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GSTP2_MOUSE
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   03-AUG-2022, entry version 158.
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; P46425; -.
DR   PeptideAtlas; P46425; -.
DR   PRIDE; P46425; -.
DR   ProteomicsDB; 271480; -.
DR   TopDownProteomics; P46425; -.
DR   DNASU; 14869; -.
DR   Ensembl; ENSMUST00000042700; ENSMUSP00000038931; ENSMUSG00000038155.
DR   GeneID; 14869; -.
DR   KEGG; mmu:14869; -.
DR   UCSC; uc008fyg.1; mouse.
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; EETRENH; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; P46425; -.
DR   TreeFam; TF105321; -.
DR   BioGRID-ORCS; 14869; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Gstp2; mouse.
DR   PRO; PR:P46425; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P46425; protein.
DR   Bgee; ENSMUSG00000038155; Expressed in duodenum and 72 other tissues.
DR   ExpressionAtlas; P46425; baseline and differential.
DR   Genevisible; P46425; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; 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:0043508; P:negative regulation of JUN kinase activity; ISO:MGI.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; 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:0006469; P:negative regulation of protein kinase activity; 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   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   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01268; GSTRNSFRASEP.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 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
 
 
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