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Q8R4U2

- PDIA1_CRIGR

UniProt

Q8R4U2 - PDIA1_CRIGR

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei55 – 551NucleophileBy similarity
    Sitei56 – 561Contributes to redox potential valueBy similarity
    Sitei57 – 571Contributes to redox potential valueBy similarity
    Active sitei58 – 581NucleophileBy similarity
    Sitei122 – 1221Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei399 – 3991NucleophileBy similarity
    Sitei400 – 4001Contributes to redox potential valueBy similarity
    Sitei401 – 4011Contributes to redox potential valueBy similarity
    Active sitei402 – 4021NucleophileBy similarity
    Sitei463 – 4631Lowers 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

    Chaperone, Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Alternative name(s):
    Prolyl 4-hydroxylase subunit beta
    p58
    Gene namesi
    Name:P4HB
    Synonyms:PDIA1
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity. Cell membrane Curated; Peripheral membrane protein Curated
    Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. melanosome Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 509490Protein disulfide-isomerasePRO_0000034194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
    Modified residuei202 – 2021N6-acetyllysineBy similarity
    Modified residuei224 – 2241N6-succinyllysineBy similarity
    Modified residuei273 – 2731N6-succinyllysineBy similarity
    Disulfide bondi399 ↔ 402Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PRIDEiQ8R4U2.

    Interactioni

    Subunit structurei

    Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-4997811.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R4U2.
    SMRiQ8R4U2. Positions 20-359, 370-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 136117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 477143Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi506 – 5094Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi482 – 4876Poly-Asp

    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

    HOVERGENiHBG005920.
    KOiK09580.

    Family and domain databases

    Gene3Di3.40.30.10. 4 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.

    Q8R4U2-1 [UniParc]FASTAAdd to Basket

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    MLSRSLLCLA LAWVARVGAD APEEEDNVLV LKKSNFAEAL AAHNYLLVEF    50
    YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
    YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAET 150
    LIDSSEVAVI GFFKDVESDS AKQFLLAAEA VDDIPFGITS NSGVFSKYQL 200
    DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
    FGGEIKTHIL LFLPKSVSDY DGKLGNFKKA AEGFKGKILF IFIDSDHTDN 300
    QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE 350
    GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG 400
    HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA 450
    TADRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDVDLEE ALEPDMEEDD 500
    DQKAVKDEL 509
    Length:509
    Mass (Da):57,010
    Last modified:June 1, 2002 - v1
    Checksum:i9B9B7513DE918194
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF364317 mRNA. Translation: AAM00284.1.
    RefSeqiNP_001233622.1. NM_001246693.1.

    Genome annotation databases

    GeneIDi100689433.
    KEGGicge:100689433.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF364317 mRNA. Translation: AAM00284.1 .
    RefSeqi NP_001233622.1. NM_001246693.1.

    3D structure databases

    ProteinModelPortali Q8R4U2.
    SMRi Q8R4U2. Positions 20-359, 370-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4997811.

    Proteomic databases

    PRIDEi Q8R4U2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100689433.
    KEGGi cge:100689433.

    Organism-specific databases

    CTDi 5034.

    Phylogenomic databases

    HOVERGENi HBG005920.
    KOi K09580.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 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. "Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine."
      Cai T.-Q., Guo Q., Wong B., Milot D., Zhang L., Wright S.D.
      Biochim. Biophys. Acta 1581:100-108(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Small intestine.

    Entry informationi

    Entry nameiPDIA1_CRIGR
    AccessioniPrimary (citable) accession number: Q8R4U2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3