ID   PDI_ALTAL               Reviewed;         436 AA.
AC   Q00002; P87325;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   AltName: Allergen=Alt a 4;
DE   Flags: Fragment;
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=9095236; DOI=10.1007/978-1-4615-5855-2_21;
RA   Achatz G., Oberkofler H., Lechenauer E., Simon B., Unger A., Kandler D.,
RA   Ebner C., Prillinger H., Kraft D., Breitenbach M.;
RT   "Molecular characterization of Alternaria alternata and Cladosporium
RT   herbarum allergens.";
RL   Adv. Exp. Med. Biol. 409:157-161(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=08-0203-Berlin;
RA   Unger A.M., Lechenauer E., Simon B., Oberkofler H., Probst G., Achatz G.,
RA   Breitenbach M.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC       bonds, may be involved in glycosylation, prolyl hydroxylation and
CC       triglyceride transfer. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:9095236}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; X84217; CAA58999.1; -; mRNA.
DR   EMBL; U82634; AAB40401.1; -; mRNA.
DR   AlphaFoldDB; Q00002; -.
DR   SMR; Q00002; -.
DR   Allergome; 18; Alt a 4.
DR   Allergome; 3061; Alt a 4.0101.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW   Redox-active center.
FT   CHAIN           <1..436
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000120175"
FT   DOMAIN          216..365
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          328..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           433..436
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        362..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            267
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            268
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..269
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   NON_TER         1
SQ   SEQUENCE   436 AA;  46275 MW;  ECBB7D93738BCEE3 CRC64;
     ARDMTKQALP AVSEVTKDTL EEFKTADKVV LVAYFAADDK ASNETFTSVA NGLRDNFLFG
     ATNDAALAKA EGVKQPGLVC TSPSTTARTS SPRPSMRTYP RLRKVASTPL IGEVGPETYA
     GYMAAGIPLA YIFAETPEER EEFAKELKPL ALKHKGEINF ATIDAKSFGQ HAGNLNLKVG
     TWPAFAIQRT EKNEKFPTNQ EAKITEKEIG KFVDDFLAGK IDPSIKSEPI PESNDGPVTV
     VVAHNYKDVV IDNDKDVLVE FYAPWCGHCK ALAPKYEELG QLYASDELSK LVTIAKVDAT
     LNDVPDEIQG FLPSSLFPLA RRMPQSTTLV PHCRGSRPVH RRERLTQASA SVGEAVEDAT
     ESAKASASSA TDSAASAVSE GTETVKSGAS VASDSASSAA SEATKSVKSA ASEVTNSASS
     AASEASASAS SVKDEL