ID   TIGA_ASPNG              Reviewed;         359 AA.
AC   Q00216;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Protein disulfide-isomerase tigA;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=tigA;
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], AND INDUCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=9256071; DOI=10.1016/s0378-1119(97)00098-x;
RA   Jeenes D.J., Pfaller R., Archer D.B.;
RT   "Isolation and characterisation of a novel stress-inducible PDI-family gene
RT   from Aspergillus niger.";
RL   Gene 193:151-156(1997).
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   -!- INDUCTION: By stress, and tunicamycin. {ECO:0000269|PubMed:9256071}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; X98748; CAA67299.1; -; Genomic_DNA.
DR   RefSeq; XP_001398661.1; XM_001398624.2.
DR   AlphaFoldDB; Q00216; -.
DR   SMR; Q00216; -.
DR   PaxDb; 5061-CADANGAP00013579; -.
DR   EnsemblFungi; CAK47274; CAK47274; An18g02020.
DR   GeneID; 4989762; -.
DR   VEuPathDB; FungiDB:An18g02020; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1128436; -.
DR   VEuPathDB; FungiDB:ATCC64974_110240; -.
DR   VEuPathDB; FungiDB:M747DRAFT_337590; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   OrthoDB; 52245at2759; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:AspGD.
DR   GO; GO:0006457; P:protein folding; IDA:AspGD.
DR   CDD; cd00238; ERp29c; 1.
DR   CDD; cd02998; PDI_a_ERp38; 2.
DR   Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR011679; ERp29_C.
DR   InterPro; IPR036356; ERp29_C_sf.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR45672:SF11; PROTEIN DISULFIDE-ISOMERASE C17H9.14C; 1.
DR   PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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; Stress response.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..359
FT                   /note="Protein disulfide-isomerase tigA"
FT                   /id="PRO_0000034245"
FT   DOMAIN          20..129
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          131..250
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           356..359
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        52
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            50
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            51
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            115
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            170
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            171
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            236
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        169..172
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   359 AA;  38592 MW;  346B64197BA37608 CRC64;
     MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG HCKNLAPVYE
     ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW FDGKSDEPED YKGGRDLESL
     SSFISEKTGV KPRGPKKEPS KVEMLNDATF KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE
     ALANDFVLEP NVVIAKVDAD AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA
     FIDFLNEKTG THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY
     VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG EEKEAKDEL
//