ID   ER38_NEUCR     STANDARD;      PRT;   369 AA.
AC   Q92249; Q7RVD7; Q9C2P3;
DT   01-NOV-1997 (Rel. 35, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   Protein disulfide-isomerase erp38 precursor (EC 5.3.4.1) (ERp38).
GN   Name=erp38; ORFNames=17E5.50, NCU03739.1;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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
RT   gene from Aspergillus niger.";
RL   Gene 193:151-156(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=74-OR23-1A / FGSC 987;
RX   MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=74-OR23-1A / 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., 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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (Potential).
CC   -!- INDUCTION: By stress.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Y07562; CAA68847.1; -.
DR   EMBL; AL513467; CAC28831.1; -.
DR   EMBL; AABX01000268; EAA32279.1; -.
DR   PIR; T47259; T47259.
DR   HSSP; P07237; 1MEK.
DR   InterPro; IPR005788; Disulph_isom.
DR   InterPro; IPR000886; ER_target_S.
DR   InterPro; IPR011027; ERP29_C.
DR   InterPro; IPR006662; Thiored.
DR   InterPro; IPR006663; Thioredox_dom2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN; 2.
KW   Endoplasmic reticulum; Isomerase; Redox-active center; Repeat; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    369       Protein disulfide-isomerase erp38.
FT   DISULFID     50     53       Redox-active (By similarity).
FT   DISULFID    170    173       Redox-active (By similarity).
FT   SITE        366    369       Prevent secretion from ER (Potential).
FT   CONFLICT    154    154       A -> P (in Ref. 1).
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
//