018.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q16772.

HOVERGEN

Q16772.

OMA

Q16772. QSHGQDY.

Enzyme and pathway databases

BRENDA

2.5.1.18. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

Q16772.

Bgee

Q16772.

CleanEx

HS_GSTA3.

GermOnline

ENSG00000174156. Homo sapiens.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11571:SF4. GST_alpha. 1 hit.

Pfam

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

PRINTS

PR01266. GSTRNSFRASEA.

PROSITE

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

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

11651.

SOURCE

Search...

Entry information

Entry name

GSTA3_HUMAN

Accession

Primary (citable) accession number: Q16772
Secondary accession number(s): O43468, Q8WWA8, Q9H415

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 27, 2002
Last modified:	July 7, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)