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Q43116 (PDI_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length498 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 498475Protein disulfide-isomerase
PRO_0000034211

Regions

Domain24 – 143120Thioredoxin 1
Domain339 – 484146Thioredoxin 2
Motif495 – 4984Prevents secretion from ER By similarity

Sites

Active site611Nucleophile By similarity
Active site641Nucleophile By similarity
Active site4061Nucleophile By similarity
Active site4091Nucleophile By similarity
Site621Contributes to redox potential value By similarity
Site631Contributes to redox potential value By similarity
Site1291Lowers pKa of C-terminal Cys of first active site By similarity
Site4071Contributes to redox potential value By similarity
Site4081Contributes to redox potential value By similarity
Site4701Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 64Redox-active By similarity
Disulfide bond406 ↔ 409Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43116 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D556492D78F955D5

FASTA49855,561
        10         20         30         40         50         60 
MASFRGSIWY CIFVLSLIAV AISAAESEEE QSSVLTLDST NFTDTISKHD FIVVEFYAPW 

        70         80         90        100        110        120 
CGHCKKLRPE YEKAASILKS HDIPVVLAKV DANEEANKEL ATQYDIKGFP TLKILRNGGK 

       130        140        150        160        170        180 
SIQEYKGPRE ADGIAEYLKK QSGPASVEIK STEAANTFIG DKKIFIVGVF PKFSGEEYEN 

       190        200        210        220        230        240 
YMSVADKLRS DYEFGHTLDA KHLPQGESSV TGPVVRLFKP FDELFVDFKD FNVDALEKFV 

       250        260        270        280        290        300 
EESSMPVVTV FNSDPSNHPF VIKFFNSPDA KAMLFMNFNG EAADSIKSKY QEVAHQFKGE 

       310        320        330        340        350        360 
GIILLLGDVE ASQGAFQYFG LKEDQVPLII IQTNDGQKYL KANLEPDHIA PWVKAYKEGK 

       370        380        390        400        410        420 
VQAYRKSEPI PEVNNEPVKV VVADTLQDIV FNSGKNVLLE FYAPWCGHCK QLAPILDEVA 

       430        440        450        460        470        480 
VSYKSDADIV IAKLDATAND IPSDTFDVRG YPTVYFRSAS GKVEQYDGDR TKDDIISFIE 

       490 
KNRDKAAQQE SANGKDEL 

« Hide

References

[1]"Molecular characterisation of plant endoplasmic reticulum. Identification of protein disulfide-isomerase as the major reticuloplasmin."
Coughlan S.J., Hastings C., Winfrey R.J.
Eur. J. Biochem. 235:215-224(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Hale.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41385 mRNA. Translation: AAB05641.1.
PIRS62626.

3D structure databases

ProteinModelPortalQ43116.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43116.
ProMEXQ43116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
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_RICCO
AccessionPrimary (citable) accession number: Q43116
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 95 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