CPLM-000209

Genbank Nucleotide ID

Glutathione S-transferase omega-1

Protein Synonyms/Alias

GSTO-1; Glutathione S-transferase omega 1-1; GSTO 1-1; Glutathione-dependent dehydroascorbate reductase; Monomethylarsonic acid reductase; MMA(V) reductase; S-(Phenacyl)glutathione reductase; SPG-R; p28

Mus musculus (Mouse)

Position	Peptide	Type	References
11	ESSRSLGKGSAPPGP	ubiquitination	[1]
43	QRTLMVLKAKGIRHE	acetylation	[2]
57	EVININLKNKPEWFF	acetylation	[2]
101	DEAYPEKKLFPDDPY	ubiquitination	[1]
109	LFPDDPYKKARQKMT	acetylation	[3]
122	MTLESFSKVPPLIAS	ubiquitination	[1]
152	ALENEFKKLEEGMDN	ubiquitination	[1]
189	RLEALELKECLAHTP	acetylation	[2, 3, 4]
189	RLEALELKECLAHTP	ubiquitination	[1]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]

Functional Description

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid (By similarity).

DOMAIN 22 101 GST N-terminal.
DOMAIN 106 227 GST C-terminal.
REGION 85 86 Glutathione binding (By similarity).
ACT_SITE 32 32 Nucleophile (By similarity).
BINDING 59 59 Glutathione (By similarity).
BINDING 72 72 Glutathione; via amide nitrogen and
MOD_RES 2 2 N-acetylserine (By similarity).
MOD_RES 57 57 N6-acetyllysine (By similarity).
MOD_RES 152 152 N6-acetyllysine (By similarity).

Acetylation; Complete proteome; Cytoplasm; Oxidoreductase; Reference proteome; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
GO:0050610; F:methylarsonate reductase activity; IEA:EC.
GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Compara.
GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IEA:Compara.
GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Compara.
GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.

IPR010987; Glutathione-S-Trfase_C-like.
IPR004045; Glutathione_S-Trfase_N.
IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
IPR004046; GST_C.
IPR005442; GST_omega.
IPR012336; Thioredoxin-like_fold.

PS50405; GST_CTER
PS50404; GST_NTER

PR01625; GSTRNSFRASEO.