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D3Z6P0 (PDIA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase A2

EC=5.3.4.1
Alternative name(s):
PDIp
Gene names
Name:Pdia2
Synonyms:Pdip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins By similarity. UniProtKB Q13087

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 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity UniProtKB Q13087.

Tissue specificity

Highly expressed in pancreas. Ref.3

Post-translational modification

Glycosylated. Ref.3

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: D3Z6P0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.2 (identifier: D3Z6P0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     184-186: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 527507Protein disulfide-isomerase A2
PRO_0000394671

Regions

Domain29 – 155127Thioredoxin 1
Domain355 – 499145Thioredoxin 2
Motif524 – 5274Prevents secretion from ER Potential

Sites

Active site741Nucleophile By similarity UniProtKB P07237
Active site771Nucleophile By similarity UniProtKB P07237
Active site4211Nucleophile By similarity UniProtKB Q13087
Active site4241Nucleophile By similarity UniProtKB Q13087
Site751Contributes to redox potential value By similarity UniProtKB Q13087
Site761Contributes to redox potential value By similarity UniProtKB Q13087
Site4221Contributes to redox potential value By similarity UniProtKB Q13087
Site4231Contributes to redox potential value By similarity UniProtKB Q13087
Site4851Lowers pKa of C-terminal Cys of second active site By similarity UniProtKB Q13087

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Disulfide bond74 ↔ 77Redox-active By similarity UniProtKB Q13087
Disulfide bond421 ↔ 424Redox-active By similarity UniProtKB Q13087

Natural variations

Alternative sequence184 – 1863Missing in isoform 2. Ref.2
VSP_039293

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: CF703D296B634441

FASTA52758,316
        10         20         30         40         50         60 
MDKQLLPVLL LLLGVSGSWG QGEEPGGPSE VLPEEPTGEE VPKEDGILVL NHRTLSLALQ 

        70         80         90        100        110        120 
EHSALMVEFY APWCGHCKEL APEYSKAAAL LAAESAVVTL AKVDGPAEPE LTKEFEVVGY 

       130        140        150        160        170        180 
PTLKFFQNGN RTNPEEYAGP KTAEGIAEWL RRRVGPSATH LEDEEGVQAL MAKWDMVVIG 

       190        200        210        220        230        240 
FFQDLQGKDM ATFLALAKDA LDMTFGFTDQ PQLFEKFGLT KDTVVLFKKF DEGRADFPVD 

       250        260        270        280        290        300 
KETGLDLGDL SRFLVIHSMH LVTEFNSQTS PKIFAAKILN HLLLFVNQTL AQHRELLTDF 

       310        320        330        340        350        360 
REAAPPFRGQ VLFVMVDVAA DNSHVLNYFG LKAEEAPTLR LINVETTKKY APTGVIAITA 

       370        380        390        400        410        420 
ASVAAFCQAV LHGEIKHYLL SQEIPPDWDQ GPVKTLVSKN FEQVAFDETK NVFVKFYAPW 

       430        440        450        460        470        480 
CSHCKEMAPA WEALAEKYKD REDIVIAELD ATANELEAFS VLGYPTLKFF PAGPDRKVID 

       490        500        510        520 
YKSTRDLETF SKFLDSGGHL PKEEPKEPAA SAPEAQANST LGPKEEL 

« Hide

Isoform 2 [UniParc].

Checksum: 4233CC4C3942C17D
Show »

FASTA52457,960

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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] (ISOFORM 2).
[3]"Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp."
Desilva M.G., Notkins A.L., Lan M.S.
DNA Cell Biol. 16:269-274(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC126438 Genomic DNA. No translation available.
BC116671 mRNA. Translation: AAI16672.1.
RefSeqNP_001074539.1. NM_001081070.1.
UniGeneMm.32631.

3D structure databases

ProteinModelPortalD3Z6P0.
SMRD3Z6P0. Positions 43-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213283. 2 interactions.
STRING10090.ENSMUSP00000035584.

Proteomic databases

PRIDED3Z6P0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039113; ENSMUSP00000035584; ENSMUSG00000024184. [D3Z6P0-1]
ENSMUST00000120333; ENSMUSP00000114080; ENSMUSG00000024184. [D3Z6P0-2]
GeneID69191.
KEGGmmu:69191.
UCSCuc008bdo.1. mouse. [D3Z6P0-1]
uc012ans.1. mouse. [D3Z6P0-2]

Organism-specific databases

CTD64714.
MGIMGI:1916441. Pdia2.

Phylogenomic databases

GeneTreeENSGT00740000115202.
HOGENOMHOG000162459.
HOVERGENHBG005920.
KOK09581.
OMATEFNSQT.
OrthoDBEOG7VHSX1.
PhylomeDBD3Z6P0.
TreeFamTF106381.

Gene expression databases

BgeeD3Z6P0.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005792. 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.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDIA2. mouse.
NextBio328852.
PROD3Z6P0.
SOURCESearch...

Entry information

Entry namePDIA2_MOUSE
AccessionPrimary (citable) accession number: D3Z6P0
Secondary accession number(s): Q14AV9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 39 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot