THIO3_PLAF7
ID THIO3_PLAF7 Reviewed; 180 AA.
AC Q4VWQ3; C0H538;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Thioredoxin 3 {ECO:0000303|PubMed:16910770};
DE Short=PfTRX3 {ECO:0000303|PubMed:16910770};
GN Name=TRX3 {ECO:0000303|PubMed:16910770};
GN ORFNames=PF3D7_0916100 {ECO:0000312|EMBL:CAX64215.2};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|EMBL:AAQ76284.1};
RN [1] {ECO:0000312|EMBL:AAQ76284.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAQ76284.1};
RA Nickel C., Rahlfs S., Becker K.;
RT "Multiple thioredoxins of the malarial parasite Plasmodium falciparum.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISULFIDE BOND.
RX PubMed=16910770; DOI=10.1089/ars.2006.8.1227;
RA Nickel C., Rahlfs S., Deponte M., Koncarevic S., Becker K.;
RT "Thioredoxin networks in the malarial parasite Plasmodium falciparum.";
RL Antioxid. Redox Signal. 8:1227-1239(2006).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=21203490; DOI=10.1371/journal.ppat.1001242;
RA Kehr S., Sturm N., Rahlfs S., Przyborski J.M., Becker K.;
RT "Compartmentation of redox metabolism in malaria parasites.";
RL PLoS Pathog. 6:e1001242-e1001242(2010).
RN [6] {ECO:0007744|PDB:3CXG}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 66-180, AND DISULFIDE BOND.
RA Wernimont A.K., Lew J., Kozieradzki I., Cossar D., Schapira M.,
RA Bochkarev A., Arrowsmith C.H., Bountra C., Wilkstrom M., Edwards A.M.,
RA Hui R., Hills T., Pizarro J.;
RT "Crystal structure of Plasmodium falciparum thioredoxin, PFI0790w.";
RL Submitted (APR-2008) to the PDB data bank.
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 {ECO:0000269|PubMed:16910770}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21203490}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- PTM: The disulfide bond between Cys-99 and Cys-102 acts as a redox-
CC active center and is reduced by thioredoxin reductase TRXR.
CC {ECO:0000305|PubMed:16910770, ECO:0000305|Ref.6}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AY306208; AAQ76284.1; -; mRNA.
DR EMBL; AL844508; CAX64215.2; -; Genomic_DNA.
DR PDB; 3CXG; X-ray; 2.00 A; A/B=66-180.
DR PDBsum; 3CXG; -.
DR AlphaFoldDB; Q4VWQ3; -.
DR SMR; Q4VWQ3; -.
DR STRING; 5833.PFI0790w; -.
DR PRIDE; Q4VWQ3; -.
DR EnsemblProtists; CAX64215; CAX64215; PF3D7_0916100.
DR VEuPathDB; PlasmoDB:PF3D7_0916100; -.
DR PhylomeDB; Q4VWQ3; -.
DR Reactome; R-PFA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-PFA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-PFA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-PFA-844456; The NLRP3 inflammasome.
DR EvolutionaryTrace; Q4VWQ3; -.
DR Proteomes; UP000001450; Chromosome 9.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Endoplasmic reticulum;
KW Membrane; Redox-active center; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..180
FT /note="Thioredoxin 3"
FT /id="PRO_0000455249"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..180
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 29..176
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 99..102
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|Ref.6, ECO:0007744|PDB:3CXG"
SQ SEQUENCE 180 AA; 20941 MW; 81CAB8D2DEA20FA7 CRC64;
MALICIGSVC FSLFHIGVII LLIINYFSSH IKKIFPSFFK NPNKEEIDKH IGNILEAKRK
NKQLEQSIYI ELKNTGSLNQ VFSSTQNSSI VIKFGAVWCK PCNKIKEYFK NQLNYYYVTL
VDIDVDIHPK LNDQHNIKAL PTFEFYFNLN NEWVLVHTVE GANQNDIEKA FQKYCLEKAK
