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Q8R4U2 (PDIA1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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):
Prolyl 4-hydroxylase subunit beta
p58
Gene names
Name:P4HB
Synonyms:PDIA1
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subunit structure

Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Melanosome By similarity. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.

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 – 1919 By similarity
Chain20 – 509490Protein disulfide-isomerase
PRO_0000034194

Regions

Domain20 – 136117Thioredoxin 1
Domain335 – 477143Thioredoxin 2
Motif506 – 5094Prevents secretion from ER By similarity
Compositional bias482 – 4876Poly-Asp

Sites

Active site551Nucleophile By similarity
Active site581Nucleophile By similarity
Active site3991Nucleophile By similarity
Active site4021Nucleophile By similarity
Site561Contributes to redox potential value By similarity
Site571Contributes to redox potential value By similarity
Site1221Lowers pKa of C-terminal Cys of first active site By similarity
Site4001Contributes to redox potential value By similarity
Site4011Contributes to redox potential value By similarity
Site4631Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2021N6-acetyllysine By similarity
Modified residue2241N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond399 ↔ 402Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R4U2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 9B9B7513DE918194

FASTA50957,010
        10         20         30         40         50         60 
MLSRSLLCLA LAWVARVGAD APEEEDNVLV LKKSNFAEAL AAHNYLLVEF YAPWCGHCKA 

        70         80         90        100        110        120 
LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA 

       130        140        150        160        170        180 
GREADDIVNW LKKRTGPAAT TLSDTAAAET LIDSSEVAVI GFFKDVESDS AKQFLLAAEA 

       190        200        210        220        230        240 
VDDIPFGITS NSGVFSKYQL DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI 

       250        260        270        280        290        300 
EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLGNFKKA AEGFKGKILF IFIDSDHTDN 

       310        320        330        340        350        360 
QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ 

       370        380        390        400        410        420 
ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE 

       430        440        450        460        470        480 
NIIIAKMDST ANEVEAVKVH SFPTLKFFPA TADRTVIDYN GERTLDGFKK FLESGGQDGA 

       490        500 
GDDDDVDLEE ALEPDMEEDD DQKAVKDEL 

« Hide

References

[1]"Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine."
Cai T.-Q., Guo Q., Wong B., Milot D., Zhang L., Wright S.D.
Biochim. Biophys. Acta 1581:100-108(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Small intestine.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF364317 mRNA. Translation: AAM00284.1.
RefSeqNP_001233622.1. NM_001246693.1.

3D structure databases

ProteinModelPortalQ8R4U2.
SMRQ8R4U2. Positions 20-359, 370-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4997811.

Proteomic databases

PRIDEQ8R4U2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689433.
KEGGcge:100689433.

Organism-specific databases

CTD5034.

Phylogenomic databases

HOVERGENHBG005920.
KOK09580.

Family and domain databases

Gene3D3.40.30.10. 4 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 namePDIA1_CRIGR
AccessionPrimary (citable) accession number: Q8R4U2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families