TRX2_SCHPO
ID TRX2_SCHPO Reviewed; 133 AA.
AC O94504;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Thioredoxin-2, mitochondrial;
DE Short=Trx-2;
DE Flags: Precursor;
GN Name=trx2; ORFNames=SPBC12D12.07c;
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] {ECO:0000305, ECO:0000312|EMBL:AAK59993.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=12020831; DOI=10.1016/s0167-4781(02)00246-4;
RA Lee Y.-J., Cho Y.-W., Kim D., Park E.-H., Fuchs J.A., Lim C.-J.;
RT "Characterization and regulation of a second gene encoding thioredoxin from
RT the fission yeast.";
RL Biochim. Biophys. Acta 1575:143-147(2002).
RN [2]
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 [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4] {ECO:0000305}
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).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH ARG3.
RX PubMed=18849471; DOI=10.1128/ec.00106-08;
RA Song J.Y., Kim K.D., Roe J.H.;
RT "Thiol-independent action of mitochondrial thioredoxin to support the urea
RT cycle of arginine biosynthesis in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 7:2160-2167(2008).
CC -!- FUNCTION: Disulfide reductase which serves multiple functions in
CC mitochondria, protecting mitochondrial components against thiol-
CC oxidative damage as a thiol-disulfide oxidoreductase, and supporting
CC urea cycle and respiration in mitochondria in a manner independent of
CC active site thiols. {ECO:0000269|PubMed:12020831,
CC ECO:0000269|PubMed:18849471}.
CC -!- SUBUNIT: Interacts with arg3. {ECO:0000269|PubMed:18849471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By aluminum chloride and ferrous chloride.
CC {ECO:0000269|PubMed:12020831}.
CC -!- DISRUPTION PHENOTYPE: Leads to auxotrophy for arginine and cysteine.
CC {ECO:0000269|PubMed:18849471}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK59993.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY034142; AAK59993.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329671; CAA22681.2; -; Genomic_DNA.
DR PIR; T39387; T39387.
DR RefSeq; NP_595954.2; NM_001021863.2.
DR AlphaFoldDB; O94504; -.
DR SMR; O94504; -.
DR BioGRID; 276444; 54.
DR STRING; 4896.SPBC12D12.07c.1; -.
DR MaxQB; O94504; -.
DR PaxDb; O94504; -.
DR PRIDE; O94504; -.
DR EnsemblFungi; SPBC12D12.07c.1; SPBC12D12.07c.1:pep; SPBC12D12.07c.
DR GeneID; 2539898; -.
DR KEGG; spo:SPBC12D12.07c; -.
DR PomBase; SPBC12D12.07c; trx2.
DR VEuPathDB; FungiDB:SPBC12D12.07c; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_5_1; -.
DR InParanoid; O94504; -.
DR OMA; FIDPFMP; -.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SPO-844456; The NLRP3 inflammasome.
DR PRO; PR:O94504; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IMP:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:PomBase.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Mitochondrion; Redox-active center;
KW Reference proteome; Stress response; Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..133
FT /note="Thioredoxin-2, mitochondrial"
FT /id="PRO_0000337144"
FT DOMAIN 30..133
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 61
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 133 AA; 15079 MW; 36905622539F263D CRC64;
MRGFIANSLK PHMRSFALRR SFTSSRILRK VNAVESFGDY NTRISADKVT VVDFYADWCG
PCKYLKPFLE KLSEQNQKAS FIAVNADKFS DIAQKNGVYA LPTMVLFRKG QELDRIVGAD
VKTLSSLLAK YQE
