ID   PDI_MAIZE               Reviewed;         513 AA.
AC   P52588;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=PDI;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 64A; TISSUE=Endosperm;
RX   PubMed=8639747; DOI=10.1007/bf00020800;
RA   Li C.P., Larkins B.A.;
RT   "Expression of protein disulfide isomerase is elevated in the endosperm of
RT   the maize floury-2 mutant.";
RL   Plant Mol. Biol. 30:873-882(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}.
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DR   EMBL; L39014; AAB08519.1; -; mRNA.
DR   PIR; S69181; S69181.
DR   AlphaFoldDB; P52588; -.
DR   SMR; P52588; -.
DR   STRING; 4577.GRMZM2G091481_P01; -.
DR   PaxDb; P52588; -.
DR   PRIDE; P52588; -.
DR   MaizeGDB; 86830; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P52588; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..513
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034210"
FT   DOMAIN          24..145
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          366..485
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          485..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        63
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            65
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            131
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            409
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            410
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        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..66
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        408..411
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   513 AA;  57097 MW;  29302DD01A3DEB80 CRC64;
     MAIRSKAWIS LLLALAVALS ARAEEEPAAA AEGEAVLTLD VDSFDEAVAK HPFMVVEFYA
     PWCGHCKKLA PEYENAAKAL SKHDPPIVLA KVDANEEKNR PLATKYEIQG FPTIKIFRDR
     GKNIQEYKGP READGIVDYL KKQVGPASKE IKSPEDATAL IDDKKIYIVG IFAEFSGTEF
     TNFMEVAEKL RSDYDFGHTL HANHLPRGDA AVERPLVRLL KPFDELVVDS KDFDVAALMK
     FIDASTIPRV VTFDKNPDNH PYLMKFFQSS APKAMLFLNF STGPFDSFKS AYSAAAEEFK
     DKEIKFLIGD IEASQGAFQY FGLKEDQTPL ILIQDGDSKK FLKVHVEADQ IVAWLKEYFD
     GKLTPFRNSE PIPEVNNEPV KVVVADNVHD FVFKSGKNVL IEFYAPWCGH CKKLAPILDE
     AATTLQSDEE VVIAKMDATA NDVPSEFDVQ GYPTLYFVTP SGKVTSYDSG RTADDIVDFI
     KKSKETAAPH HHHHPGATGI REGSRAEPVK DEL