TIGA_ASPNG
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 25-MAY-2022, entry version 121.
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 AlphaFoldDB; Q00216; -.
DR SMR; Q00216; -.
DR STRING; 5061.CADANGAP00013579; -.
DR VEuPathDB; FungiDB:An18g02020; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1128436; -.
DR VEuPathDB; FungiDB:ATCC64974_110240; -.
DR VEuPathDB; FungiDB:M747DRAFT_337590; -.
DR eggNOG; KOG0191; 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 GO; GO:0051082; F:unfolded protein binding; IDA:AspGD.
DR GO; GO:0006457; P:protein folding; IDA:AspGD.
DR CDD; cd00238; ERp29c; 1.
DR Gene3D; 1.20.1150.12; -; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF47933; SSF47933; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
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; 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
