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Protein

Protein disulfide-isomerase erp38

Gene

erp38

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileBy similarity
Sitei51 – 511Contributes to redox potential valueBy similarity
Sitei52 – 521Contributes to redox potential valueBy similarity
Active sitei53 – 531NucleophileBy similarity
Sitei116 – 1161Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei170 – 1701NucleophileBy similarity
Sitei171 – 1711Contributes to redox potential valueBy similarity
Sitei172 – 1721Contributes to redox potential valueBy similarity
Active sitei173 – 1731NucleophileBy similarity
Sitei237 – 2371Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC
  2. protein disulfide oxidoreductase activity Source: EnsemblFungi

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to oxidative stress Source: EnsemblFungi
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase erp38 (EC:5.3.4.1)
Short name:
ERp38
Gene namesi
Name:erp38
ORF Names:17E5.50, NCU03739
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 2, Linkage Group V

Organism-specific databases

EuPathDBiFungiDB:NCU03739.

Subcellular locationi

  1. Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 369351Protein disulfide-isomerase erp38PRO_0000034244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 53Redox-activePROSITE-ProRule annotation
Disulfide bondi170 ↔ 173Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By stress.

Interactioni

Protein-protein interaction databases

IntActiQ92249. 4 interactions.
MINTiMINT-4653714.
STRINGi5141.NCU03739.1.

Structurei

3D structure databases

ProteinModelPortaliQ92249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 130112Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini131 – 251121Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi366 – 3694Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000176389.
InParanoidiQ92249.
KOiK09584.
OMAiYKSGRDL.
OrthoDBiEOG71CFZN.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLKSLVVA SLAAAVAAKS AVLDLIPSNF DDVVLKSGKP TLVEFFAPWC
60 70 80 90 100
GHCKNLAPVY EELATALEYA KDKVQIAKVD ADAERALGKR FGVQGFPTLK
110 120 130 140 150
FFDGKSEQPV DYKGGRDLDS LSNFIAEKTG VKARKKGSAP SLVNILNDAT
160 170 180 190 200
IKGAIGGDKN VLVAFTAPWC GHCKNLAPTW EKLAATFASD PEITIAKVDA
210 220 230 240 250
DAPTGKKSAA EYGVSGFPTI KFFPKGSTTP EDYNGGRSEA DLVKFLNEKA
260 270 280 290 300
GTHRTPGGGL DTVAGTIAAL DEIVAKYTGG ASLAEVAEEA KEAVKSLKNS
310 320 330 340 350
AELKYADYYL RVLDKLSKSE GYATKEFARL EGILKKGGLA PAKVDELTVK
360
VNVLRKFVEK AAEEAKEEL
Length:369
Mass (Da):39,282
Last modified:April 30, 2003 - v2
Checksum:i4554092E43A8F3E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541A → P in CAA68847 (PubMed:9256071).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07562 mRNA. Translation: CAA68847.1.
AL513467 Genomic DNA. Translation: CAC28831.1.
CM002240 Genomic DNA. Translation: EAA32279.1.
PIRiT47259.
RefSeqiXP_961515.1. XM_956422.3.
UniGeneiNcr.7762.

Genome annotation databases

EnsemblFungiiEFNCRT00000003391; EFNCRP00000003391; EFNCRG00000003387.
GeneIDi3877590.
KEGGincr:NCU03739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07562 mRNA. Translation: CAA68847.1.
AL513467 Genomic DNA. Translation: CAC28831.1.
CM002240 Genomic DNA. Translation: EAA32279.1.
PIRiT47259.
RefSeqiXP_961515.1. XM_956422.3.
UniGeneiNcr.7762.

3D structure databases

ProteinModelPortaliQ92249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ92249. 4 interactions.
MINTiMINT-4653714.
STRINGi5141.NCU03739.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003391; EFNCRP00000003391; EFNCRG00000003387.
GeneIDi3877590.
KEGGincr:NCU03739.

Organism-specific databases

EuPathDBiFungiDB:NCU03739.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000176389.
InParanoidiQ92249.
KOiK09584.
OMAiYKSGRDL.
OrthoDBiEOG71CFZN.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiERP38_NEUCR
AccessioniPrimary (citable) accession number: Q92249
Secondary accession number(s): Q7RVD7, Q9C2P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 30, 2003
Last modified: April 29, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.