TRX1_SCHPO
ID TRX1_SCHPO Reviewed; 103 AA.
AC O14463; P58265; Q9UTS9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Thioredoxin-1;
DE Short=TR-1;
DE Short=Trx-1;
GN Name=trx1; Synonyms=trx2; ORFNames=SPAC7D4.07c;
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 [GENOMIC DNA / MRNA].
RX PubMed=11267679; DOI=10.1016/s0167-4781(01)00176-2;
RA Cho Y.-W., Shin Y.H., Kim Y.-T., Kim H.-G., Lee Y.-J., Park E.-H.,
RA Fuchs J.A., Lim C.-J.;
RT "Characterization and regulation of Schizosaccharomyces pombe gene encoding
RT thioredoxin.";
RL Biochim. Biophys. Acta 1518:194-199(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Lenaers G., Perret E., Bonin O., Picard A., Caput D.;
RT "TRX2, a fission yeast stress protein.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AF251279; AAF76881.1; -; Genomic_DNA.
DR EMBL; AF192765; AAF05765.1; -; mRNA.
DR EMBL; AJ003819; CAA06033.1; -; mRNA.
DR EMBL; CU329670; CAB16724.1; -; Genomic_DNA.
DR PIR; T39085; T39085.
DR RefSeq; NP_593852.1; NM_001019281.2.
DR AlphaFoldDB; O14463; -.
DR SMR; O14463; -.
DR BioGRID; 278561; 14.
DR STRING; 4896.SPAC7D4.07c.1; -.
DR iPTMnet; O14463; -.
DR MaxQB; O14463; -.
DR PaxDb; O14463; -.
DR PRIDE; O14463; -.
DR EnsemblFungi; SPAC7D4.07c.1; SPAC7D4.07c.1:pep; SPAC7D4.07c.
DR GeneID; 2542084; -.
DR KEGG; spo:SPAC7D4.07c; -.
DR PomBase; SPAC7D4.07c; trx1.
DR VEuPathDB; FungiDB:SPAC7D4.07c; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_0_1; -.
DR InParanoid; O14463; -.
DR OMA; KIKICKF; -.
DR PhylomeDB; O14463; -.
DR PRO; PR:O14463; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016209; F:antioxidant activity; IDA:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:PomBase.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IC:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:PomBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:PomBase.
DR GO; GO:1990355; P:L-methionine salvage from methionine sulphoxide; IMP:PomBase.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IMP:PomBase.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Thioredoxin-1"
FT /id="PRO_0000120043"
FT DOMAIN 2..103
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 24
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 31
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 97..102
FT /note="ASIKAN -> VRLNRS (in Ref. 1; AAF05765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11297 MW; B3A6C85F4F6A256C CRC64;
MVKQVSDSSE FKSIVCQDKL VVVDFFATWC GPCKAIAPKF EQFSNTYSDA TFIKVDVDQL
SEIAAEAGVH AMPSFFLYKN GEKIEEIVGA NPAKLEASIK ANL
