ID Q93XQ7_WHEAT Unreviewed; 515 AA.
AC Q93XQ7;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE Flags: Precursor;
GN Name=PDI3 {ECO:0000313|EMBL:AAK49425.1};
GN Synonyms=PDI {ECO:0000313|EMBL:CAI30634.1};
GN ORFNames=CFC21_060955 {ECO:0000313|EMBL:KAF7052936.1};
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 {ECO:0000313|EMBL:AAK49425.1};
RN [1] {ECO:0000313|EMBL:AAK49425.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Endosperm {ECO:0000313|EMBL:AAK49425.1};
RX AGRICOLA=IND23239870; DOI=10.1006/jcrs.2001.0382;
RA Johnson J.C., Clarke B.C., Bhave M.;
RT "Isolation and characterisation of cDNAs encoding protein disulphide
RT isomerases and cyclophilins in wheat.";
RL J. Cereal Sci. 34:159-171(2001).
RN [2] {ECO:0000313|EMBL:CAI30634.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:CAI30634.1};
RX PubMed=16289628; DOI=10.1016/j.gene.2005.07.032;
RA Ciaffi M., Paolacci A.R., D'Aloisio E., Tanzarella O.A., Porceddu E.;
RT "Cloning and characterization of wheat PDI (protein disulfide isomerase)
RT homoeologous genes and promoter sequences.";
RL Gene 366:209-218(2006).
RN [3] {ECO:0000313|EMBL:KAF7052936.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7052936.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [4] {ECO:0000313|EnsemblPlants:TraesCS4D02G098400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4D02G098400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [5] {ECO:0000313|EnsemblPlants:TraesCS4D02G098400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [6] {ECO:0000313|EMBL:KAF7052936.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7052936.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; AF262981; AAK49425.1; -; mRNA.
DR EMBL; AJ868104; CAI30634.1; -; Genomic_DNA.
DR EMBL; AJ868107; CAI30637.1; -; mRNA.
DR EMBL; CM022222; KAF7052936.1; -; Genomic_DNA.
DR SMR; Q93XQ7; -.
DR STRING; 4565.Q93XQ7; -.
DR EnsemblPlants; TraesCS4D02G098400.1; TraesCS4D02G098400.1; TraesCS4D02G098400.
DR Gramene; TraesCAD_scaffold_044799_01G000100.1; TraesCAD_scaffold_044799_01G000100.1; TraesCAD_scaffold_044799_01G000100.
DR Gramene; TraesCLE_scaffold_039740_01G000100.1; TraesCLE_scaffold_039740_01G000100.1; TraesCLE_scaffold_039740_01G000100.
DR Gramene; TraesCS4D02G098400.1; TraesCS4D02G098400.1; TraesCS4D02G098400.
DR Gramene; TraesCS4D03G0194000.1; TraesCS4D03G0194000.1.CDS; TraesCS4D03G0194000.
DR Gramene; TraesKAR4D01G0056860.1; cds.TraesKAR4D01G0056860.1; TraesKAR4D01G0056860.
DR Gramene; TraesPAR_scaffold_042093_01G000100.1; TraesPAR_scaffold_042093_01G000100.1; TraesPAR_scaffold_042093_01G000100.
DR Gramene; TraesROB_scaffold_026554_01G000200.1; TraesROB_scaffold_026554_01G000200.1; TraesROB_scaffold_026554_01G000200.
DR Gramene; TraesWEE_scaffold_041505_01G000100.1; TraesWEE_scaffold_041505_01G000100.1; TraesWEE_scaffold_041505_01G000100.
DR HOGENOM; CLU_025879_6_1_1; -.
DR OMA; FFGMKKD; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000019116; Chromosome 4D.
DR Proteomes; UP000815260; Chromosome 4D.
DR ExpressionAtlas; Q93XQ7; 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; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 26..515
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5015020141"
FT DOMAIN 14..150
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 346..489
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 68..71
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 412..415
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 515 AA; 56629 MW; EFD9E2EE149939D3 CRC64;
MAICKAWISL LLALAVVLSA PAARAEEAAA AAEEAAAPEA VLTLHADNFD DAIAKHPFIL
VEFYAPWCGH CKSLAPEYEK AAQLLSKHDP AIVLAKVDAN DEKNKPLAGK YEVQGFPTLK
IFRNGGKNIQ EYKGPREAEG IVEYLKKQVG PASKEIKAPE DATYLEDGKI HIVGVFTEFS
GTEFTNFLEV AEKLRSDYDF GHTVHANHLP RGDAAVERPL VRLFKPFDEL VVDSKDFDVS
ALEKFIDASS TPKVVTFDKN PDNHPYLLKF FQTNAPKAML FLNFSTGPFE SFKSAYYGAV
EEFSGKDVKF LIGDIEASQG AFQYFGLKED QAPLILIQDS DSKKFLKEQV EAGQIVAWLK
DYFDGKLTPF RKSEPIPEAN NEPVKVVVAD NVHDVVFKSG KNVLIEFYAP WCGHCKKLAP
ILDEAAATLQ SEEDVVIAKM DATANDVPSE FDVQGYPTLY FVTPSGKKVS YEGGRTADEI
VDYIKKNKET AGQAAAADTE KAAEPAATEP LKDEL
//
