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Q5R5B6 (PDIA1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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):
Cellular thyroid hormone-binding protein
Prolyl 4-hydroxylase subunit beta
p55
Gene names
Name:P4HB
Synonyms:PDIA1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length508 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 – 1717 By similarity
Chain18 – 508491Protein disulfide-isomerase
PRO_0000034197

Regions

Domain18 – 134117Thioredoxin 1
Domain349 – 475127Thioredoxin 2
Motif505 – 5084Prevents secretion from ER By similarity
Compositional bias480 – 4834Poly-Asp

Sites

Active site531Nucleophile By similarity
Active site561Nucleophile By similarity
Active site3971Nucleophile By similarity
Active site4001Nucleophile By similarity
Site541Contributes to redox potential value By similarity
Site551Contributes to redox potential value By similarity
Site1201Lowers pKa of C-terminal Cys of first active site By similarity
Site3981Contributes to redox potential value By similarity
Site3991Contributes to redox potential value By similarity
Site4611Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue2001N6-acetyllysine By similarity
Modified residue2221N6-succinyllysine By similarity
Modified residue2711N6-succinyllysine By similarity
Disulfide bond53 ↔ 56Redox-active By similarity
Disulfide bond397 ↔ 400Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5B6 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 114D79D9BC740400

FASTA50857,033
        10         20         30         40         50         60 
MLRRALLCLA VAGLVCADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA 

        70         80         90        100        110        120 
PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR 

       130        140        150        160        170        180 
EADDIVNWLK KRTGPAATIL PDGAAAESLV ESSEVAVVGF FKDVESDSAK QFLQAAEAID 

       190        200        210        220        230        240 
DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF 

       250        260        270        280        290        300 
TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR 

       310        320        330        340        350        360 
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL 

       370        380        390        400        410        420 
PDDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI 

       430        440        450        460        470        480 
VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD 

       490        500 
DDDLEDLEEA EEPDMEEDDD QKAVKDEL 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860947 mRNA. Translation: CAH93050.1.
RefSeqNP_001126805.1. NM_001133333.1.

3D structure databases

ProteinModelPortalQ5R5B6.
SMRQ5R5B6. Positions 18-357, 368-471.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R5B6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173809.
KEGGpon:100173809.

Organism-specific databases

CTD5034.

Phylogenomic databases

HOVERGENHBG005920.
InParanoidQ5R5B6.
KOK09580.

Family and domain databases

Gene3D3.40.30.10. 4 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...

Entry information

Entry namePDIA1_PONAB
AccessionPrimary (citable) accession number: Q5R5B6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 71 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