ID   PDI_ASPNG               Reviewed;         515 AA.
AC   Q12730;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=pdiA; Synonyms=pdi1;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RX   MEDLINE=97174110; PubMed=9021130; DOI=10.1007/s002940050187;
RA   Ngiam C., Jeenes D.J., Archer D.B.;
RT   "Isolation and characterisation of a gene encoding protein disulphide
RT   isomerase, pdiA, from Aspergillus niger.";
RL   Curr. Genet. 31:133-138(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RA   Malpricht S.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in the folding of proteins containing
CC       disulfide bonds, may be involved in glycosylation, prolyl
CC       hydroxylation and triglyceride transfer (By similarity).
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
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DR   EMBL; X98797; CAA67332.1; -; Genomic_DNA.
DR   EMBL; X89449; CAA61619.1; -; mRNA.
DR   PIR; S57942; S57942.
DR   HSSP; P07237; 1MEK.
DR   BRENDA; 5.3.4.1; 277.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR001393; Calsequestrin.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00312; CALSEQUESTRN.
DR   TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW   Repeat; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    515       Protein disulfide-isomerase.
FT                                /FTId=PRO_0000034213.
FT   DOMAIN       21    132       Thioredoxin 1.
FT   DOMAIN      339    470       Thioredoxin 2.
FT   MOTIF       512    515       Prevents secretion from ER (Potential).
FT   ACT_SITE     54     54       Nucleophile (By similarity).
FT   ACT_SITE     57     57       Nucleophile (By similarity).
FT   ACT_SITE    389    389       Nucleophile (By similarity).
FT   ACT_SITE    392    392       Nucleophile (By similarity).
FT   SITE         55     55       Contributes to redox potential value (By
FT                                similarity).
FT   SITE         56     56       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        117    117       Lowers pKa of C-terminal Cys of first
FT                                active site (By similarity).
FT   SITE        390    390       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        391    391       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        456    456       Lowers pKa of C-terminal Cys of second
FT                                active site (By similarity).
FT   DISULFID     54     57       Redox-active (By similarity).
FT   DISULFID    389    392       Redox-active (By similarity).
SQ   SEQUENCE   515 AA;  56292 MW;  2B0058B788400AD9 CRC64;
     MRSFAPWLVS LLGASAVVAA ADTESDVISL DQDTFESFMN EHGLVLAEFF APWCGHCKAL
     APKYEEAATE LKAKNIPLVK VDCTAEEDLC RSQGVEGYPT LKIFRGVDSS KPYQGARQTE
     SIVSYMIKQS LPAVSSVNEE NLEEIKTMDK IVVIGYIPSD DQETYQAFEK YAESQRDNYL
     FAATDDAAIA KSEGVEQPSI VLYKDFDEKK AVYDGEIEQE AIHSWVKSAS TPLVGEIGPE
     TYSGYIGAGV PLAYIFAETK EEREKYTEDF KPIAQKHKGA INIATIDAKM FGAHAGNLNL
     DSQKFPAFAI QDPAKNAKYP YDQAKELNAD EVEKFIQDVL DGKVEPSIKS EPVPESQEGP
     VTVVVAHSYK DLVIDNDKDV LLEFYAPWCG HCKALAPKYD ELAALYADHP DLAAKVTIAK
     IDATANDVPD PITGFPTLRL YPAGAKDSPI EYSGSRTVED LANFVKENGK HNVDALNVAS
     EETQEGGDVT EAAPSATEAE TPAATDDEKA EHDEL
//