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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)DescriptionActionsGraphical viewLength
Active sitei50NucleophileBy similarity1
Sitei51Contributes to redox potential valueBy similarity1
Sitei52Contributes to redox potential valueBy similarity1
Active sitei53NucleophileBy similarity1
Sitei116Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei170NucleophileBy similarity1
Sitei171Contributes to redox potential valueBy similarity1
Sitei172Contributes to redox potential valueBy similarity1
Active sitei173NucleophileBy similarity1
Sitei237Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001805 Componenti: Chromosome 2, Linkage Group V

Organism-specific databases

EuPathDBiFungiDB:NCU03739.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000003424419 – 369Protein disulfide-isomerase erp38Add BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.
MINTiMINT-4653714.

Structurei

3D structure databases

ProteinModelPortaliQ92249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 130Thioredoxin 1PROSITE-ProRule annotationAdd BLAST112
Domaini131 – 251Thioredoxin 2PROSITE-ProRule annotationAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi366 – 369Prevents secretion from ERPROSITE-ProRule annotation4

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

HOGENOMiHOG000176389.
InParanoidiQ92249.
KOiK09584.
OMAiEYYVKVF.
OrthoDBiEOG092C4AE3.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti154A → P in CAA68847 (PubMed:9256071).Curated1

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.

Genome annotation databases

EnsemblFungiiEAA32279; EAA32279; NCU03739.
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.

3D structure databases

ProteinModelPortaliQ92249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ92249. 4 interactors.
MINTiMINT-4653714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA32279; EAA32279; NCU03739.
GeneIDi3877590.
KEGGincr:NCU03739.

Organism-specific databases

EuPathDBiFungiDB:NCU03739.

Phylogenomic databases

HOGENOMiHOG000176389.
InParanoidiQ92249.
KOiK09584.
OMAiEYYVKVF.
OrthoDBiEOG092C4AE3.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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...

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: November 2, 2016
This is version 134 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

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 one 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.