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Q5RCH2 (PDIA2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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 A2

EC=5.3.4.1
Gene names
Name:PDIA2
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Catalytic activity

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

Subunit structure

Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. 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.

Post-translational modification

The disulfide-linked homodimer exhibits an enhanced chaperone activity By similarity.

Glycosylated 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 – 2121 Potential
Chain22 – 525504Protein disulfide-isomerase A2
PRO_0000034223

Regions

Domain27 – 152126Thioredoxin 1
Domain367 – 496130Thioredoxin 2
Motif522 – 5254Prevents secretion from ER Potential

Sites

Active site711Nucleophile By similarity
Active site741Nucleophile By similarity
Active site4181Nucleophile By similarity
Active site4211Nucleophile By similarity
Site721Contributes to redox potential value By similarity
Site731Contributes to redox potential value By similarity
Site1381Lowers pKa of C-terminal Cys of first active site By similarity
Site4191Contributes to redox potential value By similarity
Site4201Contributes to redox potential value By similarity
Site4821Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential
Glycosylation5161N-linked (GlcNAc...) Potential
Disulfide bond18Interchain By similarity
Disulfide bond71 ↔ 74Redox-active By similarity
Disulfide bond418 ↔ 421Redox-active By similarity

Experimental info

Sequence conflict3421E → G in CAH92649. Ref.1
Sequence conflict4851G → E in CAH92649. Ref.1
Sequence conflict5051E → G in CAH92649. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5RCH2 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 0C402549E70D3F32

FASTA52558,124
        10         20         30         40         50         60 
MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP 

        70         80         90        100        110        120 
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV DGPAQPELAE EFGVTEYPTL 

       130        140        150        160        170        180 
KFFRDGNRTH PEEYTGPREA EGIAEWLRRR VGPSAMRLED EAAAQALIDG RDLVVIGFFQ 

       190        200        210        220        230        240 
DLHDEDVATF LALAQDALDM TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL 

       250        260        270        280        290        300 
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA 

       310        320        330        340        350        360 
APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTTASI 

       370        380        390        400        410        420 
TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH 

       430        440        450        460        470        480 
CKEMAPAWEA LAEKYQDHED VIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS 

       490        500        510        520 
TRDLGTFSKF LDNGGVLPTE EPLEEPAAPF PEPPANSTMG SKEEL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858298 mRNA. Translation: CAH90535.1.
CR860523 mRNA. Translation: CAH92649.1.
RefSeqNP_001125285.1. NM_001131813.1.
UniGenePab.11836.
Pab.19686.

3D structure databases

ProteinModelPortalQ5RCH2.
SMRQ5RCH2. Positions 389-492.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172183.
KEGGpon:100172183.

Organism-specific databases

CTD64714.

Phylogenomic databases

HOVERGENHBG005920.
InParanoidQ5RCH2.
KOK09581.

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. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDIA2_PONAB
AccessionPrimary (citable) accession number: Q5RCH2
Secondary accession number(s): Q5R6G7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 67 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