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Q12730

- PDI_ASPNG

UniProt

Q12730 - PDI_ASPNG

Protein

Protein disulfide-isomerase

Gene

pdiA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541NucleophileBy similarity
    Sitei55 – 551Contributes to redox potential valueBy similarity
    Sitei56 – 561Contributes to redox potential valueBy similarity
    Active sitei57 – 571NucleophileBy similarity
    Sitei117 – 1171Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei389 – 3891NucleophileBy similarity
    Sitei390 – 3901Contributes to redox potential valueBy similarity
    Sitei391 – 3911Contributes to redox potential valueBy similarity
    Active sitei392 – 3921NucleophileBy similarity
    Sitei456 – 4561Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein disulfide isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Gene namesi
    Name:pdiA
    Synonyms:pdi1
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 515495Protein disulfide-isomerasePRO_0000034213Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 57Redox-activePROSITE-ProRule annotation
    Disulfide bondi389 ↔ 392Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ12730.
    SMRiQ12730. Positions 231-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 132112Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 470132Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi512 – 5154Prevents 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.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR001393. Calsequestrin.
    IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    PRINTSiPR00312. CALSEQUESTRN.
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 1 hit.
    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.

    Q12730-1 [UniParc]FASTAAdd to Basket

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    MRSFAPWLVS LLGASAVVAA ADTESDVISL DQDTFESFMN EHGLVLAEFF    50
    APWCGHCKAL APKYEEAATE LKAKNIPLVK VDCTAEEDLC RSQGVEGYPT 100
    LKIFRGVDSS KPYQGARQTE SIVSYMIKQS LPAVSSVNEE NLEEIKTMDK 150
    IVVIGYIPSD DQETYQAFEK YAESQRDNYL FAATDDAAIA KSEGVEQPSI 200
    VLYKDFDEKK AVYDGEIEQE AIHSWVKSAS TPLVGEIGPE TYSGYIGAGV 250
    PLAYIFAETK EEREKYTEDF KPIAQKHKGA INIATIDAKM FGAHAGNLNL 300
    DSQKFPAFAI QDPAKNAKYP YDQAKELNAD EVEKFIQDVL DGKVEPSIKS 350
    EPVPESQEGP VTVVVAHSYK DLVIDNDKDV LLEFYAPWCG HCKALAPKYD 400
    ELAALYADHP DLAAKVTIAK IDATANDVPD PITGFPTLRL YPAGAKDSPI 450
    EYSGSRTVED LANFVKENGK HNVDALNVAS EETQEGGDVT EAAPSATEAE 500
    TPAATDDEKA EHDEL 515
    Length:515
    Mass (Da):56,292
    Last modified:November 1, 1997 - v1
    Checksum:i2B0058B788400AD9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98797 Genomic DNA. Translation: CAA67332.1.
    X89449 mRNA. Translation: CAA61619.1.
    PIRiS57942.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98797 Genomic DNA. Translation: CAA67332.1 .
    X89449 mRNA. Translation: CAA61619.1 .
    PIRi S57942.

    3D structure databases

    ProteinModelPortali Q12730.
    SMRi Q12730. Positions 231-471.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0526.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR001393. Calsequestrin.
    IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    PRINTSi PR00312. CALSEQUESTRN.
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 1 hit.
    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 gene encoding protein disulphide isomerase, pdiA, from Aspergillus niger."
      Ngiam C., Jeenes D.J., Archer D.B.
      Curr. Genet. 31:133-138(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
    2. Malpricht S.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

    Entry informationi

    Entry nameiPDI_ASPNG
    AccessioniPrimary (citable) accession number: Q12730
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3