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P55059 (PDI_HUMIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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
OrganismHumicola insolens (Soft-rot fungus)
Taxonomic identifier34413 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Protein attributes

Sequence length505 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 By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 505485Protein disulfide-isomerase
PRO_0000034215

Regions

Domain21 – 128108Thioredoxin 1
Domain335 – 465131Thioredoxin 2
Motif502 – 5054Prevents secretion from ER Potential

Sites

Active site501Nucleophile By similarity
Active site531Nucleophile By similarity
Active site3851Nucleophile By similarity
Active site3881Nucleophile By similarity
Site511Contributes to redox potential value By similarity
Site521Contributes to redox potential value By similarity
Site1131Lowers pKa of C-terminal Cys of first active site By similarity
Site3861Contributes to redox potential value By similarity
Site3871Contributes to redox potential value By similarity
Site4511Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond50 ↔ 53Redox-active By similarity
Disulfide bond385 ↔ 388Redox-active By similarity

Secondary structure

................................................. 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55059 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 27E7C0D1A61B5F95

FASTA50555,114
        10         20         30         40         50         60 
MHKAQKFALG LLAAAAVATA SDVVQLKKDT FDDFIKTNDL VLAEFFAPWC GHCKALAPEY 

        70         80         90        100        110        120 
EEAATTLKEK NIKLAKVDCT EETDLCQQHG VEGYPTLKVF RGLDNVSPYK GQRKAAAITS 

       130        140        150        160        170        180 
YMIKQSLPAV SEVTKDNLEE FKKADKAVLV AYVDASDKAS SEVFTQVAEK LRDNYPFGSS 

       190        200        210        220        230        240 
SDAALAEAEG VKAPAIVLYK DFDEGKAVFS EKFEVEAIEK FAKTGATPLI GEIGPETYSD 

       250        260        270        280        290        300 
YMSAGIPLAY IFAETAEERK ELSDKLKPIA EAQRGVINFG TIDAKAFGAH AGNLNLKTDK 

       310        320        330        340        350        360 
FPAFAIQEVA KNQKFPFDQE KEITFEAIKA FVDDFVAGKI EPSIKSEPIP EKQEGPVTVV 

       370        380        390        400        410        420 
VAKNYNEIVL DDTKDVLIEF YAPWCGHCKA LAPKYEELGA LYAKSEFKDR VVIAKVDATA 

       430        440        450        460        470        480 
NDVPDEIQGF PTIKLYPAGA KGQPVTYSGS RTVEDLIKFI AENGKYKAAI SEDAEETSSA 

       490        500 
TETTTETATK SEEAAKETAT EHDEL 

« Hide

References

[1]"Molecular cloning of a fungal cDNA encoding protein disulfide isomerase."
Kajino T., Sarai K., Imaeda T., Idekoba C., Asami O., Yamada Y., Hirai M., Udaka S.
Biosci. Biotechnol. Biochem. 58:1424-1429(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KASI.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74296 mRNA. Translation: AAC60578.1.
PIRJC2291.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJJNMR-A354-469[»]
2DJKNMR-A228-355[»]
2KP1NMR-A354-469[»]
2KP2NMR-A228-355[»]
ProteinModelPortalP55059.
SMRP55059. Positions 226-469.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP55059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP55059.

Entry information

Entry namePDI_HUMIN
AccessionPrimary (citable) accession number: P55059
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 84 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references