THIO4_DICDI
ID THIO4_DICDI Reviewed; 104 AA.
AC Q1ZXE0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Putative thioredoxin-4;
DE Short=Trx-4;
GN Name=trxD; Synonyms=trx4; ORFNames=DDB_G0287849;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {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; AAFI02000104; EAS66847.2; -; Genomic_DNA.
DR RefSeq; XP_001134530.2; XM_001134530.2.
DR AlphaFoldDB; Q1ZXE0; -.
DR SMR; Q1ZXE0; -.
DR STRING; 44689.DDB0233281; -.
DR PaxDb; Q1ZXE0; -.
DR EnsemblProtists; EAS66847; EAS66847; DDB_G0287849.
DR GeneID; 8626353; -.
DR KEGG; ddi:DDB_G0287849; -.
DR dictyBase; DDB_G0287849; trxD.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_0_1; -.
DR InParanoid; Q1ZXE0; -.
DR OMA; IESKERC; -.
DR PhylomeDB; Q1ZXE0; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DDI-844456; The NLRP3 inflammasome.
DR PRO; PR:Q1ZXE0; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:dictyBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:dictyBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 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 CHAIN 1..104
FT /note="Putative thioredoxin-4"
FT /id="PRO_0000312530"
FT DOMAIN 2..104
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 104 AA; 11756 MW; 4C49BE047471F9EE CRC64;
MSKVTNVSIN TKLDELLKGD QVIINFGAEW CGACKVLEPI FNKLSTQYPL VTFLKVEIDK
INVHESTKSI TSIPTIMLYQ KGKKTKEIVS PNETQLRKIL DSMK
