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THIO3_DICDI
ID   THIO3_DICDI             Reviewed;         104 AA.
AC   P29447; Q1ZXA3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Thioredoxin-3;
DE            Short=Trx-3;
GN   Name=trxC; Synonyms=trx3; ORFNames=DDB_G0294489;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=1577820; DOI=10.1016/s0021-9258(19)50177-6;
RA   Wetterauer B., Jacquot J.-P., Veron M.;
RT   "Thioredoxins from Dictyostelium discoideum are a developmentally regulated
RT   multigene family.";
RL   J. Biol. Chem. 267:9895-9904(1992).
RN   [2]
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.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; M91383; AAA33260.1; -; mRNA.
DR   EMBL; AAFI02000199; EAS66808.2; -; Genomic_DNA.
DR   PIR; C46264; C46264.
DR   RefSeq; XP_001134491.2; XM_001134491.2.
DR   AlphaFoldDB; P29447; -.
DR   SMR; P29447; -.
DR   STRING; 44689.DDB0233050; -.
DR   SWISS-2DPAGE; P29447; -.
DR   PaxDb; P29447; -.
DR   EnsemblProtists; EAS66808; EAS66808; DDB_G0294489.
DR   GeneID; 8628985; -.
DR   KEGG; ddi:DDB_G0294489; -.
DR   dictyBase; DDB_G0294489; trxC.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_14_6_1; -.
DR   InParanoid; P29447; -.
DR   OMA; QKKIQKH; -.
DR   PhylomeDB; P29447; -.
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:P29447; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 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   CHAIN           1..104
FT                   /note="Thioredoxin-3"
FT                   /id="PRO_0000120031"
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            25
FT                   /note="Deprotonates C-terminal active site Cys"
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"
FT   CONFLICT        67
FT                   /note="V -> G (in Ref. 1; AAA33260)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   104 AA;  11796 MW;  F42189232A939B85 CRC64;
     MSKVIHVTSN EELDKYLQHQ RVVVDFSAEW CGPCRAIAPV FDKLSNEFTT FTFVHVDIDK
     VNTHPIVKEI RSVPTFYFYV NGAKVSEFSG ANEATLRSTL EANI
 
 
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