GSTA4_MOUSE
ID GSTA4_MOUSE Reviewed; 222 AA.
AC P24472; Q9CQ81; Q9CTY7; Q9CY87; Q9D038;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Glutathione S-transferase A4;
DE EC=2.5.1.18;
DE AltName: Full=GST A4-4;
DE Short=GSTA4-4;
DE AltName: Full=GST class-alpha member 4;
DE AltName: Full=Glutathione S-transferase 5.7;
DE Short=GST 5.7;
GN Name=Gsta4; Synonyms=Gsta;
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 TISSUE=Lung;
RX PubMed=1426286; DOI=10.1016/0014-5793(92)81438-r;
RA Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C.;
RT "A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for
RT mouse lung glutathione S-transferase GST 5.7.";
RL FEBS Lett. 313:173-176(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Small intestine, and Tongue;
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].
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 106-120 AND 167-184.
RC STRAIN=CD-1; TISSUE=Liver, and Lung;
RX PubMed=1898365; DOI=10.1042/bj2780793;
RA Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C.;
RT "Characterization of a novel glutathione S-transferase isoenzyme from mouse
RT lung and liver having structural similarity to rat glutathione S-
RT transferase 8-8.";
RL Biochem. J. 278:793-799(1991).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Lung;
RX PubMed=9498801; DOI=10.1016/s0014-5793(98)00026-x;
RA Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P.,
RA Dijkstra B.W.;
RT "Crystal structure of a murine alpha-class glutathione S-transferase
RT involved in cellular defense against oxidative stress.";
RL FEBS Lett. 422:285-290(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RC TISSUE=Lung;
RX PubMed=10508391; DOI=10.1021/bi990468i;
RA Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X.;
RT "Crystal structure of a murine glutathione S-transferase in complex with a
RT glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione
RT in the other: evidence of signaling across the dimer interface.";
RL Biochemistry 38:11887-11894(1999).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000269|PubMed:10508391}.
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 Evidence={ECO:0000269|PubMed:10508391};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10508391}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: On the basis of immunological and kinetics data, GST 5.7
CC is distinct from alpha, mu and pI classes of GTS. However it has been
CC postulated that this protein may be part of a distinct subgroup within
CC this alpha class.
CC -!- MISCELLANEOUS: The variations were found from AA sequencing and imply
CC there are multiple forms of this protein. These variations are likely
CC to be sex-linked and tissue specific.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; L06047; AAA37754.1; -; mRNA.
DR EMBL; AK008189; BAB25520.1; -; mRNA.
DR EMBL; AK008193; BAB25524.1; -; mRNA.
DR EMBL; AK008400; BAB25649.1; -; mRNA.
DR EMBL; AK008490; BAB25696.1; -; mRNA.
DR EMBL; AK009668; BAB26429.1; -; mRNA.
DR EMBL; AK010098; BAB26701.1; -; mRNA.
DR EMBL; AK011177; BAB27449.1; -; mRNA.
DR EMBL; AK011841; BAB27873.1; -; mRNA.
DR EMBL; AK019100; BAB31546.1; -; mRNA.
DR EMBL; AK019271; BAB31640.1; -; mRNA.
DR EMBL; BC012639; AAH12639.1; -; mRNA.
DR CCDS; CCDS23357.1; -.
DR PIR; S27234; S27234.
DR RefSeq; NP_034487.2; NM_010357.3.
DR PDB; 1B48; X-ray; 2.60 A; A/B=2-222.
DR PDB; 1GUK; X-ray; 2.90 A; A/B=1-222.
DR PDBsum; 1B48; -.
DR PDBsum; 1GUK; -.
DR AlphaFoldDB; P24472; -.
DR SMR; P24472; -.
DR BioGRID; 200093; 2.
DR MINT; P24472; -.
DR STRING; 10090.ENSMUSP00000034903; -.
DR iPTMnet; P24472; -.
DR PhosphoSitePlus; P24472; -.
DR REPRODUCTION-2DPAGE; P24472; -.
DR EPD; P24472; -.
DR jPOST; P24472; -.
DR MaxQB; P24472; -.
DR PaxDb; P24472; -.
DR PeptideAtlas; P24472; -.
DR PRIDE; P24472; -.
DR ProteomicsDB; 271356; -.
DR TopDownProteomics; P24472; -.
DR DNASU; 14860; -.
DR Ensembl; ENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.
DR GeneID; 14860; -.
DR KEGG; mmu:14860; -.
DR UCSC; uc009qty.2; mouse.
DR CTD; 2941; -.
DR MGI; MGI:1309515; Gsta4.
DR VEuPathDB; HostDB:ENSMUSG00000032348; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000161750; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; P24472; -.
DR OMA; AKPKLWY; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P24472; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 3474.
DR SABIO-RK; P24472; -.
DR BioGRID-ORCS; 14860; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gsta4; mouse.
DR EvolutionaryTrace; P24472; -.
DR PRO; PR:P24472; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P24472; protein.
DR Bgee; ENSMUSG00000032348; Expressed in urinary bladder urothelium and 308 other tissues.
DR ExpressionAtlas; P24472; baseline and differential.
DR Genevisible; P24472; 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: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; ISS:UniProtKB.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0004769; F:steroid delta-isomerase activity; ISO:MGI.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR003080; GST_alpha.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01266; GSTRNSFRASEA.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione S-transferase A4"
FT /id="PRO_0000185791"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..208
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT BINDING 53..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:10508391,
FT ECO:0007744|PDB:1B48"
FT BINDING 66..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:10508391,
FT ECO:0007744|PDB:1B48"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P14942"
FT VARIANT 115
FT /note="K -> P (requires 2 nucleotide substitutions)"
FT VARIANT 167
FT /note="V -> G"
FT VARIANT 179..180
FT /note="PL -> GE"
FT CONFLICT 36
FT /note="E -> D (in Ref. 2; BAB31640)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..206
FT /note="KP -> SA (in Ref. 2; BAB27873)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> I (in Ref. 1; AAA37754)"
FT /evidence="ECO:0000305"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:1B48"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1GUK"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1B48"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1B48"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:1B48"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1GUK"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:1B48"
SQ SEQUENCE 222 AA; 25564 MW; B580E3415289424D CRC64;
MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL LFGQVPLVEI
DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIAVAP FKTPKEKEES
YDLILSRAKT RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEL SAPVLSDFPL
LQAFKTRISN IPTIKKFLQP GSQRKPPPDG PYVEVVRTVL KF
