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   16-JUN-2009, entry version 68.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC   Acalypheae; Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hale;
RX   MEDLINE=96202938; PubMed=8631332;
RX   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.
RT   Identification of protein disulfide-isomerase as the major
RT   reticuloplasmin.";
RL   Eur. J. Biochem. 235:215-224(1996).
CC   -!- FUNCTION: Participates in the folding of proteins containing
CC       disulfide bonds, may be involved in glycosylation, prolyl
CC       hydroxylation and triglyceride transfer (By similarity).
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (Potential).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
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DR   EMBL; U41385; AAB05641.1; -; mRNA.
DR   PIR; S62626; S62626.
DR   HSSP; P07237; 1MEK.
DR   BRENDA; 5.3.4.1; 816.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR006662; Thioredoxin-like_subdom.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
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       Potential.
FT   CHAIN        24    498       Protein disulfide-isomerase.
FT                                /FTId=PRO_0000034211.
FT   DOMAIN       24    143       Thioredoxin 1.
FT   DOMAIN      339    484       Thioredoxin 2.
FT   MOTIF       495    498       Prevents secretion from ER (By
FT                                similarity).
FT   ACT_SITE     61     61       Nucleophile (By similarity).
FT   ACT_SITE     64     64       Nucleophile (By similarity).
FT   ACT_SITE    406    406       Nucleophile (By similarity).
FT   ACT_SITE    409    409       Nucleophile (By similarity).
FT   SITE         62     62       Contributes to redox potential value (By
FT                                similarity).
FT   SITE         63     63       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        129    129       Lowers pKa of C-terminal Cys of first
FT                                active site (By similarity).
FT   SITE        407    407       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        408    408       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        470    470       Lowers pKa of C-terminal Cys of second
FT                                active site (By similarity).
FT   CARBOHYD     41     41       N-linked (GlcNAc...) (Potential).
FT   DISULFID     61     64       Redox-active (By similarity).
FT   DISULFID    406    409       Redox-active (By similarity).
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
//