ID GSTP2_MOUSE Reviewed; 210 AA.
AC P46425; Q505C3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Glutathione S-transferase P 2;
DE Short=Gst P2;
DE EC=2.5.1.18;
DE AltName: Full=GST YF-YF;
DE AltName: Full=GST class-pi;
DE AltName: Full=GST-piA;
GN Name=Gstp2; Synonyms=Gstpia;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8135745; DOI=10.1042/bj2980385;
RA Bammler T.K., Smith C.A.D., Wolf R.C.;
RT "Isolation and characterization of two mouse PI class glutathione S-
RT transferase genes.";
RL Biochem. J. 298:385-390(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=7982937; DOI=10.1016/s0021-9258(18)43807-0;
RA Xu X., Stambrook P.J.;
RT "Two murine GSTpi genes are arranged in tandem and are differentially
RT expressed.";
RL J. Biol. Chem. 269:30268-30273(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Cannot metabolize
CC 1-chloro-2,4-dinitrobenzene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Selectively expressed in gall bladder, colon,
CC heart, and skeletal muscle.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR EMBL; X76144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U15654; AAA64836.1; -; Genomic_DNA.
DR EMBL; BC064781; AAH64781.1; -; mRNA.
DR EMBL; BC094623; AAH94623.1; -; mRNA.
DR CCDS; CCDS29412.1; -.
DR PIR; A55140; A55140.
DR RefSeq; NP_861461.1; NM_181796.2.
DR AlphaFoldDB; P46425; -.
DR SMR; P46425; -.
DR BioGRID; 200100; 2.
DR IntAct; P46425; 1.
DR STRING; 10090.ENSMUSP00000038931; -.
DR iPTMnet; P46425; -.
DR PhosphoSitePlus; P46425; -.
DR SwissPalm; P46425; -.
DR jPOST; P46425; -.
DR MaxQB; P46425; -.
DR PaxDb; 10090-ENSMUSP00000038931; -.
DR PeptideAtlas; P46425; -.
DR ProteomicsDB; 271480; -.
DR Pumba; P46425; -.
DR TopDownProteomics; P46425; -.
DR DNASU; 14869; -.
DR Ensembl; ENSMUST00000042700.12; ENSMUSP00000038931.10; ENSMUSG00000038155.12.
DR GeneID; 14869; -.
DR KEGG; mmu:14869; -.
DR UCSC; uc008fyg.1; mouse.
DR AGR; MGI:95864; -.
DR CTD; 14869; -.
DR MGI; MGI:95864; Gstp2.
DR VEuPathDB; HostDB:ENSMUSG00000038155; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000162460; -.
DR HOGENOM; CLU_039475_2_1_1; -.
DR InParanoid; P46425; -.
DR OMA; YWHTIRN; -.
DR OrthoDB; 5302341at2759; -.
DR PhylomeDB; P46425; -.
DR TreeFam; TF105321; -.
DR BioGRID-ORCS; 14869; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Gstp2; mouse.
DR PRO; PR:P46425; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P46425; Protein.
DR Bgee; ENSMUSG00000038155; Expressed in embryonic cell in blastocyst and 74 other cell types or tissues.
DR ExpressionAtlas; P46425; baseline and differential.
DR Genevisible; P46425; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0097057; C:TRAF2-GSTP1 complex; ISO:MGI.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0035730; F:S-nitrosoglutathione binding; ISO:MGI.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISO:MGI.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR GO; GO:0009890; P:negative regulation of biosynthetic process; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
DR CDD; cd03210; GST_C_Pi; 1.
DR CDD; cd03076; GST_N_Pi; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF266; GLUTATHIONE S-TRANSFERASE P 1-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Glutathione S-transferase P 2"
FT /id="PRO_0000185904"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT DOMAIN 83..204
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
SQ SEQUENCE 210 AA; 23537 MW; 48423B9F236C8A36 CRC64;
MPPYTIVYFP SPGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD
LTLYQSNAIL RHLGRSLGLY GKNQREAAQV DMVNDGVEDL RGKYGTMIYR NYENGKNDYV
KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY
VARLSARPKI KAFLSSPEHV NRPINGNGKQ
//
