ID M3W7F3_FELCA Unreviewed; 226 AA.
AC M3W7F3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN Name=GSTK1 {ECO:0000313|Ensembl:ENSFCAP00000006744.3,
GN ECO:0000313|VGNC:VGNC:62730};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000006744.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000006744.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006744.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000006744.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006744.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000006744.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006744.3};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000710,
CC ECO:0000256|PIRNR:PIRNR006386};
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000256|ARBA:ARBA00006494, ECO:0000256|PIRNR:PIRNR006386}.
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DR EMBL; AANG04000096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003983179.1; XM_003983130.4.
DR AlphaFoldDB; M3W7F3; -.
DR PaxDb; 9685-ENSFCAP00000006744; -.
DR Ensembl; ENSFCAT00000007276.6; ENSFCAP00000006744.3; ENSFCAG00000007274.6.
DR GeneID; 101087726; -.
DR KEGG; fca:101087726; -.
DR CTD; 373156; -.
DR VGNC; VGNC:62730; GSTK1.
DR eggNOG; ENOG502R0HS; Eukaryota.
DR GeneTree; ENSGT00390000002723; -.
DR HOGENOM; CLU_069253_1_1_1; -.
DR OrthoDB; 4159077at2759; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000007274; Expressed in adult mammalian kidney and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd03021; DsbA_GSTK; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 7..210
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ SEQUENCE 226 AA; 25487 MW; 975E23B832901B0D CRC64;
MTPAPRTLEL FYDVLSPYSW LGFEVLCRYK KLWNINLQLR PSLIAAIMKD SGNQPPALLP
RKAQYLQNDI RLLGQQIQVP IQFPKDFFSV ILEKGSLSAM RFLTAVNLEH PKMLEKVSRE
LWMRVWSRDE DISEPKSILA AAEKAGMSTE QAQGLLEKIS TPKVKNELRD TTNAACKYGA
FGLPVTVAHL DGQTHMLFGS DRMELLAHLL GEKWMGPVPP AINAKI
//
