ID   ERP38_NEUCR             Reviewed;         369 AA.
AC   Q92249; Q7RVD7; Q9C2P3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Protein disulfide-isomerase erp38;
DE            Short=ERp38;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=erp38; ORFNames=17E5.50, NCU03739;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; Y07562; CAA68847.1; -; mRNA.
DR   EMBL; AL513467; CAC28831.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32279.1; -; Genomic_DNA.
DR   PIR; T47259; T47259.
DR   RefSeq; XP_961515.1; XM_956422.3.
DR   AlphaFoldDB; Q92249; -.
DR   SMR; Q92249; -.
DR   IntAct; Q92249; 4.
DR   MINT; Q92249; -.
DR   STRING; 367110.Q92249; -.
DR   PaxDb; 5141-EFNCRP00000003391; -.
DR   EnsemblFungi; EAA32279; EAA32279; NCU03739.
DR   GeneID; 3877590; -.
DR   KEGG; ncr:NCU03739; -.
DR   VEuPathDB; FungiDB:NCU03739; -.
DR   HOGENOM; CLU_038617_1_1_1; -.
DR   InParanoid; Q92249; -.
DR   OMA; WEDLANT; -.
DR   OrthoDB; 52245at2759; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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   Reference proteome; Repeat; Signal; Stress response.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..369
FT                   /note="Protein disulfide-isomerase erp38"
FT                   /id="PRO_0000034244"
FT   DOMAIN          19..130
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          131..251
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           366..369
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            51
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            52
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            116
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            171
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            172
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            237
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..53
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        170..173
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        154
FT                   /note="A -> P (in Ref. 1; CAA68847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   369 AA;  39282 MW;  4554092E43A8F3E6 CRC64;
     MVLLKSLVVA SLAAAVAAKS AVLDLIPSNF DDVVLKSGKP TLVEFFAPWC GHCKNLAPVY
     EELATALEYA KDKVQIAKVD ADAERALGKR FGVQGFPTLK FFDGKSEQPV DYKGGRDLDS
     LSNFIAEKTG VKARKKGSAP SLVNILNDAT IKGAIGGDKN VLVAFTAPWC GHCKNLAPTW
     EKLAATFASD PEITIAKVDA DAPTGKKSAA EYGVSGFPTI KFFPKGSTTP EDYNGGRSEA
     DLVKFLNEKA GTHRTPGGGL DTVAGTIAAL DEIVAKYTGG ASLAEVAEEA KEAVKSLKNS
     AELKYADYYL RVLDKLSKSE GYATKEFARL EGILKKGGLA PAKVDELTVK VNVLRKFVEK
     AAEEAKEEL
//