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O43099 (PMP20_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 87. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative peroxiredoxin pmp20

EC=1.11.1.15
Alternative name(s):
Peroxisomal membrane protein pmp20
Thioredoxin reductase
Allergen=Asp f 3
Gene names
Name:pmp20
ORF Names:AFUA_6G02280
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subcellular location

Peroxisome Potential.

Allergenic properties

Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Cand b 2 of Candida boidinii.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentPeroxisome
   DiseaseAllergen
   DomainRedox-active center
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintracellular

Inferred from direct assay PubMed 20507060. Source: ASPGD

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionIgE binding

Inferred from direct assay PubMed 19032234Ref.1. Source: ASPGD

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxiredoxin activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Putative peroxiredoxin pmp20
PRO_0000056603

Regions

Domain4 – 158155Thioredoxin

Sequences

Sequence LengthMass (Da)Tools
O43099 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AFFCD72C5A1CCBB2

FASTA16818,453
        10         20         30         40         50         60 
MSGLKAGDSF PSDVVFSYIP WSEDKGEITA CGIPINYNAS KEWADKKVIL FALPGAFTPV 

        70         80         90        100        110        120 
CSARHVPEYI EKLPEIRAKG VDVVAVLAYN DAYVMSAWGK ANQVTGDDIL FLSDPDARFS 

       130        140        150        160 
KSIGWADEEG RTKRYALVID HGKITYAALE PAKNHLEFSS AETVLKHL 

« Hide

References

« Hide 'large scale' references
[1]"Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes."
Hemmann S., Blaser K., Crameri R.
Am. J. Respir. Crit. Care Med. 156:1956-1962(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 42202 / AF-102 / Ag 507.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58050 mRNA. Translation: AAB95638.1.
AAHF01000012 Genomic DNA. Translation: EAL85811.1.
RefSeqXP_747849.1. XM_742756.1.

3D structure databases

ProteinModelPortalO43099.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00000470.

Protein family/group databases

Allergome3121. Asp f 3.0101.
73. Asp f 3.

Proteomic databases

PRIDEO43099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000470; CADAFUAP00000470; CADAFUAG00000470.
GeneID3505266.
KEGGafm:AFUA_6G02280.

Phylogenomic databases

eggNOGCOG0678.
HOGENOMHOG000255884.
KOK14171.
OMAAEILCIS.
OrthoDBEOG7X3R3F.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMP20_ASPFU
AccessionPrimary (citable) accession number: O43099
Secondary accession number(s): Q4WCS7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: January 22, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Allergens

Nomenclature of allergens and list of entries