ID   PDI_HORVU               Reviewed;         513 AA.
AC   P80284;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   AltName: Full=Endosperm protein E-1;
DE   Flags: Precursor;
GN   Name=PDI;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Morex; TISSUE=Ovary;
RX   PubMed=7846178; DOI=10.1104/pp.106.4.1705;
RA   Chen F., Hayes P.M.;
RT   "Nucleotide sequence and developmental expression of duplicated genes
RT   encoding protein disulfide isomerase in barley (Hordeum vulgare L.).";
RL   Plant Physiol. 106:1705-1706(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-42.
RC   STRAIN=cv. H354-295-2-5; TISSUE=Starchy endosperm;
RX   PubMed=8125056; DOI=10.1002/elps.11501401169;
RA   Flengsrud R.;
RT   "Separation of acidic barley endosperm proteins by two-dimensional
RT   electrophoresis.";
RL   Electrophoresis 14:1060-1066(1993).
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}.
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DR   EMBL; L33250; AAA70344.1; -; mRNA.
DR   EMBL; L33251; AAA70345.1; -; mRNA.
DR   EMBL; L33252; AAA70346.1; -; mRNA.
DR   PIR; T05974; T05974.
DR   AlphaFoldDB; P80284; -.
DR   SMR; P80284; -.
DR   IntAct; P80284; 1.
DR   ExpressionAtlas; P80284; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009960; P:endosperm development; IEA:EnsemblPlants.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:EnsemblPlants.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Isomerase; Redox-active center; Repeat; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:8125056"
FT   CHAIN           26..513
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034208"
FT   DOMAIN          26..149
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          369..488
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          491..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           510..513
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        67
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        70
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            68
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            69
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            135
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            412
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            413
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            474
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        67..70
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        411..414
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   513 AA;  56463 MW;  03BBAE2EE164F972 CRC64;
     MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAPEAV LTLHADNFDD AIGQHPFILV
     EFYAPWCGHC KSLAPEYEKA AQLLSKHDPA IVLAKVDAND EKNKPLAGKY EVQGFPTLKI
     FRNGGKSIQE YKGPREAEGI VEYLKKQVGP ASKEIKAPED ATYLEDGKIH IVGVFTEFSG
     PEFTNFLEVA EKLRSYYDFG HTVHANHLPR GDAAVERPVV RLFKPFDELV VDSKDFDVSA
     LEKFIDASST PKVVIFDKNP DNHPYLLKFF QSNAPKAMLF LNFSTGPFES FKSAYYGAVE
     EFSGKDVKFL IGDIESSQGA FQYFGLKVDQ APLILIQDGD SKKFLKEHVE AGQIVAWLKD
     YFDGKLTPFR KSEPIPEANN EPVKVVVADN VHDVVFKSGK NVLIEFYAPW CGHCKKLAPI
     LDEAAATLQS EEDVVIAKMD ATENDVPGEF DVQGYPTLYF VTPSGKKVSY EGGRTADEIV
     DYIRKNKETA GQAAAATEKA AEPAATEPLK DEL