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P52589 (PDI_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase

Short name=PDI
EC=5.3.4.1
Gene names
Name:PDI
OrganismTriticum aestivum (Wheat) [Complete proteome]
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity.

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subcellular location

Endoplasmic reticulum lumen Potential.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 515490Protein disulfide-isomerase
PRO_0000034212

Regions

Domain26 – 150125Thioredoxin 1
Domain346 – 489144Thioredoxin 2
Motif512 – 5154Prevents secretion from ER Potential

Sites

Active site681Nucleophile By similarity
Active site711Nucleophile By similarity
Active site4121Nucleophile By similarity
Active site4151Nucleophile By similarity
Site691Contributes to redox potential value By similarity
Site701Contributes to redox potential value By similarity
Site1361Lowers pKa of C-terminal Cys of first active site By similarity
Site4131Contributes to redox potential value By similarity
Site4141Contributes to redox potential value By similarity
Site4751Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation2831N-linked (GlcNAc...) Potential
Disulfide bond68 ↔ 71Redox-active By similarity
Disulfide bond412 ↔ 415Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P52589 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6630AB9A252A96B6

FASTA51556,533
        10         20         30         40         50         60 
MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAAPEA VLTLHADNFD DAIAKHPFIL 

        70         80         90        100        110        120 
VEFYAPWCGH CKSLAPEYEK AAQLLSKHDP AIVLAKVDAN DEKNKPLAGK YEVQGFPTLK 

       130        140        150        160        170        180 
IFRSGGKNIQ EYKGPREAEG IVEYLKKQVG PASKEIKAPE DATYLEDGKI HIVGVFTEFS 

       190        200        210        220        230        240 
GTEFTNFLEL AEKLRSDYDF GHTVHANHLP RGDAAVERPL VRLFKPFDEL VVDSKDFDVS 

       250        260        270        280        290        300 
ALEKFIDASS TPKVVTFDKN PDNHPYLLKY FQSNAPKAML FLNFSTGPFE SFKSAYYGAV 

       310        320        330        340        350        360 
EEFSGKDVKF LIGDIEASQG AFQYNGLKED QAPLILIQDS DSKKFLKEQV EAGQIVAWLK 

       370        380        390        400        410        420 
DYFDGKLTPF RKSEPIPEAN NEPVKVVVAD NIHDVVFKSA KNVLIEFYAP WCGHCKKLAP 

       430        440        450        460        470        480 
ILDEAAATLQ SEEDVVIAKI DATANDVPGE FDVQGYPTLY FVTPSGKKVS YEGGRTADEI 

       490        500        510 
VDYIKKNKET AGQAAAAATE KAAEPAATEP LKDEL 

« Hide

References

[1]"Nucleotide sequence of a wheat cDNA encoding protein disulfide isomerase."
Shimoni Y., Segal G., Zhu X.Z., Galili G.
Plant Physiol. 107:281-281(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Chinese Spring.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11496 mRNA. Translation: AAA19660.1.
PIRT06262.
UniGeneTa.2019.

3D structure databases

ProteinModelPortalP52589.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP52589.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI_WHEAT
AccessionPrimary (citable) accession number: P52589
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families