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Reviewed, UniProtKB/Swiss-Prot P13667 (PDIA4_HUMAN)

Last modified November 3, 2009. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · 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: ERP70, ERP72
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length645 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. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.5 Ref.6

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Caution

Was originally (Ref.1) thought to be a deoxycytidine kinase.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainRedox-active center
Repeat
Signal
   Molecular functionIsomerase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

protein secretion

Traceable author statement. Source: ProtInc

   Cellular componentendoplasmic reticulum lumen

Traceable author statement. Source: ProtInc

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

protein disulfide isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF2B1Q142321EBI-1054653,EBI-491065

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 645625Protein disulfide-isomerase A4
PRO_0000034229

Regions

Domain21 – 169149Thioredoxin 1
Domain158 – 301144Thioredoxin 2
Domain505 – 636132Thioredoxin 3
Motif642 – 6454Prevents secretion from ER
Compositional bias39 – 5517Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3661N6-acetyllysine Ref.8
Disulfide bond91 ↔ 94Redox-active By similarity
Disulfide bond206 ↔ 209Redox-active By similarity
Disulfide bond555 ↔ 558Redox-active By similarity

Natural variations

Natural variant1731T → M: dbSNP rs2290971.
VAR_052580

Sequences

Sequence LengthMass (Da)Tools
P13667-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 1919C2AE12CD2684

FASTA64572,932
        10         20         30         40         50         60 
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE 

        70         80         90        100        110        120 
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI 

       130        140        150        160        170        180 
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL 

       190        200        210        220        230        240 
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE 

       250        260        270        280        290        300 
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL 

       310        320        330        340        350        360 
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP 

       370        380        390        400        410        420 
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS 

       430        440        450        460        470        480 
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD 

       490        500        510        520        530        540 
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM 

       550        560        570        580        590        600 
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF 

       610        620        630        640 
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL 

« Hide

References

« Hide 'large scale' references
[1]"Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity."
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
J. Biol. Chem. 264:14762-14768(1989) [PubMed: 2549034] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]Erratum
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
J. Biol. Chem. 266:5353-5353(1991) [PubMed: 2002068] [Abstract]
Cited for: SEQUENCE REVISION.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Muscle.
[4]"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.
[5]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

J05016 mRNA. Translation: AAA58460.1.
BC000425 mRNA. Translation: AAH00425.1.
BC001928 mRNA. Translation: AAH01928.1.
BC006344 mRNA. Translation: AAH06344.1.
BC011754 mRNA. Translation: AAH11754.1.
IPIIPI00009904.
PIRA23723.
RefSeqNP_004902.1.
UniGeneHs.93659

3D structure databases

HSSPHSSP built from PDB template 1MEK based on UniProtKB P07237.
SMRP13667. Positions 56-179, 178-284, 523-645.
ModBaseSearch...

Protein-protein interaction databases

IntActP13667. 6 interactions.
STRINGP13667.

PTM databases

PhosphoSiteP13667.

2-D gel databases

OGPP13667.
REPRODUCTION-2DPAGEIPI00009904.

Proteomic databases

PeptideAtlasP13667.
PRIDEP13667.

Genome annotation databases

EnsemblENST00000286091; ENSP00000286091; ENSG00000155660; Homo sapiens. [Genome view]
ENST00000413966; ENSP00000408628; ENSG00000155660; Homo sapiens. [Genome view]
ENST00000414033; ENSP00000409289; ENSG00000155660; Homo sapiens. [Genome view]
GeneID9601.
KEGGhsa:9601.
UCSCuc003wff.2. human.

Organism-specific databases

CTD9601.
GeneCardsGC07M148331.
HGNCHGNC:30167. PDIA4.
HPACAB017368.
HPA006139.
HPA006140.
PharmGKBPA142671190.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13667.
HOVERGENP13667.
OMARAATQFW.

Enzyme and pathway databases

BRENDA5.3.4.1. 247.

Gene expression databases

ArrayExpressP13667.
BgeeP13667.
CleanExHS_PDIA4.
GenevestigatorP13667.
GermOnlineENSG00000155660. Homo sapiens.

Family and domain databases

InterProIPR005788. Disulphide_isomerase.
IPR000886. ER_target_seq_motif.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR017936. Thioredoxin-like.
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

NextBio36019.

Entry information

Entry namePDIA4_HUMAN
AccessionPrimary (citable) accession number: P13667
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1991
Last modified: November 3, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

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