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Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Alternaria alternata (Alternaria rot fungus) (Torula alternata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei266 – 2661NucleophileBy similarity
Sitei267 – 2671Contributes to redox potential valueBy similarity
Sitei268 – 2681Contributes to redox potential valueBy similarity
Active sitei269 – 2691NucleophileBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Allergen: Alt a 4
OrganismiAlternaria alternata (Alternaria rot fungus) (Torula alternata)
Taxonomic identifieri5599 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeAlternariaAlternaria alternata group

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei18. Alt a 4.
3061. Alt a 4.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 436›436Protein disulfide-isomerasePRO_0000120175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi266 ↔ 269Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ00002.
SMRiQ00002. Positions 108-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 365150ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi433 – 4364Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi362 – 43170Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains at least 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q00002-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ARDMTKQALP AVSEVTKDTL EEFKTADKVV LVAYFAADDK ASNETFTSVA
60 70 80 90 100
NGLRDNFLFG ATNDAALAKA EGVKQPGLVC TSPSTTARTS SPRPSMRTYP
110 120 130 140 150
RLRKVASTPL IGEVGPETYA GYMAAGIPLA YIFAETPEER EEFAKELKPL
160 170 180 190 200
ALKHKGEINF ATIDAKSFGQ HAGNLNLKVG TWPAFAIQRT EKNEKFPTNQ
210 220 230 240 250
EAKITEKEIG KFVDDFLAGK IDPSIKSEPI PESNDGPVTV VVAHNYKDVV
260 270 280 290 300
IDNDKDVLVE FYAPWCGHCK ALAPKYEELG QLYASDELSK LVTIAKVDAT
310 320 330 340 350
LNDVPDEIQG FLPSSLFPLA RRMPQSTTLV PHCRGSRPVH RRERLTQASA
360 370 380 390 400
SVGEAVEDAT ESAKASASSA TDSAASAVSE GTETVKSGAS VASDSASSAA
410 420 430
SEATKSVKSA ASEVTNSASS AASEASASAS SVKDEL
Length:436
Mass (Da):46,275
Last modified:January 24, 2006 - v2
Checksum:iECBB7D93738BCEE3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84217 mRNA. Translation: CAA58999.1.
U82634 mRNA. Translation: AAB40401.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84217 mRNA. Translation: CAA58999.1.
U82634 mRNA. Translation: AAB40401.1.

3D structure databases

ProteinModelPortaliQ00002.
SMRiQ00002. Positions 108-318.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei18. Alt a 4.
3061. Alt a 4.0101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of Alternaria alternata and Cladosporium herbarum allergens."
    Achatz G., Oberkofler H., Lechenauer E., Simon B., Unger A., Kandler D., Ebner C., Prillinger H., Kraft D., Breitenbach M.
    Adv. Exp. Med. Biol. 409:157-161(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.
  2. Unger A.M., Lechenauer E., Simon B., Oberkofler H., Probst G., Achatz G., Breitenbach M.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 08-0203-Berlin.

Entry informationi

Entry nameiPDI_ALTAL
AccessioniPrimary (citable) accession number: Q00002
Secondary accession number(s): P87325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: January 7, 2015
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.