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P09102

- PDIA1_CHICK

UniProt

P09102 - PDIA1_CHICK

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (16 May 2003)
      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). Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei58 – 581NucleophileBy similarity
    Sitei59 – 591Contributes to redox potential valueBy similarity
    Sitei60 – 601Contributes to redox potential valueBy similarity
    Active sitei61 – 611NucleophileBy similarity
    Sitei125 – 1251Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei402 – 4021NucleophileBy similarity
    Sitei403 – 4031Contributes to redox potential valueBy similarity
    Sitei404 – 4041Contributes to redox potential valueBy similarity
    Active sitei405 – 4051NucleophileBy similarity
    Sitei466 – 4661Lowers 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

    Enzyme and pathway databases

    SABIO-RKP09102.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Alternative name(s):
    Cellular thyroid hormone-binding protein
    Prolyl 4-hydroxylase subunit beta
    Retina cognin
    Short name:
    R-cognin
    Gene namesi
    Name:P4HB
    Synonyms:PDI, PDIA1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. 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. 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 – 22221 PublicationAdd
    BLAST
    Chaini23 – 515493Protein disulfide-isomerase1 PublicationPRO_0000034200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotation
    Disulfide bondi402 ↔ 405Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP09102.
    PRIDEiP09102.

    Interactioni

    Subunit structurei

    Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase. Stabilizes this enzyme and retains it in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000011689.

    Structurei

    3D structure databases

    ProteinModelPortaliP09102.
    SMRiP09102. Positions 26-362, 373-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 139117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 480130Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi512 – 5154Prevents secretion from ER

    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.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP09102.
    KOiK09580.
    PhylomeDBiP09102.

    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.

    P09102-1 [UniParc]FASTAAdd to Basket

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    MAVVRVRAIV ALLCLVAALG LAEPLEEEDG VLVLRAANFE QALAAHRHLL    50
    VEFYAPWCGH CKALAPEYAK AAAQLKAEGS EIRLAKVDAT EEAELAQQFG 100
    VRGYPTIKFF RNGDKAAPRE YTAGREADDI VSWLKKRTGP AATTLTDAAA 150
    AETLVDSSEV VVIGFFKDVT SDAAKEFLLA AESVDDIPFG ISSSADVFSK 200
    YQLSQDGVVL FKKFDEGRNN FEGDLTKDNL LNFIKSNQLP LVIEFTEQTA 250
    PKIFGGEIKT HILLFLPKSV SDYEGKLDNF KTAAGNFKGK ILFIFIDSDH 300
    SDNQRILEFF GLKKEECPAV RLITLEEEMT KYKPESDDLT ADKIKEFCNK 350
    FLEGKIKPHL MSQDLPEDWD KQPVKVLVGK NFEEVAFDEN KNVFVEFYAP 400
    WCGHCKQLAP IWDKLGETYR DHENIVIAKM DSTANEVEAV KIHSFPTLKF 450
    FPAGSGRNVI DYNGERTLEG FKKFLESGGQ DGAAADDDLE DLETDEETDL 500
    EEGDDDEQKI QKDEL 515
    Length:515
    Mass (Da):57,410
    Last modified:May 16, 2003 - v3
    Checksum:iE7CC978A5109C2CE
    GO

    Sequence cautioni

    The sequence AAA49054.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231E → Q1 PublicationCurated
    Sequence conflicti23 – 231E → Q(PubMed:2852147)Curated
    Sequence conflicti94 – 952EL → DV(PubMed:2852147)Curated
    Sequence conflicti359 – 3591H → Q(PubMed:2852147)Curated
    Sequence conflicti447 – 4471T → M in CAB57801. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11147 mRNA. Translation: AAA49054.2. Different initiation.
    X13110 mRNA. Translation: CAA31502.1.
    X06768 Genomic DNA. Translation: CAB57801.1.
    PIRiS02084. ISCHSS.
    RefSeqiNP_001185639.1. NM_001198710.1.
    UniGeneiGga.4976.

    Genome annotation databases

    GeneIDi374091.
    KEGGigga:374091.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11147 mRNA. Translation: AAA49054.2 . Different initiation.
    X13110 mRNA. Translation: CAA31502.1 .
    X06768 Genomic DNA. Translation: CAB57801.1 .
    PIRi S02084. ISCHSS.
    RefSeqi NP_001185639.1. NM_001198710.1.
    UniGenei Gga.4976.

    3D structure databases

    ProteinModelPortali P09102.
    SMRi P09102. Positions 26-362, 373-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000011689.

    Proteomic databases

    PaxDbi P09102.
    PRIDEi P09102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 374091.
    KEGGi gga:374091.

    Organism-specific databases

    CTDi 5034.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P09102.
    KOi K09580.
    PhylomeDBi P09102.

    Enzyme and pathway databases

    SABIO-RK P09102.

    Miscellaneous databases

    NextBioi 20813610.
    PROi P09102.

    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. Hausman R.E.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 315; 356; 488; 491-493 AND 497.
    2. "cDNA for R-cognin: homology with a multifunctional protein."
      Krishna Rao A.S., Hausman R.E.
      Proc. Natl. Acad. Sci. U.S.A. 90:2950-2954(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-515.
      Tissue: Retina.
    3. "Structure of the gene encoding the beta-subunit of chicken prolyl 4-hydroxylase."
      Nakazawa M., Aida T., Everson W.V., Gonda M.A., Hughes S.H., Kao W.W.
      Gene 71:451-460(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-129; 163-172; 209-218; 244-253; 286-295; 353-463 AND 483-515.
    4. "Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species."
      Parkkonen T., Kivirikko K.Z., Pihlajaniemi T.
      Biochem. J. 256:1005-1011(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-515, PROTEIN SEQUENCE OF 23-31 AND 95-109.
    5. Bassuk J.A.
      Submitted (FEB-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-459.

    Entry informationi

    Entry nameiPDIA1_CHICK
    AccessioniPrimary (citable) accession number: P09102
    Secondary accession number(s): Q90969
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3