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P55059

- PDI_HUMIN

UniProt

P55059 - PDI_HUMIN

Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 sitei50 – 501NucleophileBy similarity
    Sitei51 – 511Contributes to redox potential valueBy similarity
    Sitei52 – 521Contributes to redox potential valueBy similarity
    Active sitei53 – 531NucleophileBy similarity
    Sitei113 – 1131Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei385 – 3851NucleophileBy similarity
    Sitei386 – 3861Contributes to redox potential valueBy similarity
    Sitei387 – 3871Contributes to redox potential valueBy similarity
    Active sitei388 – 3881NucleophileBy similarity
    Sitei451 – 4511Lowers 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

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    OrganismiHumicola insolens (Soft-rot fungus)
    Taxonomic identifieri34413 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    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 – 505485Protein disulfide-isomerasePRO_0000034215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 53Redox-activePROSITE-ProRule annotation
    Disulfide bondi385 ↔ 388Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP55059.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi230 – 2323
    Helixi235 – 2439
    Beta strandi248 – 2525
    Beta strandi256 – 2583
    Helixi259 – 27113
    Turni274 – 2763
    Beta strandi277 – 2826
    Turni284 – 2874
    Helixi288 – 2903
    Turni291 – 2955
    Beta strandi298 – 30710
    Turni309 – 3113
    Beta strandi314 – 3163
    Beta strandi319 – 3213
    Helixi325 – 33612
    Beta strandi356 – 3594
    Turni362 – 3676
    Beta strandi368 – 3703
    Beta strandi372 – 3743
    Beta strandi376 – 3816
    Helixi388 – 40215
    Turni405 – 4095
    Beta strandi410 – 4178
    Turni418 – 4203
    Beta strandi428 – 4369
    Beta strandi445 – 4484
    Helixi453 – 46210
    Beta strandi463 – 4664

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJJNMR-A354-469[»]
    2DJKNMR-A228-355[»]
    2KP1NMR-A354-469[»]
    2KP2NMR-A228-355[»]
    ProteinModelPortaliP55059.
    SMRiP55059. Positions 226-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55059.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 128108Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 465131Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi502 – 5054Prevents 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

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. 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.

    P55059-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHKAQKFALG LLAAAAVATA SDVVQLKKDT FDDFIKTNDL VLAEFFAPWC    50
    GHCKALAPEY EEAATTLKEK NIKLAKVDCT EETDLCQQHG VEGYPTLKVF 100
    RGLDNVSPYK GQRKAAAITS YMIKQSLPAV SEVTKDNLEE FKKADKAVLV 150
    AYVDASDKAS SEVFTQVAEK LRDNYPFGSS SDAALAEAEG VKAPAIVLYK 200
    DFDEGKAVFS EKFEVEAIEK FAKTGATPLI GEIGPETYSD YMSAGIPLAY 250
    IFAETAEERK ELSDKLKPIA EAQRGVINFG TIDAKAFGAH AGNLNLKTDK 300
    FPAFAIQEVA KNQKFPFDQE KEITFEAIKA FVDDFVAGKI EPSIKSEPIP 350
    EKQEGPVTVV VAKNYNEIVL DDTKDVLIEF YAPWCGHCKA LAPKYEELGA 400
    LYAKSEFKDR VVIAKVDATA NDVPDEIQGF PTIKLYPAGA KGQPVTYSGS 450
    RTVEDLIKFI AENGKYKAAI SEDAEETSSA TETTTETATK SEEAAKETAT 500
    EHDEL 505
    Length:505
    Mass (Da):55,114
    Last modified:October 1, 1996 - v1
    Checksum:i27E7C0D1A61B5F95
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74296 mRNA. Translation: AAC60578.1.
    PIRiJC2291.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74296 mRNA. Translation: AAC60578.1 .
    PIRi JC2291.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DJJ NMR - A 354-469 [» ]
    2DJK NMR - A 228-355 [» ]
    2KP1 NMR - A 354-469 [» ]
    2KP2 NMR - A 228-355 [» ]
    ProteinModelPortali P55059.
    SMRi P55059. Positions 226-469.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P55059.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P55059.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi 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 ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    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. "Molecular cloning of a fungal cDNA encoding protein disulfide isomerase."
      Kajino T., Sarai K., Imaeda T., Idekoba C., Asami O., Yamada Y., Hirai M., Udaka S.
      Biosci. Biotechnol. Biochem. 58:1424-1429(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: KASI.

    Entry informationi

    Entry nameiPDI_HUMIN
    AccessioniPrimary (citable) accession number: P55059
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3