ID B3W657_SCHJA Unreviewed; 493 AA.
AC B3W657;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 13-SEP-2023, entry version 80.
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 japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:ACE06849.1};
RN [1] {ECO:0000313|EMBL:ACE06849.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R.,
RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., Xue C.L.,
RA Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., Han Z.G.;
RT "New perspectives on host-parasite interplay by comparative transcriptomic
RT and proteomic analyses of Schistosoma japonicum.";
RL PLoS Pathog. 2:268-281(2006).
RN [2] {ECO:0000313|EMBL:ACE06849.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu F., Lu J., Hu W., Wang S.-Y., Cui S.-J., Chi M., Yan Q., Wang X.-R.,
RA Song H.-D., Xu X.-N., Wang J.-J., Zhang X.-L., Zhang X., Wang Z.-Q.,
RA Xue C.-L., Brindley P.J., McManus D.P., Yang P.-Y., Feng Z., Chen Z.,
RA Han Z.-G.;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; EZ000069; ACE06849.1; -; mRNA.
DR AlphaFoldDB; B3W657; -.
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; 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:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 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 2: Evidence at transcript level;
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..24
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 25..493
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005122962"
FT DOMAIN 7..133
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 347..476
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 54..57
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 397..400
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 493 AA; 55709 MW; 7B1ADA0F05E90379 CRC64;
MFVRRALKML WLSPFLLLFA FATCSEVLEL TKDNFHSQLK SIPVCLVKFY APWCGHCKSL
APEYKSAADI ISKKTANLKL AEVDCTAHGD ICSEFGVNGY PTLKIFRDGI FDSEYNGPRN
ADGIANYMIS RAGPVSKEIS AFKDVEDSLS DDKPSVVAFI KSSSDPLMKT FMTLAKSMID
NAVFLHSHNN IYENSGENEL RLYLPKRLRT KLEPDFSIYS GEMEVDDIKK WIRKDGHGLV
GYRSPDDSFY FVDSNLVVIY NNESINTYPS GVKYLRNRIL KTLKNHPDKF KDLKFAYSFT
GDFSYELSDY EINADQLPAV RISSKDGKKY RLDKYSPESF LEFLNKFQDG LLTPHLKSEP
IPTSDSSVVK KLVALNFNDI VNDEEKDVMV VFHAPWCGHC KNLMPKYEEA ASKLKNEPNL
VLAAMDATAN DVPPPYEVTG FPTIYFVPKG KKSSPMLYQG GRDTSDIIKF LAREATEELS
GYDRSGNTKK SDL
//
