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Reviewed, UniProtKB/Swiss-Prot P08003 (PDIA4_MOUSE)

Last modified February 9, 2010. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein disulfide-isomerase A4
    EC=5.3.4.1
Alternative name(s):
    Protein ERp-72
      Short name=ERp72
Gene names
Name: Pdia4
Synonyms: Cai, Erp72
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length638 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 a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, 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.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Sequence caution

The sequence CAA68777.1 differs from that shown. Reason: Frameshift at position 544.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMAcetylation
Disulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein disulfide isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 638618Protein disulfide-isomerase A4
PRO_0000034230

Regions

Domain21 – 162142Thioredoxin 1
Domain162 – 294133Thioredoxin 2
Domain498 – 629132Thioredoxin 3
Motif635 – 6384Prevents secretion from ER
Compositional bias39 – 5012Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3591N6-acetyllysine By similarity
Glycosylation361N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 87Redox-active By similarity
Disulfide bond199 ↔ 202Redox-active By similarity
Disulfide bond548 ↔ 551Redox-active By similarity

Secondary structure

................. 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08003-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: FA06D250D06A27BB

FASTA63871,973
        10         20         30         40         50         60 
MKLRKAWLLV LLLALTQLLA AASAGDAQED TSDTENATEE EEEEDDDDLE VKEENGVWVL 

        70         80         90        100        110        120 
NDGNFDNFVA DKDTVLLEFY APWCGHCKQF APEYEKIAST LKDNDPPIAV AKIDATSASM 

       130        140        150        160        170        180 
LASKFDVSGY PTIKILKKGQ AVDYDGSRTQ EEIVAKVREV SQPDWTPPPE VTLSLTKDNF 

       190        200        210        220        230        240 
DDVVNNADII LVEFYAPWCG HCKKLAPEYE KAAKELSKRS PPIPLAKVDA TEQTDLAKRF 

       250        260        270        280        290        300 
DVSGYPTLKI FRKGRPFDYN GPREKYGIVD YMIEQSGPPS KEILTLKQVQ EFLKDGDDVV 

       310        320        330        340        350        360 
IIGLFQGDGD PAYLQYQDAA NNLREDYKFH HTFSPEIAKF LKVSLGKLVL THPEKFQSKY 

       370        380        390        400        410        420 
EPRFHVMDVQ GSTEASAIKD YVVKHALPLV GHRKTSNDAK RYSKRPLVVV YYSVDFSFDY 

       430        440        450        460        470        480 
RAATQFWRNK VLEVAKDFPE YTFAIADEED YATEVKDLGL SESGEDVNAA ILDESGKKFA 

       490        500        510        520        530        540 
MEPEEFDSDT LREFVTAFKK GKLKPVIKSQ PVPKNNKGPV KVVVGKTFDA IVMDPKKDVL 

       550        560        570        580        590        600 
IEFYAPWCGH CKQLEPIYTS LGKKYKGQKD LVIAKMDATA NDITNDQYKV EGFPTIYFAP 

       610        620        630 
SGDKKNPIKF EGGNRDLEHL SKFIDEHATK RSRTKEEL 

« Hide

References

[1]"ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase."
Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M.
J. Biol. Chem. 265:1094-1101(1990) [PubMed: 2295602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"An mRNA sharing sequences with a variant granulocyte-macrophage colony stimulating factor cDNA clone."
Gough N.M., King J.A., Dunn A.R.
Nucleic Acids Res. 15:10584-10584(1987) [PubMed: 3320970] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638.
Strain: BALB/c.
Tissue: T-cell.
[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: 12475965] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[4]"The solution structure of thioredoxin domains of mouse protein disulfide-isomerase A4."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 46-277 AND 516-638.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05186 mRNA. Translation: AAA39907.1.
Y00884 mRNA. Translation: CAA68777.1. Frameshift.
IPIIPI00271951.
PIRISMSER. B34930.
S06318.
UniGeneMm.2442

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJ1NMR-A46-172[»]
2DJ2NMR-A171-277[»]
2DJ3NMR-A518-638[»]
SMRP08003. Positions 53-219, 170-632.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08003.

PTM databases

PhosphoSiteP08003.

Proteomic databases

PRIDEP08003.

Genome annotation databases

EnsemblENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:104864. Pdia4.

Phylogenomic databases

eggNOGroNOG09466.
HOVERGENP08003.
InParanoidP08003.

Enzyme and pathway databases

BRENDA5.3.4.1. 244.

Gene expression databases

ArrayExpressP08003.
BgeeP08003.
CleanExMM_PDIA4.
GenevestigatorP08003.
GermOnlineENSMUSG00000025823. Mus musculus.

Family and domain databases

InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR006662. Thioredoxin-like_subdom.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFPIRSF036862. Disulphide_isom_A4. 1 hit.
PRINTSPR00421. THIOREDOXIN.
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 Resources

SOURCESearch...

Entry information

Entry namePDIA4_MOUSE
AccessionPrimary (citable) accession number: P08003
Secondary accession number(s): P15841
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: May 1, 1991
Last modified: February 9, 2010
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents