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Q43116

- PDI_RICCO

UniProt

Q43116 - PDI_RICCO

Protein

Protein disulfide-isomerase

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Nov 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 sitei61 – 611NucleophileBy similarity
    Sitei62 – 621Contributes to redox potential valueBy similarity
    Sitei63 – 631Contributes to redox potential valueBy similarity
    Active sitei64 – 641NucleophileBy similarity
    Sitei129 – 1291Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei406 – 4061NucleophileBy similarity
    Sitei407 – 4071Contributes to redox potential valueBy similarity
    Sitei408 – 4081Contributes to redox potential valueBy similarity
    Active sitei409 – 4091NucleophileBy similarity
    Sitei470 – 4701Lowers 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
    OrganismiRicinus communis (Castor bean)
    Taxonomic identifieri3988 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 498475Protein disulfide-isomerasePRO_0000034211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi61 ↔ 64Redox-activePROSITE-ProRule annotation
    Disulfide bondi406 ↔ 409Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ43116.
    ProMEXiQ43116.

    Structurei

    3D structure databases

    ProteinModelPortaliQ43116.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 143120Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 484146Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi495 – 4984Prevents 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.

    Q43116-1 [UniParc]FASTAAdd to Basket

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    MASFRGSIWY CIFVLSLIAV AISAAESEEE QSSVLTLDST NFTDTISKHD    50
    FIVVEFYAPW CGHCKKLRPE YEKAASILKS HDIPVVLAKV DANEEANKEL 100
    ATQYDIKGFP TLKILRNGGK SIQEYKGPRE ADGIAEYLKK QSGPASVEIK 150
    STEAANTFIG DKKIFIVGVF PKFSGEEYEN YMSVADKLRS DYEFGHTLDA 200
    KHLPQGESSV TGPVVRLFKP FDELFVDFKD FNVDALEKFV EESSMPVVTV 250
    FNSDPSNHPF VIKFFNSPDA KAMLFMNFNG EAADSIKSKY QEVAHQFKGE 300
    GIILLLGDVE ASQGAFQYFG LKEDQVPLII IQTNDGQKYL KANLEPDHIA 350
    PWVKAYKEGK VQAYRKSEPI PEVNNEPVKV VVADTLQDIV FNSGKNVLLE 400
    FYAPWCGHCK QLAPILDEVA VSYKSDADIV IAKLDATAND IPSDTFDVRG 450
    YPTVYFRSAS GKVEQYDGDR TKDDIISFIE KNRDKAAQQE SANGKDEL 498
    Length:498
    Mass (Da):55,561
    Last modified:November 1, 1996 - v1
    Checksum:iD556492D78F955D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41385 mRNA. Translation: AAB05641.1.
    PIRiS62626.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41385 mRNA. Translation: AAB05641.1 .
    PIRi S62626.

    3D structure databases

    ProteinModelPortali Q43116.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q43116.
    ProMEXi Q43116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 characterisation of plant endoplasmic reticulum. Identification of protein disulfide-isomerase as the major reticuloplasmin."
      Coughlan S.J., Hastings C., Winfrey R.J.
      Eur. J. Biochem. 235:215-224(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Hale.

    Entry informationi

    Entry nameiPDI_RICCO
    AccessioniPrimary (citable) accession number: Q43116
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3