Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P38659 (PDIA4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase A4

EC=5.3.4.1
Alternative name(s):
Calcium-binding protein 2
Short name=CaBP2
Endoplasmic reticulum resident protein 70
Short name=ER protein 70
Short name=ERp70
Endoplasmic reticulum resident protein 72
Short name=ER protein 72
Short name=ERp-72
Short name=ERp72
Gene names
Name:Pdia4
Synonyms:Cabp2, Erp70
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity.

Induction

Upon glucose starvation, as well as treatment with tunicamycin.

Post-translational modification

O-glycosylated.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dmel_CG7484Q9VVJ72EBI-917435,EBI-128899From a different organism.
PpibP243682EBI-917435,EBI-916926
TgP068823EBI-917435,EBI-1549657

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 643623Protein disulfide-isomerase A4
PRO_0000034231

Regions

Domain21 – 167147Thioredoxin 1
Domain167 – 299133Thioredoxin 2
Domain503 – 634132Thioredoxin 3
Motif640 – 6434Prevents secretion from ER

Amino acid modifications

Modified residue3641N6-acetyllysine By similarity
Disulfide bond89 ↔ 92Redox-active By similarity
Disulfide bond204 ↔ 207Redox-active By similarity
Disulfide bond553 ↔ 556Redox-active By similarity

Experimental info

Sequence conflict431D → E in AAA19217. Ref.1
Sequence conflict3911A → D in AAA19217. Ref.1
Sequence conflict4971Q → R in AAA19217. Ref.1

Secondary structure

.......................................... 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38659 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: C5BC8536834543ED

FASTA64372,720
        10         20         30         40         50         60 
MKLRKAWLLV LLLALTQLLA AASAEDAHED ASDSENPIED DDDEEEDEED EDDLEVKEEN 

        70         80         90        100        110        120 
GVWVLNDENF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE KIASTLKDND PPIAVAKIDA 

       130        140        150        160        170        180 
TSASMLASKF DVSGYPTIKI LKKGQAVDYD GSRTQEEIVA KVREVSQPDW TPPPEVTLTL 

       190        200        210        220        230        240 
TKENFDDVVN NADIILVEFY APWCGHCKKL APEYEKAAKE LSKRSPPIPL AKVDATEQTD 

       250        260        270        280        290        300 
LAKRFDVSGY PTLKIFRKGR PFDYNGPREK YGIVDYMVEQ SGPPSKEILT LKQVQEFLKD 

       310        320        330        340        350        360 
GDDVVILGVF QGVGDPGYLQ YQDAANTLRE DYKFHHTFST EIAKFLKVSL GKLVLMQPEK 

       370        380        390        400        410        420 
FQSKYEPRMH VMDVQGSTEA SAIKDYVVKH ALPLVGHRKT SNDAKRYSKR PLVVVYYSVD 

       430        440        450        460        470        480 
FSFDYRTATQ FWRNKVLEVA KDFPEYTFAI ADEEDYATEV KDLGLSESGE DVNAAILDES 

       490        500        510        520        530        540 
GKKFAMEPEE FDSDALQEFV MAFKKGKLKP VIKSQPVPKN NKGPVRVVVG KTFDAIVMDP 

       550        560        570        580        590        600 
KKDVLIEFYA PWCGHCKQLE PVYTSLGKKY KGQKDLVIAK MDATANDITN DRYKVEGFPT 

       610        620        630        640 
IYFAPSGDKK NPIKFEGGNR DLEHLSKFID EHATKRSRTK EEL 

« Hide

References

« Hide 'large scale' references
[1]"CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity."
Van P.N., Rupp K., Lampen A., Soeling H.-D.
Eur. J. Biochem. 213:789-795(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[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].
Tissue: Pituitary.
[3]"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86870 mRNA. Translation: AAA19217.1.
BC061535 mRNA. Translation: AAH61535.1.
PIRS32476.
RefSeqNP_446301.1. NM_053849.1.
UniGeneRn.39305.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EC3X-ray1.92A/B283-523[»]
ProteinModelPortalP38659.
SMRP38659. Positions 54-282, 521-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250512. 5 interactions.
IntActP38659. 10 interactions.
MINTMINT-4565672.
STRING10116.ENSRNOP00000008728.

Proteomic databases

PaxDbP38659.
PRIDEP38659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116598.
KEGGrno:116598.
UCSCRGD:619835. rat.

Organism-specific databases

CTD9601.
RGD619835. Pdia4.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP38659.
KOK09582.
PhylomeDBP38659.

Gene expression databases

GenevestigatorP38659.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFPIRSF036862. Disulphide_isom_A4. 1 hit.
SUPFAMSSF52833. SSF52833. 5 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38659.
NextBio619299.

Entry information

Entry namePDIA4_RAT
AccessionPrimary (citable) accession number: P38659
Secondary accession number(s): Q6P7S5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 25, 2005
Last modified: June 11, 2014
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references