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Database: UniProt
Entry: Q26593_SCHMA
LinkDB: Q26593_SCHMA
Original site: Q26593_SCHMA 
ID   Q26593_SCHMA            Unreviewed;       482 AA.
AC   Q26593;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|EMBL:CAA80520.1};
RN   [1] {ECO:0000313|EMBL:CAA80520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liberia {ECO:0000313|EMBL:CAA80520.1};
RX   PubMed=8078516; DOI=10.1016/0166-6851(94)90141-4;
RA   Finken M., Sobek A., Symmons P., Kunz W.;
RT   "Characterization of the complete protein disulfide isomerase gene of
RT   Schistosoma mansoni and identification of the tissues of its expression.";
RL   Mol. Biochem. Parasitol. 64:135-144(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC         ECO:0000256|RuleBase:RU361130};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; Z22933; CAA80520.1; -; Genomic_DNA.
DR   PIR; S34275; S34275.
DR   AlphaFoldDB; Q26593; -.
DR   HOGENOM; CLU_025879_1_0_1; -.
DR   ExpressionAtlas; Q26593; baseline.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT   CHAIN           22..482
FT                   /note="Protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5005142827"
FT   DOMAIN          5..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          328..467
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        391..394
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   482 AA;  54155 MW;  EA2DE2E2BB209658 CRC64;
     MKLSVALVVV FLVFAASEVT EEDDVLVLNK KNFDDVIKTN KFVLVEFYAP WCGHCKALAP
     EYSEAAKKLK EKGSLIKLAK VDATVEEELA LKHGEKGYPT LKFFRNEQPI DFLGERDSDA
     IVNWCLRKSK PSVEYIDSLD SCKQFIDKAN IAILGFIKDT DSLDLADFEK VADELDDAGF
     AIANSSEILT EYGITQTPKI VLFKNFDENR VEYTGGTLEN LKHFIQVESV PLVSEFSQKT
     AGVVFGSPIQ KHIVFFLSKS TDHSDLVDKL TEVARQFKGK LHVIYVDVDV ENNLRVLEFF
     GLSKNDAPTY RIIELGEETT KYKPDTNDYS VSAMSDFVQR TIDGKVKPFL MSEEIPSDQT
     GAVKVLVGKN YNDVVKDKSK DVFVKLYAPW CGHCKALAPV WDELGETFKN SDTVIAKMDA
     TVNEVEDLKV TSFPTLKFYP KNSEEVIDYT GDRSFEALKK FVESGGKSSE ATKQEDQIKD
     EL
//
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