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Q63081 (PDIA6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. 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 A6

EC=5.3.4.1
Alternative name(s):
Calcium-binding protein 1
Short name=CaBP1
Protein disulfide isomerase P5
Thioredoxin domain-containing protein 7
Gene names
Name:Pdia6
Synonyms:Cabp1, Txndc7
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length440 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.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence caution

The sequence AAH82063.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   DomainRedox-active center
Repeat
Signal
   LigandCalcium
   Molecular functionChaperone
Isomerase
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

platelet activation

Inferred from sequence or structural similarity. Source: UniProtKB

platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to endoplasmic reticulum stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentendoplasmic reticulum lumen

Inferred from direct assay PubMed 14561759. Source: HGNC

endoplasmic reticulum-Golgi intermediate compartment

Traceable author statement Ref.2. Source: RGD

melanosome

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

smooth endoplasmic reticulum

Inferred from direct assay PubMed 22665516. Source: UniProtKB

   Molecular_functioncalcium ion binding

Traceable author statement Ref.2. Source: RGD

protein disulfide isomerase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 440421Protein disulfide-isomerase A6
PRO_0000034240

Regions

Domain21 – 133113Thioredoxin 1
Domain151 – 287137Thioredoxin 2
Motif437 – 4404Prevents secretion from ER By similarity
Compositional bias422 – 43615Asp/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 residue4281Phosphoserine By similarity
Disulfide bond55 ↔ 58Redox-active By similarity
Disulfide bond190 ↔ 193Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63081 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 8D388E4FFD743719

FASTA44048,173
        10         20         30         40         50         60 
MARLVLGLVS CTFFLAVSAL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR 

        70         80         90        100        110        120 
LTPEWKKAAS ALKDVVKVGA VNADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG 

       130        140        150        160        170        180 
EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRGDSSSKK DVVELTDDTF DKNVLDSEDV 

       190        200        210        220        230        240 
WMVEFYAPWC GHCKNLEPEW AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI 

       250        260        270        280        290        300 
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA 

       310        320        330        340        350        360 
VLPHILDTGA TGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG IGGFGYPAMA 

       370        380        390        400        410        420 
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GSFPNITPRE PWDGKDGELP 

       430        440 
VEDDIDLSDV ELDDLEKDEL 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[2]"CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment."
Fuellekrug J., Soennichsen B., Wuensch U., Arseven K., Van P.N., Soeling H.-D., Mieskes G.
J. Cell Sci. 107:2719-2727(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-440.
Strain: Wistar.
Tissue: Liver.
[3]Lubec G., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 119-132; 217-231 AND 314-322, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC082063 mRNA. Translation: AAH82063.1. Different initiation.
X79328 mRNA. Translation: CAA55891.1.
PIRS45038.
RefSeqNP_001004442.1. NM_001004442.1.
UniGeneRn.2685.

3D structure databases

ProteinModelPortalQ63081.
SMRQ63081. Positions 20-132, 154-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid251898. 1 interaction.
IntActQ63081. 4 interactions.
MINTMINT-1775443.

PTM databases

PhosphoSiteQ63081.

Proteomic databases

PRIDEQ63081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000074829; ENSRNOP00000064632; ENSRNOG00000050197.
GeneID286906.
KEGGrno:286906.

Organism-specific databases

CTD10130.
RGD628688. Pdia6.

Phylogenomic databases

GeneTreeENSGT00730000110455.
HOVERGENHBG053548.
KOK09584.
OrthoDBEOG7XDBFV.
PhylomeDBQ63081.

Gene expression databases

GenevestigatorQ63081.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR005788. Disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 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...

Other

NextBio625007.

Entry information

Entry namePDIA6_RAT
AccessionPrimary (citable) accession number: Q63081
Secondary accession number(s): Q641Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 29, 2005
Last modified: June 11, 2014
This is version 115 of the entry and version 2 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