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

P08003 (PDIA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 A4

EC=5.3.4.1
Alternative name(s):
Endoplasmic reticulum resident protein 72
Short name=ER protein 72
Short name=ERp-72
Short name=ERp72
Gene names
Name:Pdia4
Synonyms:Cai, Erp72
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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.

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.

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

Experimental info

Sequence conflict281H → Q in AAA39907. Ref.1
Sequence conflict281H → Q in BAE27045. Ref.2
Sequence conflict281H → Q in AAI41079. Ref.3
Sequence conflict391E → EEEE in BAC25863. Ref.2
Sequence conflict391E → EEEE in BAE41134. Ref.2
Sequence conflict391E → EEEE in BAE36446. Ref.2
Sequence conflict391E → EEEE in BAE29664. Ref.2
Sequence conflict4681N → S in BAC25863. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P08003 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 2DDE2CE80BD77F6E

FASTA63871,982
        10         20         30         40         50         60 
MKLRKAWLLV LLLALTQLLA AASAGDAHED 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

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Amnion, Bone marrow, Head, Ovary and Uterus.
[3]"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].
Strain: C57BL/6J.
Tissue: Brain and Embryonic germ cell.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638.
Strain: BALB/c.
Tissue: T-cell.
[5]"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.
[6]"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.
AK028292 mRNA. Translation: BAC25863.1.
AK146288 mRNA. Translation: BAE27045.1.
AK150566 mRNA. Translation: BAE29664.1.
AK161534 mRNA. Translation: BAE36446.1.
AK169387 mRNA. Translation: BAE41134.1.
BC066857 mRNA. Translation: AAH66857.1.
BC141078 mRNA. Translation: AAI41079.1.
Y00884 mRNA. Translation: CAA68777.1. Frameshift.
PIRISMSER. B34930.
S06318.
RefSeqNP_033917.2. NM_009787.2.
UniGeneMm.2442.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJ1NMR-A46-172[»]
2DJ2NMR-A171-277[»]
2DJ3NMR-A518-638[»]
ProteinModelPortalP08003.
SMRP08003. Positions 47-507, 516-638.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198446. 1 interaction.
IntActP08003. 5 interactions.
MINTMINT-4106888.

PTM databases

PhosphoSiteP08003.

Proteomic databases

PaxDbP08003.
PRIDEP08003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823.
GeneID12304.
KEGGmmu:12304.
UCSCuc009btf.1. mouse.

Organism-specific databases

CTD9601.
MGIMGI:104864. Pdia4.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115037.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidQ6NXW4.
KOK09582.
OrthoDBEOG7VHSX1.
PhylomeDBP08003.
TreeFamTF106382.

Gene expression databases

BgeeP08003.
CleanExMM_PDIA4.
GenevestigatorP08003.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFPIRSF036862. Disulphide_isom_A4. 1 hit.
PRINTSPR00421. THIOREDOXIN.
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

ChiTaRSPDIA4. mouse.
EvolutionaryTraceP08003.
NextBio280830.
PROP08003.
SOURCESearch...

Entry information

Entry namePDIA4_MOUSE
AccessionPrimary (citable) accession number: P08003
Secondary accession number(s): P15841 expand/collapse secondary AC list , Q3TT79, Q3UJW0, Q6NXW4, Q8BMT8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 143 of the entry and version 3 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

MGD cross-references

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