ID   PDI_DATGL               Reviewed;         507 AA.
AC   Q9XF61;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=PDI;
OS   Datisca glomerata (Durango root).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Datiscaceae; Datisca.
OX   NCBI_TaxID=34297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RA   Okubara P.A., Berry A.M.;
RT   "DgPDIa, full-length cDNA from symbiotic root nodules of Datisca glomerata
RT   with homology to protein disulfide isomerase genes.";
RL   (er) Plant Gene Register PGR99-052(1999).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AF131223; AAD28260.1; -; mRNA.
DR   AlphaFoldDB; Q9XF61; -.
DR   SMR; Q9XF61; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW   Redox-active center; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..507
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034207"
FT   DOMAIN          21..144
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          365..485
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          484..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           504..507
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        65
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            63
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            130
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            408
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            409
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            471
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..65
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        407..410
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   507 AA;  57089 MW;  4CE20915BBB2B9D1 CRC64;
     MASMVSFCFL LLFLAFFASS FNEIYAEESE SKEFVLTLDK SNFFDTVSKH NFIVVEFYAP
     WCGHCKKLAP EYEKAASILS SHDPPVILAK VDANEEANKE LASEFEVRGF PTIKILRNGG
     KIVQEYKGPR DADGIVDYLK KQSGPPSAEI KSIEDATNLV SEKKIVVVGI FPKFSGEEFE
     NFSALAEKLR SDYEFGHTLD AKLLPRGESS VSGPVVRLFK PFDELFVDFQ DFDVNALEKL
     VEESSVPTVT IFDKDPSNHP FVVKFFNNAN AKAMLFLNFT SEVVESFRSI YREVAEKNKG
     EGISFLIGDT ESSQGAFQYF GLRDDQVPLI VIQNNDGTKY LKPNLEPDHI ASWVKEYKDC
     KLSPYRKSEP IPEHNNEPVK VVVADSLDEI VFKSGKNVLL EFYAPWCGHC KQLAPILDEV
     AVSFENDPDV LIAKLDATAN DYPTNTFDVK GYPTLYFKSA SGELLQYDGG RTKEDFIEFI
     EKNREKSSKK ESIVKDDQTD SETKAEL