PDI_ASPNG
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 25-MAY-2022, entry version 112.
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; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX 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 / FGSC 732;
RA Malpricht S.;
RL Submitted (JUL-1995) 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 -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; X98797; CAA67332.1; -; Genomic_DNA.
DR EMBL; X89449; CAA61619.1; -; mRNA.
DR PIR; S57942; S57942.
DR AlphaFoldDB; Q12730; -.
DR SMR; Q12730; -.
DR STRING; 5061.CADANGAP00002931; -.
DR VEuPathDB; FungiDB:An02g14800; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1136225; -.
DR VEuPathDB; FungiDB:ATCC64974_50950; -.
DR VEuPathDB; FungiDB:M747DRAFT_299997; -.
DR eggNOG; KOG0190; Eukaryota.
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; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 1.
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
FT /evidence="ECO:0000255"
FT CHAIN 21..515
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034213"
FT DOMAIN 21..132
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 339..470
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 478..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 512..515
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 55
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 390
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 391
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 456
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 54..57
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 389..392
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
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
