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 27-MAR-2024, entry version 123. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U11496; AAA19660.1; -; mRNA. DR PIR; T06262; T06262. DR AlphaFoldDB; P52589; -. DR SMR; P52589; -. DR STRING; 4565.P52589; -. DR GlyCosmos; P52589; 1 site, No reported glycans. DR PaxDb; 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 CDD; cd02961; PDI_a_family; 1. DR CDD; cd02995; PDI_a_PDI_a'_C; 1. DR CDD; cd02982; PDI_b'_family; 1. DR CDD; cd02981; PDI_b_family; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 4. DR InterPro; IPR005788; PDI_thioredoxin-like_dom. DR InterPro; IPR005792; Prot_disulphide_isomerase. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01130; ER_PDI_fam; 1. DR NCBIfam; TIGR01126; pdi_dom; 2. DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1. DR PANTHER; PTHR18929:SF254; PROTEIN DISULFIDE ISOMERASE-LIKE 1-1; 1. DR Pfam; PF00085; Thioredoxin; 2. DR Pfam; PF13848; Thioredoxin_6; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 4. 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 //