ID   PDI_RICCO               Reviewed;         498 AA.
AC   Q43116;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hale;
RX   PubMed=8631332; DOI=10.1111/j.1432-1033.1996.00215.x;
RA   Coughlan S.J., Hastings C., Winfrey R.J.;
RT   "Molecular characterisation of plant endoplasmic reticulum. Identification
RT   of protein disulfide-isomerase as the major reticuloplasmin.";
RL   Eur. J. Biochem. 235:215-224(1996).
CC   -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC       bonds, may be involved in glycosylation, prolyl hydroxylation and
CC       triglyceride transfer. {ECO:0000250}.
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:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {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; U41385; AAB05641.1; -; mRNA.
DR   PIR; S62626; S62626.
DR   RefSeq; NP_001310686.1; NM_001323757.1.
DR   AlphaFoldDB; Q43116; -.
DR   SMR; Q43116; -.
DR   STRING; 3988.XP_002513744.1; -.
DR   PRIDE; Q43116; -.
DR   GeneID; 8281065; -.
DR   KEGG; rcu:8281065; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
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; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Redox-active center; Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..498
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034211"
FT   DOMAIN          24..143
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          339..484
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           495..498
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            62
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            63
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            129
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            407
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            408
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            470
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..64
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        406..409
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   498 AA;  55561 MW;  D556492D78F955D5 CRC64;
     MASFRGSIWY CIFVLSLIAV AISAAESEEE QSSVLTLDST NFTDTISKHD FIVVEFYAPW
     CGHCKKLRPE YEKAASILKS HDIPVVLAKV DANEEANKEL ATQYDIKGFP TLKILRNGGK
     SIQEYKGPRE ADGIAEYLKK QSGPASVEIK STEAANTFIG DKKIFIVGVF PKFSGEEYEN
     YMSVADKLRS DYEFGHTLDA KHLPQGESSV TGPVVRLFKP FDELFVDFKD FNVDALEKFV
     EESSMPVVTV FNSDPSNHPF VIKFFNSPDA KAMLFMNFNG EAADSIKSKY QEVAHQFKGE
     GIILLLGDVE ASQGAFQYFG LKEDQVPLII IQTNDGQKYL KANLEPDHIA PWVKAYKEGK
     VQAYRKSEPI PEVNNEPVKV VVADTLQDIV FNSGKNVLLE FYAPWCGHCK QLAPILDEVA
     VSYKSDADIV IAKLDATAND IPSDTFDVRG YPTVYFRSAS GKVEQYDGDR TKDDIISFIE
     KNRDKAAQQE SANGKDEL