THIO2_PLAF7
ID THIO2_PLAF7 Reviewed; 157 AA.
AC Q8IDP4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Thioredoxin 2 {ECO:0000303|PubMed:16910770};
DE Short=PfTRX2 {ECO:0000303|PubMed:16910770};
DE Flags: Precursor;
GN Name=TRX2 {ECO:0000303|PubMed:16910770};
GN ORFNames=PF3D7_1345100 {ECO:0000312|EMBL:CAD52575.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|EMBL:AAQ05974.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAQ05974.1};
RA Nickel C., Rahlfs S., Becker K.;
RT "Plasmodium falciparum possesses a mitochondrial thioredoxin system.";
RL Submitted (FEB-2002) 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 FUNCTION, AND IDENTIFICATION IN THE PTEX COMPLEX.
RX PubMed=19536257; DOI=10.1038/nature08104;
RA de Koning-Ward T.F., Gilson P.R., Boddey J.A., Rug M., Smith B.J.,
RA Papenfuss A.T., Sanders P.R., Lundie R.J., Maier A.G., Cowman A.F.,
RA Crabb B.S.;
RT "A newly discovered protein export machine in malaria parasites.";
RL Nature 459:945-949(2009).
RN [6] {ECO:0007744|PDB:3UL3}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 29-156, FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22355694; DOI=10.1038/srep00179;
RA Sharma A., Sharma A., Dixit S., Sharma A.;
RT "Structural insights into thioredoxin-2: a component of malaria parasite
RT protein secretion machinery.";
RL Sci. Rep. 1:179-179(2011).
RN [7] {ECO:0007744|PDB:4O32}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 24-157, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=25475729; DOI=10.1016/j.bbrc.2014.11.096;
RA Peng M., Cascio D., Egea P.F.;
RT "Crystal structure and solution characterization of the thioredoxin-2 from
RT Plasmodium falciparum, a constituent of an essential parasitic protein
RT export complex.";
RL Biochem. Biophys. Res. Commun. 456:403-409(2015).
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 (PubMed:16910770,
CC PubMed:22355694). As part of the translocon PTEX complex, plays a role
CC in the export of parasite proteins into the host erythrocyte (By
CC similarity). The translocon PTEX complex is a multi-protein machinery
CC resident in the parasite parasitophorous vacuolar membrane, responsible
CC for protein secretion into host cells (PubMed:19536257). May contribute
CC to the unfolding of proteins containing the PEXEL localization motif
CC before their passage through the translocon or regulate the PTEX
CC complex function (PubMed:19536257). {ECO:0000250|UniProtKB:A0A509AQW5,
CC ECO:0000269|PubMed:16910770, ECO:0000269|PubMed:19536257,
CC ECO:0000269|PubMed:22355694, ECO:0000303|PubMed:19536257}.
CC -!- SUBUNIT: Monomer (PubMed:25475729). Component of the Plasmodium
CC translocon of exported proteins (PTEX) complex composed of HSP101,
CC EXP2, PTEX150, PTEX88 and TRX2 (PubMed:19536257).
CC {ECO:0000269|PubMed:19536257, ECO:0000269|PubMed:25475729}.
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole membrane
CC {ECO:0000269|PubMed:22355694}; Peripheral membrane protein
CC {ECO:0000305}. Note=Appears to localize to other uncharacterized
CC organelles. {ECO:0000269|PubMed:22355694}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC including in rings, trophozoites, schizonts and merozoites (at protein
CC level). {ECO:0000269|PubMed:22355694}.
CC -!- PTM: The disulfide bond between Cys-82 and Cys-85 acts as a redox-
CC active center and is reduced by thioredoxin reductase TRXR.
CC {ECO:0000305|PubMed:16910770, ECO:0000305|PubMed:25475729}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AF484689; AAQ05974.1; -; mRNA.
DR EMBL; AL844509; CAD52575.1; -; Genomic_DNA.
DR RefSeq; XP_001350166.1; XM_001350130.1.
DR PDB; 3UL3; X-ray; 2.90 A; A/B=29-156.
DR PDB; 4O32; X-ray; 2.20 A; A/B/C=24-157.
DR PDBsum; 3UL3; -.
DR PDBsum; 4O32; -.
DR AlphaFoldDB; Q8IDP4; -.
DR SMR; Q8IDP4; -.
DR STRING; 5833.MAL13P1.225; -.
DR TCDB; 3.A.26.1.1; the plasmodium translocon of exported proteins (ptex) family.
DR PRIDE; Q8IDP4; -.
DR EnsemblProtists; CAD52575; CAD52575; PF3D7_1345100.
DR GeneID; 813783; -.
DR KEGG; pfa:PF3D7_1345100; -.
DR VEuPathDB; PlasmoDB:PF3D7_1345100; -.
DR HOGENOM; CLU_1681429_0_0_1; -.
DR InParanoid; Q8IDP4; -.
DR OMA; AKWCHAC; -.
DR PhylomeDB; Q8IDP4; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0097619; C:PTEX complex; IDA:GeneDB.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:GeneDB.
DR GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Membrane;
KW Redox-active center; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..157
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5011949510"
FT DOMAIN 46..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 82..85
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:25475729, ECO:0007744|PDB:4O32"
SQ SEQUENCE 157 AA; 18630 MW; 68C9B12DF4B9197B CRC64;
MKKYIFFFLF SFINFFFVYD VTCTKEVTST NDDPLTPLNR FDKYYLRMFK KVPRLQQNGS
NIINGVNMKN TVIVLYFFAK WCQACTMQST EMDKLQKYYG KRIYLLKVDL DKNESLARKF
SVKSLPTIIL LKNKTMLARK DHFVSSNDLI ALIKKHL
