GSTM5_MOUSE
ID GSTM5_MOUSE Reviewed; 224 AA.
AC P48774; Q545W5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Glutathione S-transferase Mu 5;
DE EC=2.5.1.18;
DE AltName: Full=Fibrous sheath component 2;
DE Short=Fsc2;
DE AltName: Full=GST class-mu 5;
GN Name=Gstm5; Synonyms=Fsc2, Gstm3;
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 [MRNA].
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=8607970; DOI=10.1002/mrd.1080420407;
RA Fulcher K.D., Welch J.E., Klapper D.G., O'Brien D.A., Eddy E.M.;
RT "Identification of a unique mu-class glutathione S-transferase in mouse
RT spermatogenic cells.";
RL Mol. Reprod. Dev. 42:415-424(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Kidney, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 22-34; 54-70; 71-81; 156-171 AND 197-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH PFKM.
RX PubMed=19889946; DOI=10.1095/biolreprod.109.080580;
RA Nakamura N., Mori C., Eddy E.M.;
RT "Molecular complex of three testis-specific isozymes associated with the
RT mouse sperm fibrous sheath: hexokinase 1, phosphofructokinase M, and
RT glutathione S-transferase mu class 5.";
RL Biol. Reprod. 82:504-515(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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.
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 (By similarity). Interacts with PFKM isoform 2 and
CC isoform 3 (via N-terminal testis-specific region) (PubMed:19889946).
CC {ECO:0000250, ECO:0000269|PubMed:19889946}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; U24428; AAB04096.1; -; mRNA.
DR EMBL; AK002750; BAB22327.1; -; mRNA.
DR EMBL; AK019317; BAB31661.1; -; mRNA.
DR EMBL; AK028098; BAC25746.1; -; mRNA.
DR EMBL; BC008206; AAH08206.1; -; mRNA.
DR CCDS; CCDS17741.1; -.
DR RefSeq; NP_034490.1; NM_010360.2.
DR AlphaFoldDB; P48774; -.
DR SMR; P48774; -.
DR BioGRID; 200098; 5.
DR IntAct; P48774; 4.
DR MINT; P48774; -.
DR STRING; 10090.ENSMUSP00000004134; -.
DR iPTMnet; P48774; -.
DR PhosphoSitePlus; P48774; -.
DR SwissPalm; P48774; -.
DR EPD; P48774; -.
DR jPOST; P48774; -.
DR MaxQB; P48774; -.
DR PaxDb; P48774; -.
DR PeptideAtlas; P48774; -.
DR PRIDE; P48774; -.
DR ProteomicsDB; 271343; -.
DR Antibodypedia; 33773; 218 antibodies from 32 providers.
DR DNASU; 14866; -.
DR Ensembl; ENSMUST00000004134; ENSMUSP00000004134; ENSMUSG00000004032.
DR GeneID; 14866; -.
DR KEGG; mmu:14866; -.
DR UCSC; uc008qxs.1; mouse.
DR CTD; 2949; -.
DR MGI; MGI:1309466; Gstm5.
DR VEuPathDB; HostDB:ENSMUSG00000004032; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000157663; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; P48774; -.
DR OMA; DIMENQV; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P48774; -.
DR TreeFam; TF353040; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR SABIO-RK; P48774; -.
DR BioGRID-ORCS; 14866; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Gstm5; mouse.
DR PRO; PR:P48774; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P48774; protein.
DR Bgee; ENSMUSG00000004032; Expressed in seminiferous tubule of testis and 290 other tissues.
DR ExpressionAtlas; P48774; baseline and differential.
DR Genevisible; P48774; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; ISO:MGI.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0042178; P:xenobiotic catabolic 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; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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 Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..224
FT /note="Glutathione S-transferase Mu 5"
FT /id="PRO_0000185829"
FT DOMAIN 4..91
FT /note="GST N-terminal"
FT DOMAIN 93..211
FT /note="GST C-terminal"
FT BINDING 10..11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 49..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 62..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 75..76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B2"
SQ SEQUENCE 224 AA; 26635 MW; 70122FD0682237E2 CRC64;
MSSKSMVLGY WDIRGLAHAI RMLLEFTDTS YEEKRYICGE APDYDRSQWL DVKFKLDLDF
PNLPYLMDGK NKITQSNAIL RYIARKHNMC GDTEEEKIRV DIMENQIMDF RMQLVRLCYN
SNHENLKPQY LEQLPAQLKQ FSLFLGKFTW FAGEKLTFVD FLTYDVLDQN RIFEPKCLDE
FPNLKAFMCR FEALEKIAAF LQSDRFFKMP INNKMAKWGN KCLC
