ID Q5RDN0_PONAB Unreviewed; 190 AA.
AC Q5RDN0; A0A2J8V2U2; A0A2J8V2W5; H2PNV4;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN Name=DKFZp459M1330 {ECO:0000313|EMBL:CAH90127.1};
GN Synonyms=GSTK1 {ECO:0000313|Ensembl:ENSPPYP00000020320.3};
GN ORFNames=CR201_G0022711 {ECO:0000313|EMBL:PNJ51848.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|EMBL:CAH90127.1};
RN [1] {ECO:0000313|EMBL:CAH90127.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cortex {ECO:0000313|EMBL:CAH90127.1};
RG The German cDNA Consortium;
RA Koehrer K., Beyer A., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G.,
RA Han M., Wiemann S.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000020320.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNJ51848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ51848.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSPPYP00000020320.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; CR857874; CAH90127.1; -; mRNA.
DR EMBL; NDHI03003435; PNJ51848.1; -; Genomic_DNA.
DR RefSeq; NP_001125024.1; NM_001131552.1.
DR RefSeq; XP_009241620.1; XM_009243345.1.
DR STRING; 9601.ENSPPYP00000020320; -.
DR Ensembl; ENSPPYT00000021117.3; ENSPPYP00000020320.3; ENSPPYG00000018113.3.
DR GeneID; 100171904; -.
DR KEGG; pon:100171904; -.
DR CTD; 373156; -.
DR GeneTree; ENSGT00440000033697; -.
DR OrthoDB; 4159077at2759; -.
DR TreeFam; TF105323; -.
DR Proteomes; UP000001595; Chromosome 7.
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 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006386}.
FT DOMAIN 7..179
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 190 AA; 21786 MW; 701402231506DC78 CRC64;
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP
RKGQYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTALNLEH PEMLEKASRE
LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKMS TPKVKNQLKE TTEAACRYGE
RSGWALYLQL
//
