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P05307

- PDIA1_BOVIN

UniProt

P05307 - PDIA1_BOVIN

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      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. procollagen-proline 4-dioxygenase activity Source: AgBase
    2. protein disulfide isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: AgBase

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15199.

    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
    p55
    Gene namesi
    Name:P4HB
    Synonyms:PDIA1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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 Source: AgBase
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. melanosome Source: UniProtKB-SubCell
    4. 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 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 510490Protein disulfide-isomerasePRO_0000034193Add
    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

    PaxDbiP05307.
    PRIDEiP05307.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP05307.
    SMRiP05307. Positions 21-359, 370-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 136110Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 477127Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi507 – 5104Prevents 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.
    InParanoidiP05307.
    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.

    P05307-1 [UniParc]FASTAAdd to Basket

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    MLRRALLCLA LTALFRAGAG APDEEDHVLV LHKGNFDEAL AAHKYLLVEF    50
    YAPWCGHCKA LAPEYAKAAG KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
    YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAS TLSDGAAAEA 150
    LVESSEVAVI GFFKDMESDS AKQFFLAAEV IDDIPFGITS NSDVFSKYQL 200
    DKDGVVLFKK FDEGRNNFEG EVTKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
    FGGEIKTHIL LFLPKSVSDY EGKLSNFKKA AESFKGKILF IFIDSDHTDN 300
    QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE 350
    GKIKPHLMSQ ELPDDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG 400
    HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAVKVH SFPTLKFFPA 450
    SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDLEDLE EAEEPDLEED 500
    DDQKAVKDEL 510
    Length:510
    Mass (Da):57,266
    Last modified:November 1, 1988 - v1
    Checksum:iF19BEC892E03C4CC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17596 mRNA. Translation: AAA30690.1.
    PIRiA26829. ISBOSS.
    RefSeqiNP_776560.1. NM_174135.3.
    UniGeneiBt.106831.

    Genome annotation databases

    GeneIDi281373.
    KEGGibta:281373.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17596 mRNA. Translation: AAA30690.1 .
    PIRi A26829. ISBOSS.
    RefSeqi NP_776560.1. NM_174135.3.
    UniGenei Bt.106831.

    3D structure databases

    ProteinModelPortali P05307.
    SMRi P05307. Positions 21-359, 370-473.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P05307.
    PRIDEi P05307.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281373.
    KEGGi bta:281373.

    Organism-specific databases

    CTDi 5034.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P05307.
    KOi K09580.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-15199.

    Miscellaneous databases

    NextBioi 20805377.

    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. "Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase."
      Yamauchi K., Yamamoto T., Hayashi H., Koya S., Takikawa H., Toyoshima K., Horiuchi R.
      Biochem. Biophys. Res. Commun. 146:1485-1492(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex."
      Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J.
      J. Biol. Chem. 265:9800-9807(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-45, INTERACTION WITH MTTP.
    3. Parkinson D.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-32.

    Entry informationi

    Entry nameiPDIA1_BOVIN
    AccessioniPrimary (citable) accession number: P05307
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 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