PDI_WHEAT
ID PDI_WHEAT Reviewed; 515 AA.
AC P52589;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=PDI;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=7870823; DOI=10.1104/pp.107.1.281;
RA Shimoni Y., Segal G., Zhu X.Z., Galili G.;
RT "Nucleotide sequence of a wheat cDNA encoding protein disulfide
RT isomerase.";
RL Plant Physiol. 107:281-281(1995).
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; U11496; AAA19660.1; -; mRNA.
DR PIR; T06262; T06262.
DR AlphaFoldDB; P52589; -.
DR SMR; P52589; -.
DR STRING; 4565.Traes_4DS_26272902A.1; -.
DR eggNOG; KOG0190; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P52589; 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..25
FT /evidence="ECO:0000250"
FT CHAIN 26..515
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034212"
FT DOMAIN 26..150
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 346..489
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 512..515
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 68
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 69
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 70
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 136
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 413
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 414
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 475
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..71
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 412..415
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 515 AA; 56533 MW; 6630AB9A252A96B6 CRC64;
MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAAPEA VLTLHADNFD DAIAKHPFIL
VEFYAPWCGH CKSLAPEYEK AAQLLSKHDP AIVLAKVDAN DEKNKPLAGK YEVQGFPTLK
IFRSGGKNIQ EYKGPREAEG IVEYLKKQVG PASKEIKAPE DATYLEDGKI HIVGVFTEFS
GTEFTNFLEL AEKLRSDYDF GHTVHANHLP RGDAAVERPL VRLFKPFDEL VVDSKDFDVS
ALEKFIDASS TPKVVTFDKN PDNHPYLLKY FQSNAPKAML FLNFSTGPFE SFKSAYYGAV
EEFSGKDVKF LIGDIEASQG AFQYNGLKED QAPLILIQDS DSKKFLKEQV EAGQIVAWLK
DYFDGKLTPF RKSEPIPEAN NEPVKVVVAD NIHDVVFKSA KNVLIEFYAP WCGHCKKLAP
ILDEAAATLQ SEEDVVIAKI DATANDVPGE FDVQGYPTLY FVTPSGKKVS YEGGRTADEI
VDYIKKNKET AGQAAAAATE KAAEPAATEP LKDEL
