ERP60_SCHMA
ID ERP60_SCHMA Reviewed; 484 AA.
AC P38658;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable protein disulfide-isomerase ER-60;
DE EC=5.3.4.1;
DE AltName: Full=ERP60;
DE Flags: Precursor;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Liberian;
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;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a phosphatidylinositol 4,5-
CC bisphosphate phosphodiesterase type I (phospholipase C-alpha).
CC {ECO:0000305}.
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DR EMBL; Z22934; CAA80521.1; -; Genomic_DNA.
DR AlphaFoldDB; P38658; -.
DR SMR; P38658; -.
DR STRING; 6183.Smp_079770.1; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_6_0_1; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..484
FT /note="Probable protein disulfide-isomerase ER-60"
FT /id="PRO_0000034228"
FT DOMAIN 15..125
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 338..467
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 481..484
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 47
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 389
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 390
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 453
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 46..49
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 388..391
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 484 AA; 54306 MW; D85606CFC5C269B9 CRC64;
MRWLLSCLFL VAFASCSKVL ELTKDNFHSE LKSIPVALVK FYAPWCGHCK KLAPEFTSAA
QIISGKTNDV KLVKVDCTTQ ESICSEFGVS GYPTLKIFRN GDLDGEYNGP RNANGIANYM
ISRAGPVSKE VSTVSDVENV LSDDKPTVFA FVKSSSDPLI KTFMALAKSM VDDAVFCHSH
NNLFVTPSDN ELRVYLPKRL RTKFEDDFAV YKGELESNNI KDWIRKHGQG LVGYRSPSNT
FYFENSDLVV LYNNQSIDSY PSGVKYLRNR VLKTLKDNPQ KFKNLVFAYS FADDFSYEIS
DYGIEADKLP AVVIQSKDKK YKLEKFSLDA FSDFLNKFED GLLTPHVKSE PLPTDDSSAV
KKLVALNFDE IVNNEEKDVM VVFHAGWCGH CKNLMPKYEE AASKVKNEPN LVLAAMDATA
NDVPSPYQVR GFPTIYFVPK GKKSSPVSYE GGRDTNDIIK YLAREATEEL IGYDRSGNPK
KSEL
