Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q92249

- ERP38_NEUCR

UniProt

Q92249 - ERP38_NEUCR

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: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. response to stress Source: UniProtKB-KW

    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: Chromosome 2, Linkage Group V

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    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.
    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

    MVLLKSLVVA SLAAAVAAKS AVLDLIPSNF DDVVLKSGKP TLVEFFAPWC    50
    GHCKNLAPVY EELATALEYA KDKVQIAKVD ADAERALGKR FGVQGFPTLK 100
    FFDGKSEQPV DYKGGRDLDS LSNFIAEKTG VKARKKGSAP SLVNILNDAT 150
    IKGAIGGDKN VLVAFTAPWC GHCKNLAPTW EKLAATFASD PEITIAKVDA 200
    DAPTGKKSAA EYGVSGFPTI KFFPKGSTTP EDYNGGRSEA DLVKFLNEKA 250
    GTHRTPGGGL DTVAGTIAAL DEIVAKYTGG ASLAEVAEEA KEAVKSLKNS 300
    AELKYADYYL RVLDKLSKSE GYATKEFARL EGILKKGGLA PAKVDELTVK 350
    VNVLRKFVEK AAEEAKEEL 369
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07562 mRNA. Translation: CAA68847.1.
    AL513467 Genomic DNA. Translation: CAC28831.1.
    CM002240 Genomic DNA. Translation: EAA32279.1.
    PIRiT47259.
    RefSeqiXP_961515.1. XM_956422.2.
    UniGeneiNcr.7762.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07562 mRNA. Translation: CAA68847.1 .
    AL513467 Genomic DNA. Translation: CAC28831.1 .
    CM002240 Genomic DNA. Translation: EAA32279.1 .
    PIRi T47259.
    RefSeqi XP_961515.1. XM_956422.2.
    UniGenei Ncr.7762.

    3D structure databases

    ProteinModelPortali Q92249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q92249. 4 interactions.
    MINTi MINT-4653714.
    STRINGi 5141.NCU03739.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000003391 ; EFNCRP00000003391 ; EFNCRG00000003387 .
    GeneIDi 3877590.
    KEGGi ncr:NCU03739.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000176389.
    KOi K09584.
    OMAi YKSGRDL.
    OrthoDBi EOG71CFZN.

    Family and domain databases

    Gene3Di 1.20.1150.12. 1 hit.
    3.40.30.10. 2 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR011679. ER_p29_C.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF07749. ERp29. 1 hit.
    PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47933. SSF47933. 1 hit.
    SSF52833. SSF52833. 2 hits.
    TIGRFAMsi TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 122 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