ID YC12_SCHPO Reviewed; 220 AA. AC O74830; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 134. DE RecName: Full=Putative glutathione S-transferase C1183.02; DE EC=2.5.1.18; GN ORFNames=SPCC1183.02; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the fission RT yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). CC -!- FUNCTION: Involved in the oxidative stress response and detoxification. CC {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329672; CAA21082.1; -; Genomic_DNA. DR PIR; T40842; T40842. DR RefSeq; NP_587885.1; NM_001022877.2. DR AlphaFoldDB; O74830; -. DR SMR; O74830; -. DR BioGRID; 275588; 7. DR STRING; 284812.O74830; -. DR iPTMnet; O74830; -. DR MaxQB; O74830; -. DR PaxDb; 4896-SPCC1183-02-1; -. DR EnsemblFungi; SPCC1183.02.1; SPCC1183.02.1:pep; SPCC1183.02. DR GeneID; 2539015; -. DR KEGG; spo:SPCC1183.02; -. DR PomBase; SPCC1183.02; -. DR VEuPathDB; FungiDB:SPCC1183.02; -. DR eggNOG; KOG0867; Eukaryota. DR HOGENOM; CLU_011226_3_2_1; -. DR InParanoid; O74830; -. DR OMA; NTRTVCL; -. DR PhylomeDB; O74830; -. DR Reactome; R-SPO-156842; Eukaryotic Translation Elongation. DR PRO; PR:O74830; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; ISM:PomBase. DR GO; GO:0002182; P:cytoplasmic translational elongation; ISS:PomBase. DR CDD; cd03181; GST_C_EF1Bgamma_like; 1. DR CDD; cd03044; GST_N_EF1Bgamma; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1. DR PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 3: Inferred from homology; KW Cytoplasm; Reference proteome; Transferase. FT CHAIN 1..220 FT /note="Putative glutathione S-transferase C1183.02" FT /id="PRO_0000316037" FT DOMAIN 2..81 FT /note="GST N-terminal" FT DOMAIN 89..216 FT /note="GST C-terminal" SQ SEQUENCE 220 AA; 25504 MW; 4BB915229C886213 CRC64; MFLGTLYSFK TNTRTVCLLE LAKLLDLQVD LVETYPHKFS ADLAAKFPLQ KLPVFIGADG FELSEVIAIV KYFYEKGKHN DKEGLGPVNE VEEAEMLKWM CFINFDIVTP QNVRPWVGMF RGNIPYEEKP FKESATRAID SLKIPNELVK DRTYLVGDRF TLADLFFGSL LRIFFNSIID EKTRKELPHL TRYYITMFHQ AKLETYFPLE LPLTVTVAKK //