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P04785

- PDIA1_RAT

UniProt

P04785 - PDIA1_RAT

Protein

Protein disulfide-isomerase

Gene

P4hb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      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. enzyme binding Source: RGD
    2. procollagen-proline 4-dioxygenase activity Source: Ensembl
    3. protein disulfide isomerase activity Source: RGD
    4. protein heterodimerization activity Source: RGD

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to hypoxia Source: Ensembl
    3. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: Ensembl
    4. protein folding Source: GOC
    5. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: RefGenome
    6. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_213899. Detoxification of Reactive Oxygen Species.

    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
    Gene namesi
    Name:P4hb
    Synonyms:Pdia1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 10

    Organism-specific databases

    RGDi3244. P4hb.

    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: RefGenome
    2. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. melanosome Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell
    6. procollagen-proline 4-dioxygenase complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 509490Protein disulfide-isomerasePRO_0000034199Add
    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

    PaxDbiP04785.
    PRIDEiP04785.

    PTM databases

    PhosphoSiteiP04785.

    Expressioni

    Gene expression databases

    GenevestigatoriP04785.

    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

    BioGridi247538. 1 interaction.
    IntActiP04785. 3 interactions.
    MINTiMINT-4996344.
    STRINGi10116.ENSRNOP00000051841.

    Structurei

    3D structure databases

    ProteinModelPortaliP04785.
    SMRiP04785. 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 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.
    GeneTreeiENSGT00740000115202.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP04785.
    KOiK09580.
    OMAiCHHFLEG.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiP04785.
    TreeFamiTF106381.

    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.

    P04785-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFAEAL AAHNYLLVEF    50
    YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
    YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAES 150
    LVDSSEVTVI GFFKDAGSDS AKQFLLAAEA VDDIPFGITS NSDVFSKYQL 200
    DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
    FGGEIKTHIL LFLPKSVSDY DGKLSNFKKA AEGFKGKILF IFIDSDHTDN 300
    QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITQFCHHFLE 350
    GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG 400
    HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAVKVH SFPTLKFFPA 450
    SADRTVIDYN GERTLDGFKK FLESGGQDGA GDNDDLDLEE ALEPDMEEDD 500
    DQKAVKDEL 509
    Length:509
    Mass (Da):56,951
    Last modified:October 1, 1989 - v2
    Checksum:i3056107F5E8B1B54
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 402AL → P in CAA26675. (PubMed:3840230)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21018 mRNA. Translation: AAA40620.1.
    BC061857 mRNA. Translation: AAH61857.1.
    X02918 mRNA. Translation: CAA26675.1.
    M21476 mRNA. Translation: AAA40619.1.
    PIRiA24595. ISRTSS.
    S68028.
    RefSeqiNP_037130.1. NM_012998.1.
    UniGeneiRn.4234.

    Genome annotation databases

    EnsembliENSRNOT00000054958; ENSRNOP00000051841; ENSRNOG00000036689.
    GeneIDi25506.
    KEGGirno:25506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21018 mRNA. Translation: AAA40620.1 .
    BC061857 mRNA. Translation: AAH61857.1 .
    X02918 mRNA. Translation: CAA26675.1 .
    M21476 mRNA. Translation: AAA40619.1 .
    PIRi A24595. ISRTSS.
    S68028.
    RefSeqi NP_037130.1. NM_012998.1.
    UniGenei Rn.4234.

    3D structure databases

    ProteinModelPortali P04785.
    SMRi P04785. Positions 20-359, 370-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247538. 1 interaction.
    IntActi P04785. 3 interactions.
    MINTi MINT-4996344.
    STRINGi 10116.ENSRNOP00000051841.

    PTM databases

    PhosphoSitei P04785.

    Proteomic databases

    PaxDbi P04785.
    PRIDEi P04785.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000054958 ; ENSRNOP00000051841 ; ENSRNOG00000036689 .
    GeneIDi 25506.
    KEGGi rno:25506.

    Organism-specific databases

    CTDi 5034.
    RGDi 3244. P4hb.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00740000115202.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P04785.
    KOi K09580.
    OMAi CHHFLEG.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi P04785.
    TreeFami TF106381.

    Enzyme and pathway databases

    Reactomei REACT_198584. Collagen biosynthesis and modifying enzymes.
    REACT_213899. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    NextBioi 606925.
    PROi P04785.

    Gene expression databases

    Genevestigatori P04785.

    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 protein disulphide isomerase and implications of its relationship to thioredoxin."
      Edman J.C., Ellis L., Blacher R.W., Roth R.A., Rutter W.J.
      Nature 317:267-270(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    3. "Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats."
      Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T.
      Biochim. Biophys. Acta 1158:339-344(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-34.
      Strain: LEC.
      Tissue: Liver.
    4. "Nucleotide sequence of rat liver iodothyronine 5'-monodeiodinase (5' MD): its identity with the protein disulfide isomerase."
      Boado R.J., Campbell D.A., Chopra I.J.
      Biochem. Biophys. Res. Commun. 155:1297-1304(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-509.
      Tissue: Liver.
    5. "Enzyme binding-inhibiting assay for iodothyronine 5'-monodeiodinase (5'-MD) and its application to isolation of complementary deoxyribonucleic acid clones for the 5'-MD in rat liver."
      Boado R.J., Chopra I.J., Flink I.L., Campbell D.A.
      Endocrinology 123:1264-1273(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-394.
      Tissue: Liver.
    6. Lubec G., Afjehi-Sadat L., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 233-249; 288-302 AND 341-352, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.
    7. "Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites."
      Noiva R., Freedman R.B., Lennarz W.J.
      J. Biol. Chem. 268:19210-19217(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 471-494.
    8. "Rat liver type I iodothyronine deiodinase is not identical to protein disulfide isomerase."
      Schoenmakers C.H.H., Pigmans I.G.A.J., Hawkins H.C., Freedman R.B., Visser T.J.
      Biochem. Biophys. Res. Commun. 162:857-868(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT PROTEIN IS NOT IDENTICAL TO THYROXINE DEIODINASE.

    Entry informationi

    Entry nameiPDIA1_RAT
    AccessioniPrimary (citable) accession number: P04785
    Secondary accession number(s): P13700
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally (PubMed:8251535 and PubMed:3178809) thought to be identical to thyroxine deiodinase but this was later shown to be incorrect.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3