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Q00002 (PDI_ALTAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Allergen=Alt a 4
OrganismAlternaria alternata (Alternaria rot fungus) (Torula alternata)
Taxonomic identifier5599 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeAlternariaAlternaria alternata group

Protein attributes

Sequence length436 AA.
Sequence statusFragment.
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 By similarity.

Allergenic properties

Causes an allergic reaction in human. Ref.1

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains at least 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DiseaseAllergen
   DomainRedox-active center
   Molecular functionIsomerase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein disulfide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 436›436Protein disulfide-isomerase
PRO_0000120175

Regions

Domain216 – 365150Thioredoxin
Motif433 – 4364Prevents secretion from ER Potential
Compositional bias362 – 43170Ser-rich

Sites

Active site2661Nucleophile By similarity
Active site2691Nucleophile By similarity
Site2671Contributes to redox potential value By similarity
Site2681Contributes to redox potential value By similarity

Amino acid modifications

Disulfide bond266 ↔ 269Redox-active By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q00002 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: ECBB7D93738BCEE3

FASTA43646,275
        10         20         30         40         50         60 
ARDMTKQALP AVSEVTKDTL EEFKTADKVV LVAYFAADDK ASNETFTSVA NGLRDNFLFG 

        70         80         90        100        110        120 
ATNDAALAKA EGVKQPGLVC TSPSTTARTS SPRPSMRTYP RLRKVASTPL IGEVGPETYA 

       130        140        150        160        170        180 
GYMAAGIPLA YIFAETPEER EEFAKELKPL ALKHKGEINF ATIDAKSFGQ HAGNLNLKVG 

       190        200        210        220        230        240 
TWPAFAIQRT EKNEKFPTNQ EAKITEKEIG KFVDDFLAGK IDPSIKSEPI PESNDGPVTV 

       250        260        270        280        290        300 
VVAHNYKDVV IDNDKDVLVE FYAPWCGHCK ALAPKYEELG QLYASDELSK LVTIAKVDAT 

       310        320        330        340        350        360 
LNDVPDEIQG FLPSSLFPLA RRMPQSTTLV PHCRGSRPVH RRERLTQASA SVGEAVEDAT 

       370        380        390        400        410        420 
ESAKASASSA TDSAASAVSE GTETVKSGAS VASDSASSAA SEATKSVKSA ASEVTNSASS 

       430 
AASEASASAS SVKDEL 

« Hide

References

[1]"Molecular characterization of Alternaria alternata and Cladosporium herbarum allergens."
Achatz G., Oberkofler H., Lechenauer E., Simon B., Unger A., Kandler D., Ebner C., Prillinger H., Kraft D., Breitenbach M.
Adv. Exp. Med. Biol. 409:157-161(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.
[2]Unger A.M., Lechenauer E., Simon B., Oberkofler H., Probst G., Achatz G., Breitenbach M.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 08-0203-Berlin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84217 mRNA. Translation: CAA58999.1.
U82634 mRNA. Translation: AAB40401.1.

3D structure databases

ProteinModelPortalQ00002.
SMRQ00002. Positions 108-318.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome18. Alt a 4.
3061. Alt a 4.0101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI_ALTAL
AccessionPrimary (citable) accession number: Q00002
Secondary accession number(s): P87325
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Allergens

Nomenclature of allergens and list of entries