P00502

PR
Gene name
Gsta1
Protein name
Glutathione S-transferase alpha-1
Names
13-hydroperoxyoctadecadienoate peroxidase, Androst-5-ene-3,17-dione isomerase, GST 1-1, GST 1a-1a, GST A1-1, GST B, Glutathione S-transferase Ya-1, GST Ya1, Ligandin
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:24422
EC number
2.5.1.18: Transferring alkyl or aryl groups, other than methyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

158-222 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for P00502

Entry ID Method Resolution Chain Position Source
1EV4 X-ray 220 A A/C/D 2-222 PDB
1EV9 X-ray 220 A A/C/D 2-222 PDB
AF-P00502-F1 Predicted AlphaFoldDB

No variants for P00502

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P00502

No associated diseases with P00502

3 regional properties for P00502

Type Name Position InterPro Accession
domain Glutathione S-transferase, N-terminal 3 - 83 IPR004045
domain Glutathione S-transferase, C-terminal 101 - 199 IPR004046
domain Glutathione S-transferase, C-terminal-like 85 - 208 IPR010987

Functions

Description
EC Number 2.5.1.18 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
organelle membrane A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle.

7 GO annotations of molecular function

Name Definition
dinitrosyl-iron complex binding Binding to a dinitrosyl-iron complex. Nitric oxide (NO) is stored as dinitrosyl-iron complexes, which form spontaneously from Glutathione (GSH), S-nitrosoglutathione, and trace amounts of ferrous ions, or by reaction of iron-sulfur centers with NO.
fatty acid binding Binding to a fatty acid, an aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
glutathione binding Binding to glutathione; a tripeptide composed of the three amino acids cysteine, glutamic acid and glycine.
glutathione peroxidase activity Catalysis of the reaction: 2 glutathione + hydrogen peroxide = oxidized glutathione + 2 H2O.
glutathione transferase activity Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group.
protein homodimerization activity Binding to an identical protein to form a homodimer.
steroid delta-isomerase activity Catalysis of the reaction: a 3-oxo-delta(5)-steroid = a 3-oxo-delta(4)-steroid.

10 GO annotations of biological process

Name Definition
aging A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
epithelial cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium.
glutathione derivative biosynthetic process The chemical reactions and pathways resulting in the formation of glutathione derivative.
glutathione metabolic process The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.
linoleic acid metabolic process The chemical reactions and pathways involving linoleic acid, an unsaturated omega-6 fatty acid that has the molecular formula C18H32O2.
prostaglandin metabolic process The chemical reactions and pathways involving prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities.
response to nutrient levels Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients.
response to xenobiotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
xenobiotic catabolic process The chemical reactions and pathways resulting in the breakdown of a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
xenobiotic metabolic process The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI
70 80 90 100 110 120
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK
130 140 150 160 170 180
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL
190 200 210 220
LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF