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Q12730 (PDI_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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:pdiA
Synonyms:pdi1
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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 By similarity.

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
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_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein disulfide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 515495Protein disulfide-isomerase
PRO_0000034213

Regions

Domain21 – 132112Thioredoxin 1
Domain339 – 470132Thioredoxin 2
Motif512 – 5154Prevents secretion from ER Potential

Sites

Active site541Nucleophile By similarity
Active site571Nucleophile By similarity
Active site3891Nucleophile By similarity
Active site3921Nucleophile By similarity
Site551Contributes to redox potential value By similarity
Site561Contributes to redox potential value By similarity
Site1171Lowers pKa of C-terminal Cys of first active site By similarity
Site3901Contributes to redox potential value By similarity
Site3911Contributes to redox potential value By similarity
Site4561Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond54 ↔ 57Redox-active By similarity
Disulfide bond389 ↔ 392Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12730 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2B0058B788400AD9

FASTA51556,292
        10         20         30         40         50         60 
MRSFAPWLVS LLGASAVVAA ADTESDVISL DQDTFESFMN EHGLVLAEFF APWCGHCKAL 

        70         80         90        100        110        120 
APKYEEAATE LKAKNIPLVK VDCTAEEDLC RSQGVEGYPT LKIFRGVDSS KPYQGARQTE 

       130        140        150        160        170        180 
SIVSYMIKQS LPAVSSVNEE NLEEIKTMDK IVVIGYIPSD DQETYQAFEK YAESQRDNYL 

       190        200        210        220        230        240 
FAATDDAAIA KSEGVEQPSI VLYKDFDEKK AVYDGEIEQE AIHSWVKSAS TPLVGEIGPE 

       250        260        270        280        290        300 
TYSGYIGAGV PLAYIFAETK EEREKYTEDF KPIAQKHKGA INIATIDAKM FGAHAGNLNL 

       310        320        330        340        350        360 
DSQKFPAFAI QDPAKNAKYP YDQAKELNAD EVEKFIQDVL DGKVEPSIKS EPVPESQEGP 

       370        380        390        400        410        420 
VTVVVAHSYK DLVIDNDKDV LLEFYAPWCG HCKALAPKYD ELAALYADHP DLAAKVTIAK 

       430        440        450        460        470        480 
IDATANDVPD PITGFPTLRL YPAGAKDSPI EYSGSRTVED LANFVKENGK HNVDALNVAS 

       490        500        510 
EETQEGGDVT EAAPSATEAE TPAATDDEKA EHDEL 

« Hide

References

[1]"Isolation and characterisation of a gene encoding protein disulphide isomerase, pdiA, from Aspergillus niger."
Ngiam C., Jeenes D.J., Archer D.B.
Curr. Genet. 31:133-138(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]Malpricht S.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98797 Genomic DNA. Translation: CAA67332.1.
X89449 mRNA. Translation: CAA61619.1.
PIRS57942.

3D structure databases

ProteinModelPortalQ12730.
SMRQ12730. Positions 231-471.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0526.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR001393. Calsequestrin.
IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00312. CALSEQUESTRN.
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI_ASPNG
AccessionPrimary (citable) accession number: Q12730
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 85 of the entry and version 1 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