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   02-SEP-2026, entry version 164.
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,
RC   Pancreas, 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=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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; 3.
DR   DIP; DIP-48623N; -.
DR   FunCoup; Q9DCM2; 1213.
DR   IntAct; Q9DCM2; 1.
DR   STRING; 10090.ENSMUSP00000031897; -.
DR   GlyGen; Q9DCM2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DCM2; -.
DR   PhosphoSitePlus; Q9DCM2; -.
DR   SwissPalm; Q9DCM2; -.
DR   jPOST; Q9DCM2; -.
DR   PaxDb; 10090-ENSMUSP00000031897; -.
DR   PeptideAtlas; Q9DCM2; -.
DR   ProteomicsDB; 271104; -.
DR   Antibodypedia; 1607; 389 antibodies from 38 providers.
DR   DNASU; 76263; -.
DR   Ensembl; ENSMUST00000031897.8; ENSMUSP00000031897.6; ENSMUSG00000029864.8.
DR   GeneID; 76263; -.
DR   KEGG; mmu:76263; -.
DR   UCSC; uc009bqo.1; mouse.
DR   AGR; MGI:1923513; -.
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; PFWGFDR; -.
DR   OrthoDB; 4664297at2759; -.
DR   PhylomeDB; Q9DCM2; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-9033241; Peroxisomal protein import.
DR   BioGRID-ORCS; 76263; 0 hits in 76 CRISPR screens.
DR   PRO; PR:Q9DCM2; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9DCM2; protein.
DR   Bgee; ENSMUSG00000029864; Expressed in left lobe of liver and 256 other cell types or tissues.
DR   ExpressionAtlas; Q9DCM2; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0005777; C:peroxisome; ISO:GO_Central.
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   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
DR   GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR   CDD; cd03021; DsbA_GSTK; 1.
DR   FunFam; 3.40.30.10:FF:000096; Glutathione S-transferase kappa; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR051924; GST_Kappa/NadH.
DR   InterPro; IPR044088; GSTK.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//