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Q00002

- PDI_ALTAL

UniProt

Q00002 - PDI_ALTAL

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Protein
Protein disulfide-isomerase
Gene
N/A
Organism
Alternaria alternata (Alternaria rot fungus) (Torula alternata)
Status
Reviewed - 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 – 2661Nucleophile By similarity
Sitei267 – 2671Contributes to redox potential value By similarity
Sitei268 – 2681Contributes to redox potential value By similarity
Active sitei269 – 2691Nucleophile By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC
Complete GO annotation...

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

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-isomerase
PRO_0000120175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi266 ↔ 269Redox-active By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ00002.
SMRiQ00002. Positions 108-318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 365150Thioredoxin
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi433 – 4364Prevents secretion from ER Reviewed prediction

Compositional bias

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

Sequence similaritiesi

Contains at least 1 thioredoxin domain.

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

ARDMTKQALP AVSEVTKDTL EEFKTADKVV LVAYFAADDK ASNETFTSVA    50
NGLRDNFLFG ATNDAALAKA EGVKQPGLVC TSPSTTARTS SPRPSMRTYP 100
RLRKVASTPL IGEVGPETYA GYMAAGIPLA YIFAETPEER EEFAKELKPL 150
ALKHKGEINF ATIDAKSFGQ HAGNLNLKVG TWPAFAIQRT EKNEKFPTNQ 200
EAKITEKEIG KFVDDFLAGK IDPSIKSEPI PESNDGPVTV VVAHNYKDVV 250
IDNDKDVLVE FYAPWCGHCK ALAPKYEELG QLYASDELSK LVTIAKVDAT 300
LNDVPDEIQG FLPSSLFPLA RRMPQSTTLV PHCRGSRPVH RRERLTQASA 350
SVGEAVEDAT ESAKASASSA TDSAASAVSE GTETVKSGAS VASDSASSAA 400
SEATKSVKSA ASEVTNSASS AASEASASAS SVKDEL 436
Length:436
Mass (Da):46,275
Last modified:January 24, 2006 - v2
Checksum:iECBB7D93738BCEE3
GO

Non-terminal residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84217 mRNA. Translation: CAA58999.1.
U82634 mRNA. Translation: AAB40401.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84217 mRNA. Translation: CAA58999.1 .
U82634 mRNA. Translation: AAB40401.1 .

3D structure databases

ProteinModelPortali Q00002.
SMRi Q00002. Positions 108-318.
ModBasei Search...

Protein family/group databases

Allergomei 18. Alt a 4.
3061. Alt a 4.0101.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: April 16, 2014
This is version 75 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