Skip Header

Contribute Send feedback
Read comments (?) or add your own

P38660 (PDIA6_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. 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
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 A6
EC=5.3.4.1
Alternative name(s):
Protein disulfide isomerase P5
Gene names
Name:PDIA6
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin By similarity.

Catalytic activity

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

Subunit structure

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with ITGB3 following platelet stimulation By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Cell membrane By similarity. Melanosome By similarity.

Tissue specificity

Expressed most abundantly in lung and kidney, followed by heart, liver and brain.

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 Ref.1
Chain20 – 439420Protein disulfide-isomerase A6
PRO_0000034237

Regions

Domain20 – 133114Thioredoxin 1
Domain151 – 287137Thioredoxin 2
Motif436 – 4394Prevents secretion from ER By similarity
Compositional bias421 – 43515Asp/Glu-rich (acidic)

Sites

Active site551Nucleophile By similarity
Active site581Nucleophile By similarity
Active site1901Nucleophile By similarity
Active site1931Nucleophile By similarity
Site561Contributes to redox potential value By similarity
Site571Contributes to redox potential value By similarity
Site1181Lowers pKa of C-terminal Cys of first active site By similarity
Site1911Contributes to redox potential value By similarity
Site1921Contributes to redox potential value By similarity
Site2561Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Modified residue4271Phosphoserine By similarity
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond190 ↔ 193Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P38660 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E24CAECF5FFF5F8D

FASTA43948,161
        10         20         30         40         50         60 
MARLGFGLVS CTFFLAASGL YSSSDDVIEL TPSNFNREVI QSNSLWLVEF YAPWCGHCQR 

        70         80         90        100        110        120 
LTPEWKKAAT ALKDVVKVGA VDADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG 

       130        140        150        160        170        180 
EAIVDAALSA LRQLVKDRLS GRSGGYSSGK QGRGDSSSKK DVIELTDDTF DKNVLDSDDV 

       190        200        210        220        230        240 
WMVEFYAPWC GHCKNLEPEW ATAATEVKEQ TKGKVKLAAV DATVNQVLAN RYGIRGFPTI 

       250        260        270        280        290        300 
KIFQKGEAPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDVAKKM CEEHQLCVVA 

       310        320        330        340        350        360 
VLPHILDTGA ARNSYLEILL KLADKYKKKM WGWLWTEAGA QSELENALGI GGFGYPAMAR 

       370        380        390        400        410        420 
INARKMKFAL LKGSFSEQGI NEFLRELSFG RASTAPVGGG SFPAITAREP WDGRDGELPV 

       430 
EDDIDLSDVE LDDLEKDEL

« Hide

References

[1]"The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells."
Chaudhuri M.M., Tonin P.N., Lewis W.H., Srinivasan P.R.
Biochem. J. 281:645-650(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-43.
[2]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X62678 mRNA. Translation: CAA44550.1.
PIRS19656.

3D structure databases

ProteinModelPortalP38660.
SMRP38660. Positions 20-132, 154-280.
ModBaseSearch...

Proteomic databases

PRIDEP38660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG053548.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR005788. 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. Thiordxn-like_fd. 3 hits.
TIGRFAMsTIGR01126. 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 namePDIA6_MESAU
AccessionPrimary (citable) accession number: P38660
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 89 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents