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Q92249 (ERP38_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase erp38
Short name=ERp38
EC=5.3.4.1
Gene names
Name:erp38
ORF Names:17E5.50, NCU03739
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subcellular location

Endoplasmic reticulum lumen Potential.

Induction

By stress.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 369351Protein disulfide-isomerase erp38
PRO_0000034244

Regions

Domain19 – 130112Thioredoxin 1
Domain131 – 251121Thioredoxin 2
Motif366 – 3694Prevents secretion from ER Potential

Sites

Active site501Nucleophile By similarity
Active site531Nucleophile By similarity
Active site1701Nucleophile By similarity
Active site1731Nucleophile By similarity
Site511Contributes to redox potential value By similarity
Site521Contributes to redox potential value By similarity
Site1161Lowers pKa of C-terminal Cys of first active site By similarity
Site1711Contributes to redox potential value By similarity
Site1721Contributes to redox potential value By similarity
Site2371Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond50 ↔ 53Redox-active By similarity
Disulfide bond170 ↔ 173Redox-active By similarity

Experimental info

Sequence conflict1541A → P in CAA68847. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q92249 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 4554092E43A8F3E6

FASTA36939,282
        10         20         30         40         50         60 
MVLLKSLVVA SLAAAVAAKS AVLDLIPSNF DDVVLKSGKP TLVEFFAPWC GHCKNLAPVY 

        70         80         90        100        110        120 
EELATALEYA KDKVQIAKVD ADAERALGKR FGVQGFPTLK FFDGKSEQPV DYKGGRDLDS 

       130        140        150        160        170        180 
LSNFIAEKTG VKARKKGSAP SLVNILNDAT IKGAIGGDKN VLVAFTAPWC GHCKNLAPTW 

       190        200        210        220        230        240 
EKLAATFASD PEITIAKVDA DAPTGKKSAA EYGVSGFPTI KFFPKGSTTP EDYNGGRSEA 

       250        260        270        280        290        300 
DLVKFLNEKA GTHRTPGGGL DTVAGTIAAL DEIVAKYTGG ASLAEVAEEA KEAVKSLKNS 

       310        320        330        340        350        360 
AELKYADYYL RVLDKLSKSE GYATKEFARL EGILKKGGLA PAKVDELTVK VNVLRKFVEK 


AAEEAKEEL

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterisation of a novel stress-inducible PDI-family gene from Aspergillus niger."
Jeenes D.J., Pfaller R., Archer D.B.
Gene 193:151-156(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y07562 mRNA. Translation: CAA68847.1.
AL513467 Genomic DNA. Translation: CAC28831.1.
AABX02000011 Genomic DNA. Translation: EAA32279.1.
PIRT47259.
RefSeqXP_961515.1. XM_956422.2.
UniGeneNcr.7762.

3D structure databases

ProteinModelPortalQ92249.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4653714.
STRING5141.NCU03739.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000003391; EFNCRP00000003391; EFNCRG00000003387.
GeneID3877590.
KEGGncr:NCU03739.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000176389.
KOK09584.
OMAFFPKGST.
OrthoDBEOG4X9BS1.

Family and domain databases

Gene3D1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF47933. ERP29_C. 1 hit.
SSF52833. Thiordxn-like_fd. 2 hits.
TIGRFAMsTIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERP38_NEUCR
AccessionPrimary (citable) accession number: Q92249
Secondary accession number(s): Q7RVD7, Q9C2P3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 30, 2003
Last modified: April 3, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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