ID   A0A1I8EAU2_WUCBA        Unreviewed;       463 AA.
AC   A0A1I8EAU2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thioredoxin domain-containing protein {ECO:0000313|WBParaSite:maker-PairedContig_1259-snap-gene-4.14-mRNA-1, ECO:0000313|WBParaSite:maker-PairedContig_1261-snap-gene-2.8-mRNA-1};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_1259-snap-gene-4.14-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-PairedContig_1259-snap-gene-4.14-mRNA-1, ECO:0000313|WBParaSite:maker-PairedContig_1261-snap-gene-2.8-mRNA-1}
RP   IDENTIFICATION.
RC   STRAIN=pt0022
RC   {ECO:0000313|WBParaSite:maker-PairedContig_1259-snap-gene-4.14-mRNA-1,
RC   ECO:0000313|WBParaSite:maker-PairedContig_1261-snap-gene-2.8-mRNA-1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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DR   STRING; 6293.A0A1I8EAU2; -.
DR   WBParaSite; maker-PairedContig_1259-snap-gene-4.14-mRNA-1; maker-PairedContig_1259-snap-gene-4.14-mRNA-1; maker-PairedContig_1259-snap-gene-4.14.
DR   WBParaSite; maker-PairedContig_1261-snap-gene-2.8-mRNA-1; maker-PairedContig_1261-snap-gene-2.8-mRNA-1; maker-PairedContig_1261-snap-gene-2.8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..463
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009605229"
FT   DOMAIN          11..136
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   463 AA;  53131 MW;  6CABB5CA8577C1BB CRC64;
     MWLLNCCING FLIFTRLQII NIIQATNIPS QVIELNDKFL QVKNDGLWFV DFYAPWCAHC
     KRLTPVWEHV GHALADRQSL VRVAKLDCTR YTNTASALNI RGYPTIIFFR NGREMVYEGE
     RKKEAIIDFA IKAAGPMVGI IESVHQLSQM RKDLKEPFFV YVEENYDTQL LELFDNYSDI
     AEMLFSSTRF YRAKRDVFPK SVSILEIPSI LVFKDGEYLT YNKEGGSLSD WIHSERWSLI
     PLITSTNVKE VGKMRLLVLI VVNMVERRNH TTRVGKFFSL VTNVAQMVRK DSSLSNIFQF
     GWLDGNEIAN NVVLDVPTAT VLLYLGLLVF NVTSYEYYSS NDAVSVMTEK SIISFLKRIA
     TGDVPPLGGR SLSQRFKRLC FEIFTNIAEM FRAQPLLTLC LLGVPLSFLS LITYCICSTD
     FTIDRDEIYP DDDDSFISGN YKTMREMSED FEMEGDESSN MKN
//