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P80284 (PDI_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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
Alternative name(s):
Endosperm protein E-1
Gene names
Name:PDI
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

embryo development

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

regulation of programmed cell death

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to zinc ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

seed development

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

lytic vacuole within protein storage vacuole

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plant-type cell wall

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasma membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

thylakoid

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

vacuolar membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionprotein disulfide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.2
Chain26 – 513488Protein disulfide-isomerase
PRO_0000034208

Regions

Domain26 – 149124Thioredoxin 1
Domain369 – 488120Thioredoxin 2
Motif510 – 5134Prevents secretion from ER Potential

Sites

Active site671Nucleophile By similarity
Active site701Nucleophile By similarity
Active site4111Nucleophile By similarity
Active site4141Nucleophile By similarity
Site681Contributes to redox potential value By similarity
Site691Contributes to redox potential value By similarity
Site1351Lowers pKa of C-terminal Cys of first active site By similarity
Site4121Contributes to redox potential value By similarity
Site4131Contributes to redox potential value By similarity
Site4741Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation2821N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 70Redox-active By similarity
Disulfide bond411 ↔ 414Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P80284 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 03BBAE2EE164F972

FASTA51356,463
        10         20         30         40         50         60 
MAISKVWISL LLALAVVLSA PAARAEEAAA AEEAAAPEAV LTLHADNFDD AIGQHPFILV 

        70         80         90        100        110        120 
EFYAPWCGHC KSLAPEYEKA AQLLSKHDPA IVLAKVDAND EKNKPLAGKY EVQGFPTLKI 

       130        140        150        160        170        180 
FRNGGKSIQE YKGPREAEGI VEYLKKQVGP ASKEIKAPED ATYLEDGKIH IVGVFTEFSG 

       190        200        210        220        230        240 
PEFTNFLEVA EKLRSYYDFG HTVHANHLPR GDAAVERPVV RLFKPFDELV VDSKDFDVSA 

       250        260        270        280        290        300 
LEKFIDASST PKVVIFDKNP DNHPYLLKFF QSNAPKAMLF LNFSTGPFES FKSAYYGAVE 

       310        320        330        340        350        360 
EFSGKDVKFL IGDIESSQGA FQYFGLKVDQ APLILIQDGD SKKFLKEHVE AGQIVAWLKD 

       370        380        390        400        410        420 
YFDGKLTPFR KSEPIPEANN EPVKVVVADN VHDVVFKSGK NVLIEFYAPW CGHCKKLAPI 

       430        440        450        460        470        480 
LDEAAATLQS EEDVVIAKMD ATENDVPGEF DVQGYPTLYF VTPSGKKVSY EGGRTADEIV 

       490        500        510 
DYIRKNKETA GQAAAATEKA AEPAATEPLK DEL 

« Hide

References

[1]"Nucleotide sequence and developmental expression of duplicated genes encoding protein disulfide isomerase in barley (Hordeum vulgare L.)."
Chen F., Hayes P.M.
Plant Physiol. 106:1705-1706(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Morex.
Tissue: Ovary.
[2]"Separation of acidic barley endosperm proteins by two-dimensional electrophoresis."
Flengsrud R.
Electrophoresis 14:1060-1066(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-42.
Strain: cv. H354-295-2-5.
Tissue: Starchy endosperm.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33250 mRNA. Translation: AAA70344.1.
L33251 mRNA. Translation: AAA70345.1.
L33252 mRNA. Translation: AAA70346.1.
PIRT05974.

3D structure databases

ProteinModelPortalP80284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP80284. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP80284.

Gene expression databases

GenevestigatorP80284.

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_HORVU
AccessionPrimary (citable) accession number: P80284
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 94 of the entry and version 2 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