GSTK1_MOUSE
ID GSTK1_MOUSE Reviewed; 226 AA.
AC Q9DCM2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glutathione S-transferase kappa 1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:12720545};
DE AltName: Full=GST 13-13;
DE AltName: Full=GST class-kappa;
DE AltName: Full=GSTK1-1;
DE Short=mGSTK1;
DE AltName: Full=Glutathione S-transferase subunit 13;
GN Name=Gstk1;
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=12720545; DOI=10.1042/bj20030415;
RA Jowsey I.R., Thomson R.E., Orton T.C., Elcombe C.R., Hayes J.D.;
RT "Biochemical and genetic characterization of a murine class Kappa
RT glutathione S-transferase.";
RL Biochem. J. 373:559-569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 STRAIN=FVB/N; TISSUE=Liver;
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 203-213, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-49; LYS-68; LYS-74;
RP LYS-93; LYS-116; LYS-144; LYS-158; LYS-167; LYS-177 AND LYS-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-74; LYS-85; LYS-93;
RP LYS-116; LYS-158; LYS-165; LYS-167 AND LYS-177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Glutathione S-transferase that catalyzes the conjugation of
CC glutathione to exogenous and endogenous compounds.
CC {ECO:0000269|PubMed:12720545}.
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:12720545};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Q3}.
CC -!- INTERACTION:
CC Q9DCM2; Q60994: Adipoq; NbExp=3; IntAct=EBI-8369416, EBI-7264589;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12720545}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart, kidney, liver and
CC skeletal muscle. {ECO:0000269|PubMed:12720545}.
CC -!- PTM: Acetylation of Lys-93 is observed in liver mitochondria from
CC fasted mice but not from fed mice. {ECO:0007744|PubMed:23806337}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000305}.
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DR EMBL; AK002661; BAB22268.1; -; mRNA.
DR EMBL; AY279096; AAP20655.1; -; mRNA.
DR EMBL; BC058163; AAH58163.1; -; mRNA.
DR CCDS; CCDS20063.1; -.
DR RefSeq; NP_083831.1; NM_029555.2.
DR AlphaFoldDB; Q9DCM2; -.
DR SMR; Q9DCM2; -.
DR BioGRID; 218054; 1.
DR DIP; DIP-48623N; -.
DR IntAct; Q9DCM2; 1.
DR STRING; 10090.ENSMUSP00000031897; -.
DR iPTMnet; Q9DCM2; -.
DR PhosphoSitePlus; Q9DCM2; -.
DR SwissPalm; Q9DCM2; -.
DR EPD; Q9DCM2; -.
DR jPOST; Q9DCM2; -.
DR MaxQB; Q9DCM2; -.
DR PaxDb; Q9DCM2; -.
DR PeptideAtlas; Q9DCM2; -.
DR PRIDE; Q9DCM2; -.
DR ProteomicsDB; 271104; -.
DR Antibodypedia; 1607; 375 antibodies from 35 providers.
DR DNASU; 76263; -.
DR Ensembl; ENSMUST00000031897; ENSMUSP00000031897; ENSMUSG00000029864.
DR GeneID; 76263; -.
DR KEGG; mmu:76263; -.
DR UCSC; uc009bqo.1; mouse.
DR CTD; 373156; -.
DR MGI; MGI:1923513; Gstk1.
DR VEuPathDB; HostDB:ENSMUSG00000029864; -.
DR eggNOG; ENOG502R0HS; Eukaryota.
DR GeneTree; ENSGT00440000033697; -.
DR HOGENOM; CLU_069253_1_1_1; -.
DR InParanoid; Q9DCM2; -.
DR OMA; CYLDCVS; -.
DR OrthoDB; 1320977at2759; -.
DR PhylomeDB; Q9DCM2; -.
DR TreeFam; TF105323; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 76263; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gstk1; mouse.
DR PRO; PR:Q9DCM2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DCM2; protein.
DR Bgee; ENSMUSG00000029864; Expressed in left lobe of liver and 254 other tissues.
DR ExpressionAtlas; Q9DCM2; baseline and differential.
DR Genevisible; Q9DCM2; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR CDD; cd03021; DsbA_GSTK; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR044088; GSTK.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Transferase.
FT CHAIN 1..226
FT /note="Glutathione S-transferase kappa 1"
FT /id="PRO_0000185892"
FT BINDING 16..18
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q3"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q3"
FT BINDING 183
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q3"
FT BINDING 200..201
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q3"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 74
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 116
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 167
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 167
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 177
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 177
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 226 AA; 25704 MW; 480332FD618ABCDD CRC64;
MGPAPRILEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLQLR PTLIAGIMKD SGNQPPAMVP
RKGQYIFKEI PLLKQFFQVP LNIPKDFFGE TVKKGSINAM RFLTTVSMEQ PEMLEKVSRE
IWMRVWSRDE DITEYQSILA AAVKAGMSTA QAQHFLEKIS TQQVKNKLIE NTDAACKYGA
FGLPTTVAHV DGKTYMLFGS DRLELLAYLL GEKWMGPVPP TANARL
