THIO2_PLABA
ID THIO2_PLABA Reviewed; 157 AA.
AC A0A509AQW5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Thioredoxin 2 {ECO:0000303|PubMed:23869529};
DE Short=PbTRX2 {ECO:0000303|PubMed:23869529};
DE Flags: Precursor;
GN Name=TRX2 {ECO:0000303|PubMed:23869529};
GN ORFNames=PBANKA_1358000 {ECO:0000312|EMBL:VUC57967.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PTEX COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=23869529; DOI=10.1111/mmi.12334;
RA Matthews K., Kalanon M., Chisholm S.A., Sturm A., Goodman C.D., Dixon M.W.,
RA Sanders P.R., Nebl T., Fraser F., Haase S., McFadden G.I., Gilson P.R.,
RA Crabb B.S., de Koning-Ward T.F.;
RT "The Plasmodium translocon of exported proteins (PTEX) component
RT thioredoxin-2 is important for maintaining normal blood-stage growth.";
RL Mol. Microbiol. 89:1167-1186(2013).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25043043; DOI=10.1038/nature13555;
RA Elsworth B., Matthews K., Nie C.Q., Kalanon M., Charnaud S.C.,
RA Sanders P.R., Chisholm S.A., Counihan N.A., Shaw P.J., Pino P., Chan J.A.,
RA Azevedo M.F., Rogerson S.J., Beeson J.G., Crabb B.S., Gilson P.R.,
RA de Koning-Ward T.F.;
RT "PTEX is an essential nexus for protein export in malaria parasites.";
RL Nature 511:587-591(2014).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=25820521; DOI=10.1128/ec.00276-14;
RA Matz J.M., Ingmundson A., Costa Nunes J., Stenzel W., Matuschewski K.,
RA Kooij T.W.;
RT "In Vivo Function of PTEX88 in Malaria Parasite Sequestration and
RT Virulence.";
RL Eukaryot. Cell 14:528-534(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 (By similarity). As part
CC of the translocon PTEX complex, plays a role in the export of parasite
CC proteins into the host erythrocyte (PubMed:25043043). The translocon
CC PTEX complex is a multi-protein machinery resident in the parasite
CC parasitophorous vacuolar membrane, responsible for protein secretion
CC into host cells (PubMed:23869529, PubMed:25043043). May contribute to
CC the unfolding of proteins containing the PEXEL localization motif
CC before their passage through the translocon or regulate the PTEX
CC complex function (PubMed:25043043). {ECO:0000250|UniProtKB:Q8IDP4,
CC ECO:0000269|PubMed:23869529, ECO:0000269|PubMed:25043043,
CC ECO:0000303|PubMed:25043043}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the translocon PTEX
CC complex composed of HSP101, EXP2, PTEX150, PTEX88 and TRX2
CC (PubMed:23869529). {ECO:0000250|UniProtKB:Q8IDP4,
CC ECO:0000269|PubMed:23869529}.
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:0000250|UniProtKB:Q8IDP4}.
CC -!- DISRUPTION PHENOTYPE: Mice of infection with knockout parasites have
CC reduced blood parasitemia due to a slower growth at the ring and
CC schizont stages (PubMed:23869529). Parasite burden in vessels of lung
CC and adipose tissue is reduced (PubMed:25820521). Also, the development
CC of experimental cerebral malaria is delayed (PubMed:23869529,
CC PubMed:25820521). In infected host erythrocytes, surface expression of
CC parasite antigens is reduced (PubMed:25043043).
CC {ECO:0000269|PubMed:23869529, ECO:0000269|PubMed:25043043,
CC ECO:0000269|PubMed:25820521}.
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; LK023128; VUC57967.1; -; Genomic_DNA.
DR STRING; 5821.PBANKA_135800; -.
DR VEuPathDB; PlasmoDB:PBANKA_1358000; -.
DR OMA; AKWCHAC; -.
DR Proteomes; UP000074855; Chromosome 13.
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 Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..157
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5021193043"
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"
SQ SEQUENCE 157 AA; 18418 MW; 48C0469D80E8C40B CRC64;
MKHILALVVF IISFFCFKDV NCIKDFQLSP IESPLTALNK YDKFFLRMYN KMPRLEQSST
DYINGINMKN TIFVLYFYAK WCHACKLQGP ELDKLEKNFG KKVHIIRIDI DNNEEIAKKN
FIKALPTTII IKNKVILAKN EHFVTSNELT STIRKHL
