ERP38_NEUCR
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 03-AUG-2022, entry version 157.
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; 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; FINEHAG; -.
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 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 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
